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https://en.wikipedia.org/wiki/%28S%29-tetrahydroprotoberberine%20N-methyltransferase | In enzymology, a (S)-tetrahydroprotoberberine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + (S)-7,8,13,14-tetrahydroprotoberberine S-adenosyl-L-homocysteine + cis-N-methyl-(S)-7,8,13,14-tetrahydroprotoberberine
Thus, the two substrates of this enzyme are S-adenosyl methionine and (S)-7,8,13,14-tetrahydroprotoberberine, whereas its two products are S-adenosylhomocysteine and cis-N-methyl-(S)-7,8,13,14-tetrahydroprotoberberine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(S)-7,8,13,14-tetrahydroprotoberberine cis-N-methyltransferase. This enzyme is also called tetrahydroprotoberberine cis-N-methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tabersonine%2016-O-methyltransferase | In enzymology, a tabersonine 16-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 16-hydroxytabersonine S-adenosyl-L-homocysteine + 16-methoxytabersonine
Thus, the two substrates of this enzyme are S-adenosyl methionine and 16-hydroxytabersonine, whereas its two products are S-adenosylhomocysteine and 16-methoxytabersonine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:16-hydroxytabersonine 16-O-methyltransferase. Other names in common use include 11-demethyl-17-deacetylvindoline 11-methyltransferase, 11-O-demethyl-17-O-deacetylvindoline O-methyltransferase, S-adenosyl-L-methionine:11-O-demethyl-17-O-deacetylvindoline, and 11-O-methyltransferase. This enzyme participates in terpene indole and ipecac alkaloid biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tetrahydrocolumbamine%202-O-methyltransferase | In enzymology, a tetrahydrocolumbamine 2-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 5,8,13,13a-tetrahydrocolumbamine S-adenosyl-L-homocysteine + tetrahydropalmatine
Thus, the two substrates of this enzyme are S-adenosyl methionine and 5,8,13,13a-tetrahydrocolumbamine, whereas its two products are S-adenosylhomocysteine and tetrahydropalmatine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:5,8,13,13a-tetrahydrocolumbamine 2-O-methyltransferase. This enzyme is also called tetrahydrocolumbamine methyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tetrahydromethanopterin%20S-methyltransferase | In enzymology, a tetrahydromethanopterin S-methyltransferase () is an enzyme that catalyzes the chemical reaction
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate 5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
Thus, the two substrates of this enzyme are 5-methyl-5,6,7,8-tetrahydromethanopterin and 2-mercaptoethanesulfonate (coenzyme M), whereas its two products are 5,6,7,8-tetrahydromethanopterin and 2-(methylthio)ethanesulfonate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is 5-methyl-5,6,7,8-tetrahydromethanopterin:2-mercaptoethanesulfonate 2-methyltransferase. This enzyme is also called tetrahydromethanopterin methyltransferase. This enzyme participates in folate biosynthesis.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Theobromine%20synthase | In enzymology, a theobromine synthase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + 7-methylxanthine S-adenosyl-L-homocysteine + 3,7-dimethylxanthine
Thus, the two substrates of this enzyme are S-adenosyl methionine and 7-methylxanthine, whereas its two products are S-adenosylhomocysteine and 3,7-dimethylxanthine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:7-methylxanthine N3-methyltransferase. Other names in common use include monomethylxanthine methyltransferase, MXMT, CTS1, CTS2, and S-adenosyl-L-methionine:7-methylxanthine 3-N-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thetin%E2%80%94homocysteine%20S-methyltransferase | In enzymology, a thetin-homocysteine S-methyltransferase () is an enzyme that catalyzes the chemical reaction
dimethylsulfonioacetate + L-homocysteine S-methylthioglycolate + L-methionine
Thus, the two substrates of this enzyme are dimethylsulfonioacetic acid and L-homocysteine, whereas its two products are S-methylthioglycolic acid and L-methionine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is dimethylsulfonioacetic acid:L-homocysteine S-methyltransferase. Other names in common use include dimethylthetin-homocysteine methyltransferase, and thetin-homocysteine methylpherase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thioether%20S-methyltransferase | In enzymology, a thioether S-methyltransferase () is an enzyme that catalyzes the chemical reaction.
S-adenosyl-L-methionine + dimethyl sulfide S-adenosyl-L-homocysteine + trimethylsulfonium
Thus, the two substrates of this enzyme are S-adenosyl methionine and dimethyl sulfide, whereas its two products are S-adenosylhomocysteine and trimethylsulfonium.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:dimethyl-sulfide S-methyltransferase. Other names in common use include S-adenosyl-L-methionine:thioether S-methyltransferase, and thioether methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiol%20S-methyltransferase | In enzymology, a thiol S-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + a thiol S-adenosyl-L-homocysteine + a thioether
Thus, the two substrates of this enzyme are S-adenosyl methionine and thiol, whereas its two products are S-adenosylhomocysteine and thioether.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:thiol S-methyltransferase. Other names in common use include S-methyltransferase, thiol methyltransferase, and TMT. This enzyme participates in selenoamino acid metabolism.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thymidylate%20synthase%20%28FAD%29 | In enzymology, a thymidylate synthase (FAD) () is an enzyme that catalyzes the chemical reaction
5,10-methylenetetrahydrofolate + dUMP + FADH2 dTMP + tetrahydrofolate + FAD
The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, dUMP, and FADH2, whereas its 3 products are dTMP, tetrahydrofolate, and FAD.
This enzyme belongs to the family of transferases, to be specific those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate,FADH2:dUMP C-methyltransferase. Other names in common use include Thy1, and ThyX. This enzyme participates in pyrimidine metabolism and one carbon pool by folate.
Most organisms, including humans, use the thyA- or TYMS-encoded classic thymidylate synthase whereas some bacteria use the similar flavin-dependent thymidylate synthase (FDTS) instead.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
See also
Thymidylate synthetase
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tocopherol%20O-methyltransferase | In enzymology, a tocopherol O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + gamma-tocopherol S-adenosyl-L-homocysteine + alpha-tocopherol
Thus, the two substrates of this enzyme are S-adenosyl methionine and gamma-tocopherol, whereas its two products are S-adenosylhomocysteine and alpha-tocopherol.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:gamma-tocopherol 5-O-methyltransferase. This enzyme is also called gamma-tocopherol methyltransferase. This enzyme participates in biosynthesis of steroids.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trans-aconitate%202-methyltransferase | In enzymology, a trans-aconitate 2-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + trans-aconitate S-adenosyl-L-homocysteine + (E)-3-(methoxycarbonyl)pent-2-enedioate
Thus, the two substrates of this enzyme are S-adenosyl methionine and trans-aconitate, whereas its two products are S-adenosylhomocysteine and (E)-3-(methoxycarbonyl)pent-2-enedioate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate 2'-O-methyltransferase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Trans-aconitate%203-methyltransferase | In enzymology, a trans-aconitate 3-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + trans-aconitate S-adenosyl-L-homocysteine + (E)-2-(methoxycarbonylmethyl)butenedioate
Thus, the two substrates of this enzyme are S-adenosyl methionine and trans-aconitate, whereas its two products are S-adenosylhomocysteine and (E)-2-(methoxycarbonylmethyl)butenedioate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(E)-prop-1-ene-1,2,3-tricarboxylate 3'-O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trimethylsulfonium%E2%80%94tetrahydrofolate%20N-methyltransferase | In enzymology, a trimethylsulfonium-tetrahydrofolate N-methyltransferase () is an enzyme that catalyzes the chemical reaction
trimethylsulfonium + tetrahydrofolate dimethylsulfide + 5-methyltetrahydrofolate
Thus, the two substrates of this enzyme are trimethylsulfonium and tetrahydrofolate, whereas its two products are dimethyl sulfide and 5-methyltetrahydrofolate.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is trimethylsulfonium:tetrahydrofolate N-methyltransferase. This enzyme is also called trimethylsulfonium-tetrahydrofolate methyltransferase. This enzyme participates in one carbon pool by folate.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/TRNA%20%285-methylaminomethyl-2-thiouridylate%29-methyltransferase | In enzymology, a tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing 5-methylaminomethyl-2-thiouridylic acid.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (5-methylaminomethyl-2-thio-uridylate)-methyltransferase. Other names in common use include transfer ribonucleate 5-methylaminomethyl-2-thiouridylate, 5-methyltransferase, and tRNA 5-methylaminomethyl-2-thiouridylate 5'-methyltransferase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/TRNA%20%28adenine-N1-%29-methyltransferase | In enzymology, a tRNA (adenine-N1-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing N1-methyladenine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing N1-methyladenine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (adenine-N1-)-methyltransferase. Other names in common use include transfer ribonucleate adenine 1-methyltransferase, transfer RNA (adenine-1) methyltransferase, 1-methyladenine transfer RNA methyltransferase, adenine-1-methylase, and S-adenosyl-L-methionine:tRNA (adenine-1-N-)-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Bipolar%20transistor%20biasing | Bipolar transistors must be properly biased to operate correctly. In circuits made with individual devices (discrete circuits), biasing networks consisting of resistors are commonly employed. Much more elaborate biasing arrangements are used in integrated circuits, for example, bandgap voltage references and current mirrors. The voltage divider configuration achieves the correct voltages by the use of resistors in certain patterns. By selecting the proper resistor values, stable current levels can be achieved that vary only little over temperature and with transistor properties such as β.
The operating point of a device, also known as bias point, quiescent point, or Q-point, is the point on the output characteristics that shows the DC collector–emitter voltage (Vce) and the collector current (Ic) with no input signal applied.
Bias circuit requirements
A bias network is selected to stabilize the operating point of the transistor, by reducing the following effects of device variability, temperature, and voltage changes:
The gain of a transistor can vary significantly between different batches, which results in widely different operating points for sequential units in serial production or after replacement of a transistor.
Due to the Early effect, the current gain is affected by the collector–emitter voltage.
Both gain and base–emitter voltage depend on the temperature.
The leakage current also increases with temperature.
A bias circuit may be composed of only resistors |
https://en.wikipedia.org/wiki/TRNA%20%28adenine-N6-%29-methyltransferase | In enzymology, a tRNA (adenine-N6-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing N6-methyladenine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing N6-methyladenine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (adenine-N6-)-methyltransferase. This enzyme is also called S-adenosyl-L-methionine:tRNA (adenine-6-N-)-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/TRNA%20%28cytosine-5-%29-methyltransferase | In enzymology, a tRNA (cytosine-5-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing 5-methylcytosine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing 5-methylcytosine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (cytosine-5-)-methyltransferase. Other names in common use include transfer ribonucleate cytosine 5-methyltransferase, and transfer RNA cytosine 5-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/TRNA%20%28guanine-N1-%29-methyltransferase | In enzymology, a tRNA (guanine-N1-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing N1-methylguanine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing N1-methylguanine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (guanine-N1-)-methyltransferase. Other names in common use include transfer ribonucleate guanine 1-methyltransferase, tRNA guanine 1-methyltransferase, and S-adenosyl-L-methionine:tRNA (guanine-1-N-)-methyltransferase.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/TRNA%20%28guanine-N2-%29-methyltransferase | In enzymology, a tRNA (guanine-N2-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing N2-methylguanine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing N2-Methylguanine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (guanine-N2-)-methyltransferase. Other names in common use include transfer ribonucleate guanine 2-methyltransferase, transfer ribonucleate guanine N2-methyltransferase, transfer RNA guanine 2-methyltransferase, guanine-N2-methylase, and S-adenosyl-L-methionine:tRNA (guanine-2-N-)-methyltransferase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/TRNA%20%28guanine-N7-%29-methyltransferase | In enzymology, a tRNA (guanine-N7-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing N7-methylguanine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing N7-methylguanine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (guanine-N7-)-methyltransferase. Other names in common use include transfer ribonucleate guanine 7-methyltransferase, 7-methylguanine transfer ribonucleate methylase, tRNA guanine 7-methyltransferase, N7-methylguanine methylase, and S-adenosyl-L-methionine:tRNA (guanine-7-N-)-methyltransferase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/TRNA%20guanosine-2%27-O-methyltransferase | In enzymology, a tRNA guanosine-2'-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing 2'-O-methylguanosine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing 2'-O-methylguanosine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA guanosine-2'-O-methyltransferase. Other names in common use include transfer ribonucleate guanosine 2'-methyltransferase, tRNA guanosine 2'-methyltransferase, tRNA (guanosine 2')-methyltransferase, tRNA (Gm18) 2'-O-methyltransferase, tRNA (Gm18) methyltransferase, tRNA (guanosine-2'-O-)-methyltransferase, and S-adenosyl-L-methionine:tRNA (guanosine-2'-O-)-methyltransferase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/TRNA%20%28uracil-5-%29-methyltransferase | In enzymology, a tRNA (uracil-5-)-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tRNA containing uridine at position 54 S-adenosyl-L-homocysteine + tRNA containing ribothymidine at position 54
Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA containing uridine at position 54, whereas its two products are S-adenosylhomocysteine and tRNA containing ribothymidine at position 54.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (uracil-5-)-methyltransferase. Other names in common use include ribothymidyl synthase, transfer RNA uracil 5-methyltransferase, transfer RNA uracil methylase, tRNA uracil 5-methyltransferase, m5U-methyltransferase, tRNA:m5U54-methyltransferase, and RUMT.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CSNK2A2 | Casein kinase II subunit alpha' is an enzyme that in humans is encoded by the CSNK2A2 gene.
Interactions
CSNK2A2 has been shown to interact with over 160 different substrates.
CSNK2A2 has been shown to interact with:
Activating transcription factor 2,
ATF1,
C-Fos,
CREB binding protein,
CSNK2B,
FGF1,
Nucleolin,
PIN1,
PTEN, and
RELA.
References
External links
Further reading |
https://en.wikipedia.org/wiki/Tryptophan%202-C-methyltransferase | In enzymology, a tryptophan 2-C-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + L-tryptophan S-adenosyl-L-homocysteine + L-2-methyltryptophan
Thus, the two substrates of this enzyme are S-adenosyl methionine and L-tryptophan, whereas its two products are S-adenosylhomocysteine and L-2-methyltryptophan.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:L-tryptophan 2-C-methyltransferase. Other names in common use include tryptophan 2-methyltransferase, and S-adenosylmethionine:tryptophan 2-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tyramine%20N-methyltransferase | In enzymology, a tyramine N-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + tyramine S-adenosyl-L-homocysteine + N-methyltyramine
Thus, the two substrates of this enzyme are S-adenosyl methionine and tyramine, whereas its two products are S-adenosylhomocysteine and N-methyltyramine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tyramine N-methyltransferase. Other names in common use include DIB O-methyltransferase (3,5-diiodo-4-hydroxy-benzoic acid), S-adenosyl-methionine:tyramine N-methyltransferase, and tyramine methylpherase. This enzyme participates in tyrosine metabolism.
References
EC 2.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Vitexin%202%22-O-rhamnoside%207-O-methyltransferase | In enzymology, a vitexin 2"-O-rhamnoside 7-O-methyltransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + vitexin 2"-O-beta-L-rhamnoside S-adenosyl-L-homocysteine + 7-O-methylvitexin 2"-O-beta-L-rhamnoside
Thus, the two substrates of this enzyme are S-adenosyl methionine and vitexin 2"-O-beta-L-rhamnoside, whereas its two products are S-adenosylhomocysteine and 7-O-methylvitexin 2"-O-beta-L-rhamnoside.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:vitexin-2"-O-beta-L-rhamnoside 7-O-methyltransferase.
References
EC 2.1.1
Enzymes of unknown structure
O-methylated flavones metabolism |
https://en.wikipedia.org/wiki/G%20protein-coupled%20bile%20acid%20receptor | The G protein-coupled bile acid receptor 1 (GPBAR1) also known G-protein coupled receptor 19 (GPCR19), membrane-type receptor for bile acids (M-BAR) or TGR5 as is a protein that in humans is encoded by the GPBAR1 gene.
Function
This gene encodes a member of the G protein-coupled receptor (GPCR) superfamily. This protein functions as a cell surface receptor for bile acids. Treatment of cells expressing this GPCR with bile acids induces the production of intracellular cAMP, activation of a MAP kinase signaling pathway, and internalization of the receptor. The receptor is implicated in the suppression of macrophage functions and regulation of energy homeostasis by bile acids.
One effect of this receptor is to activate deiodinases which convert the prohormone thyroxine (T4) to the active hormone triiodothyronine (T3). T3 in turn activates the thyroid hormone receptor which increases metabolic rate.
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Cyclin%20T1 | Cyclin-T1 is a protein that in humans is encoded by the CCNT1 gene.
Function
The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns that contribute to the temporal coordination of each mitotic event. This cyclin tightly associates with CDK9 kinase, and was found to be a major subunit of the transcription elongation factor p-TEFb. The kinase complex containing this cyclin and the elongation factor can interact with, and act as a cofactor of human immunodeficiency virus type 1 (HIV-1) Tat protein, and was shown to be both necessary and sufficient for full activation of viral transcription. This cyclin and its kinase partner were also found to be involved in the phosphorylation and regulation of the carboxy-terminal domain (CTD) of the largest RNA polymerase II subunit.
Interactions
Cyclin T1 has been shown to interact with the following:
Aryl hydrocarbon receptor
CDK9
Granulin
HEXIM1
Myc
NUFIP1
Promyelocytic leukemia protein
References
Further reading |
https://en.wikipedia.org/wiki/NFKB2 | Nuclear factor NF-kappa-B p100 subunit is a protein that in humans is encoded by the NFKB2 gene.
Function
NF-κB has been detected in numerous cell types that express cytokines, chemokines, growth factors, cell adhesion molecules, and some acute phase proteins in health and in various disease states. NF-κB is activated by a wide variety of stimuli such as cytokines, oxidant-free radicals, inhaled particles, ultraviolet irradiation, and bacterial or viral products. Inappropriate activation of NF-kappa-B has been linked to inflammatory events associated with autoimmune arthritis, asthma, septic shock, lung fibrosis, glomerulonephritis, atherosclerosis, and AIDS. In contrast, complete and persistent inhibition of NF-kappa-B has been linked directly to apoptosis, inappropriate immune cell development, and delayed cell growth. For reviews, see Chen et al. (1999) and Baldwin (1996).[supplied by OMIM]
Clinical significance
Mutation of the NFKB2 gene has been linked to Common variable immunodeficiency (CVID) as the cause of the disease. Other genes might also be responsible. The frequency of NFKB2 mutation in CVID population is yet to be established.
The protein NFKB2 can become mutated and lead to hereditary endocrine and immuneodeficiences. The mutation occurs at the C-terminus of NFKB2 and it causes common variable immunodeficienciency which in turn causes endocrine deficiency and immunodeficiencies. A NFKB2 mutation can cause things like adrenocorticotropic hormone deficien |
https://en.wikipedia.org/wiki/Phosphatidylinositol%20transfer%20protein | Phosphatidylinositol transfer protein (PITP) or priming in exocytosis protein 3 (PEP3) is a ubiquitous cytosolic domain involved in transport of phospholipids from their site of synthesis in the endoplasmic reticulum and Golgi to other
cell membranes.
Biological function
PITP has been also shown to be an essential component of the polyphosphoinositide synthesis machinery and is hence required for proper signalling by epidermal growth factor and f-Met-Leu-Phe, as well as for exocytosis. The role of PITP in polyphosphoinositide synthesis may also explain its involvement in intracellular vesicular traffic.
Structure and evolution
Along with the structurally unrelated Sec14p family (found in ), this family can bind/exchange one molecule of phosphatidylinositol (PI) or phosphatidylcholine (PC) and thus aids their transfer between different membrane compartments. There are three sub-families - all share an N-terminal PITP-like domain, whose sequence is highly conserved. It is described as consisting of three regions. The N-terminal region is thought to bind the lipid and contains two helices and an eight-stranded, mostly antiparallel beta-sheet. An intervening loop region, which is thought to play a role in protein-protein interactions, separates this from the C-terminal region, which exhibits the greatest sequence variation and may be involved in membrane binding. This motif marks PITP as part of the larger SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) domain superfamily.
PIT |
https://en.wikipedia.org/wiki/Interstitial%20collagenase | Interstitial collagenase, also known as fibroblast collagenase, and matrix metalloproteinase-1 (MMP-1) is an enzyme that in humans is encoded by the MMP1 gene. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP-1 was the first vertebrate collagenase both purified to homogeneity as a protein, and cloned as a cDNA. MMP-1 has an estimated molecular mass of 54 kDa.
Structure
MMP-1 has an archetypal structure consisting of a pre-domain, a pro-domain, a catalytic domain, a linker region and a hemopexin-like domain. The primary structure of MMP-1 was first published by Goldberg, G I, et al. Two main nomenclatures for the primary structure are currently in use, the original one from which the first amino-acid starts with the signalling peptide and a second one where the first amino-acid starts counting from the prodomain (proenzyme nomenclature).
Catalytic domain
The catalytic domains of MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40 Å. Despite the similarity of the catalytic domains of MMPs, this entry will focus only on the structural features of MMP-1 catalytic domain.
Overall structural characteristics
The catalytic domain of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca2+ and two Zn2+, one of which with catalytic role.
The catalytic domain (CAT) of MMP-1 starts with t |
https://en.wikipedia.org/wiki/Nagy%20Habib | Nagy Habib (born 1952), is professor of hepato-biliary surgery at Imperial College, London, and is known for devising radio-frequency based liver resection devices which remove liver tumour with minimal blood loss. His work has also focused on stem cells and gene therapy.
Early life and education
Nagy Habib was born in Cairo, Egypt, 1952. He trained under both and the transplant surgeon Thomas Starzl.
Career
His work has focused on stem cells and gene therapy. He led the first clinical trial in the use of oncolytic adenoviruses for the treatment of liver cancer. It was carried out by means of a locally restricted injection into the main blood vessel to the liver. The findings were published in 2001. It was found to be safe, but the second phase of the trial did not find it effective. In 2004, he took stem cells from a person with liver cirrhosis and injected them into their liver artery, resulting in some improvement of liver function.
In 2003 he was appointed professor of hepato-biliary surgery at Imperial College, London. In June 2007 he was appointed pro-rector for Commercial Affairs at Imperial.
Habib developed several radio-frequency (RF) based liver resection devices. He devised the Habib RF device using the Habib needle, which has a modified version called the Habib 4X. It removes tumour with minimal blood loss. The procedure has come to be known as 'Habib's resection'.
MiNA Therapeutics, a biotechnology company dealing in small activating RNA technology was co-f |
https://en.wikipedia.org/wiki/Glutathione%20S-transferase%20Mu%201 | Glutathione S-transferase Mu 1 (gene name GSTM1) is a human glutathione S-transferase.
Function
Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a cytoplasmic glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress, by conjugation with glutathione.
The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3, and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins, as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with an increase in a number of cancers, likely due to an increased susceptibility to environmental toxins and carcinogens. Multiple protein isoforms are encoded by transcript variants of this gene.
See also
Biliary atresia
References
Further reading
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human Glutathione S-transferase Mu 1 |
https://en.wikipedia.org/wiki/GSTP1 | Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene.
Function
Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, the soluble GSTs are categorized into four main classes: alpha, mu, pi, and theta. The glutathione S-transferase pi gene (GSTP1) is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.
Interactions
GSTP1 has been shown to interact with Fanconi anemia, complementation group C and MAPK8.
GST-Pi is expressed in many human tissues, particularly in the biliary tree, renal distal convoluted tubules and lungs.
Possible drug target
Triple-negative breast cancer cells rely on glutathione-S-transferase Pi1, and inhibitors are being studied. Piperlongumine has been found to silence the gene.
References
Further reading |
https://en.wikipedia.org/wiki/PTPN6 | Tyrosine-protein phosphatase non-receptor type 6, also known as Src homology region 2 domain-containing phosphatase-1 (SHP-1), is an enzyme that in humans is encoded by the PTPN6 gene.
Function
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling, (e.g., the LYN-CD22-SHP-1 pathway). Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported.
Expression
SHP-1 gene has two promoters: P-1, active in epithelial cells, and P-2, active in hemopoietic cells. In addition the expression of SHP-1 is low in epithelial cells and high in hemopoietic cells. SHP-1 level in epithelial cells increases and in hematopoietic cells decreases in cancer.
Interactions
PTPN6 has been shown to interact with:
BCR gene,
CD117,
CD22,
CD31,
CTNND1,
EGFR,
E |
https://en.wikipedia.org/wiki/Centre%20for%20Artificial%20Intelligence%20and%20Robotics | The Centre for Artificial Intelligence and Robotics (CAIR) is a laboratory of the Defence Research & Development Organization (DRDO). Located in Bangalore, Karnataka, involved in the Research & Development of high quality Secure Communication, Command and Control, and Intelligent Systems. CAIR was founded by Arogyaswami Paulraj. CAIR is the primary laboratory for R&D in different areas of Defence Information and Communication Technology (ICT).
History
CAIR was established in October 1986. Its research focus was initially in the areas of Artificial Intelligence (AI), Robotics, and Control systems. In November 2000, R&D groups working in the areas of Command, Control, Communications & Intelligence (C3I) systems, Communication and Networking, and communication secrecy in Electronics and Radar Development Establishment (LRDE) were merged with CAIR.
CAIR, which was operating from different campuses across Bangalore has now moved .
Projects
DRDO NETRA, software to intercept online communications.
SecOS, Secure Operating System
Muntra - unmanned ground vehicle manufactured at the Ordnance Factory Medak.
External links
CAIR Home Page
Robot soldiers!
Defence Research and Development Organisation laboratories
Artificial intelligence laboratories
Research institutes in Bangalore
Laboratories in India
1986 establishments in Karnataka
Research institutes established in 1986
Robotics in India |
https://en.wikipedia.org/wiki/Eugene%20%28given%20name%29 | Eugene is a common male given name that comes from the Greek εὐγενής (eugenēs), "noble", literally "well-born", from εὖ (eu), "well" and γένος (genos), "race, stock, kin". Gene is a common shortened form. The feminine variant is Eugenia or Eugenie.
Egon, a common given name in parts of central and northern Europe, is also a variant of Eugene / Eugine. Other male foreign-language variants include:
People
Notable people with the given name Eugene or Eugène include:
Christianity
Eugene or Eugenios of Trebizond, 4th century Christian saint and martyr
St. Eugene, one of the deacons of saint Zenobius of Florence
Eugene (Eoghan) (died c. 618), Irish saint
Pope Eugene I (died 657), Italian pope from 655 to 657
Pope Eugene II (died 827), Italian pope from 824 to 827
Pope Eugene III (died 1153), Italian pope from 1145 to 1153
Pope Eugene IV (1383–1447), Italian pope from 1431 to 1447
Eugène Philippe LaRocque (1927–2018), Roman Catholic bishop from Canada
Eugene Antonio Marino (1934–2000), first African-American archbishop in the United States
Military
Prince Eugene of Savoy (1663–1736), Austrian general, statesman of the Holy Roman Empire and the Austrian monarchy
Eugène de Beauharnais (1781–1824), stepson and adopted child of Napoleon
Eugene A. Greene (1921–1942), American sailor, posthumous recipient of the Navy Cross
Eugène Maizan (1819–1845), French naval lieutenant and explorer
Eugene Sledge (1923–2001), American World War II Marine and academic
Eugene Sullivan, (1918-1942 |
https://en.wikipedia.org/wiki/Samsung%20U740%20Alias | The Samsung Alias (formerly known as the SCH-u740) was a cell phone made by Samsung. The phone was originally available in a champagne finish then black, with the dialing keys in grey in contrast to black keys. A subsequent relaunch under the "Alias" name was accompanied by the switch to a blue/silver color scheme with the dialing keys half white and half black instead of grey and black. It features a dual-hinge design that can be opened portrait or landscape style. In landscape mode it features a QWERTY keyboard and VCAST music on the Verizon Wireless network within Australia and the USA.
The phone runs on Verizon Wireless's digital and Ev-DO networks. It also is available within Canada on Bell Mobility's network.
The music format is WMA. Its external features are a small postage stamp sized front display, touch sensitive music control buttons and a 1.3-megapixel camera with flash. On the right side there is a speakerphone button and a microSD (Transflash) card slot. On the left, there is a hold button along with an up/down volume button and proprietary charger/data transfer port. Opened in portrait mode, a standard numerical dialing pad along with two soft keys, send and end keys, a camera button, a voice command button, and a circular four-point dial with an OK key in the center are all available. Opened horizontally, the full QWERTY keypad is usable and a simple button press allows switching between the various alphanumeric functions. A pair of stereo speakers are mount |
https://en.wikipedia.org/wiki/CBL%20%28gene%29 | Cbl (named after Casitas B-lineage Lymphoma) is a mammalian gene encoding the protein CBL which is an E3 ubiquitin-protein ligase involved in cell signalling and protein ubiquitination. Mutations to this gene have been implicated in a number of human cancers, particularly acute myeloid leukaemia.
Discovery
In 1989 a virally encoded portion of the chromosomal mouse Cbl gene was the first member of the Cbl family to be discovered and was named v-Cbl to distinguish it from normal mouse c-Cbl. The virus used in the experiment was a mouse-tropic strain of Murine leukemia virus isolated from the brain of a mouse captured at Lake Casitas, California known as Cas-Br-M, and was found to have excised approximately a third of the original c-Cbl gene from a mouse into which it was injected. Sequencing revealed that the portion carried by the retrovirus encoded a tyrosine kinase binding domain, and that this was the oncogenic form as retroviruses carrying full-length c-Cbl did not induce tumor formation. The resultant transformed retrovirus was found to consistently induce a type of pre-B lymphoma, known as Casitas B-lineage lymphoma, in infected mice.
Structure
Full length c-Cbl has been found to consist of several regions encoding for functionally distinct protein domains:
N-terminal tyrosine kinase binding domain (TKB domain): determines the protein which it can bind to
RING finger domain motif: recruits enzymes involved in ubiquitination
Proline-rich region: the site of interac |
https://en.wikipedia.org/wiki/Sameridine | Sameridine is a 4-phenylpiperidine derivative that is related to the opioid analgesic drug pethidine (meperidine).
Sameridine has an unusual pharmacological profile, being both a local anaesthetic and a μ-opioid partial agonist. It is currently under development for use in surgical anasthesia, mainly administered by intrathecal infusion. It produces less respiratory depression than morphine, even at a high dose, and produces no respiratory depression at a low dose.
Sameridine is not currently a controlled drug, although if approved for medical use it will certainly be a prescription medicine, and it would probably be assigned to one of the controlled drug schedules in more restrictive jurisdictions such as Australia and the United States, especially if it were found to be addictive in animals.
References
External links
Substituted 4-phenyl-4-piperidinecarboxamides with both local anaesthetic and analgesic effect. US Patent 5227389
Process for the preparation of Sameridine. US Patent 5756748
4-Phenylpiperidines
Synthetic opioids
Carboxamides
Mu-opioid receptor agonists |
https://en.wikipedia.org/wiki/Semorphone | Semorphone (Mr 2264) is an opiate analogue that is an N-substituted derivative of oxymorphone.
Semorphone is a partial agonist at μ-opioid receptors. It is around twice the potency of morphine, but with a ceiling effect on both analgesia and respiratory depression which means that these effects stop becoming any stronger after a certain maximum dose.
It is not currently used in medicine, and is not a controlled drug, although it might be considered to be a controlled substance analogue of oxymorphone on the grounds of its related chemical structure in some jurisdictions such as the United States, Canada, Australia and New Zealand.
References
4,5-Epoxymorphinans
Opioids
Phenols
Tertiary alcohols
Ketones
Ethers
Mu-opioid receptor agonists |
https://en.wikipedia.org/wiki/Signet%20ring%20cell | In histology, a signet ring cell is a cell with a large vacuole. The malignant type is seen predominantly in carcinomas.
Signet ring cells are most frequently associated with stomach cancer, but can arise from any number of tissues including the prostate, bladder, gallbladder, breast, colon, ovarian stroma and testis.
Types
The NCI Thesaurus identifies the following types of signet ring cell
Castration cell, a non-malignant cell arising in the anterior pituitary gland under certain abnormal hormonal conditions.
Neoplastic thyroid gland follicular signet ring cell
Signet ring adenocarcinoma cell
Signet ring melanoma cell
Signet ring stromal cell
Appearance
The name of the cell comes from its appearance; signet ring cells resemble signet rings. They contain a large amount of mucin, which pushes the nucleus to the cell periphery. The pool of mucin in a signet ring cell mimics the appearance of a finger hole and the nucleus mimics the appearance of the face of the ring in profile.
Diagnostic significance
A significant number of signet ring cells, generally, are associated with a worse prognosis.
Classification of carcinomas
SRC carcinomas can be classified using immunohistochemistry.
See also
Signet ring cell carcinoma
References
External links
Signet ring cells - med.Utah.edu.
Signet ring cell definition - cancer.gov.
Signet ring cell cancer information - sites.google.com/site/signetringcancer.
Histopathology |
https://en.wikipedia.org/wiki/Juan%20Antonio | Juan Ignacio Antonio (born 5 January 1988) is an Argentine former professional football who played as a forward.
External links
Argentine Primera statistics
Player profile on the River Plate website
1988 births
Living people
People from Trelew
Footballers from Chubut Province
Argentine men's footballers
Argentine expatriate men's footballers
Men's association football forwards
Club Atlético River Plate footballers
Brescia Calcio players
Ascoli Calcio 1898 FC players
UC Sampdoria players
SSD Varese Calcio players
Parma Calcio 1913 players
Feralpisalò players
Serie A players
Serie B players
Serie C players
Expatriate men's footballers in Italy |
https://en.wikipedia.org/wiki/NSP1%20%28rotavirus%29 | NSP1 (NS53), the product of rotavirus gene 5, is a nonstructural RNA-binding protein that contains a cysteine-rich region and is a component of early replication intermediates. RNA-folding predictions suggest that this region of the NSP1 mRNA can interact with itself, producing a stem-loop structure similar to that found near the 5'-terminus of the NSP1 mRNA.
The carboxyl-half of the rotavirus nonstructural protein NSP1 is not required for virus replication.
NSP1 could play a role in host range restriction.
The cysteine-rich region of NSP1 is not considered essential for genome segment reassortment with heterologous virus.
NSP1 interacts with IRF3 in the infected cell. NSP1 is an antagonist of the IFN-signaling pathway.
Interferon regulatory factor 3 (IRF3) is a key transcription factor involved in the induction of interferon (IFN) in response to viral infection. NSP1 binds to and targets IRF3 for proteasome degradation early post-infection. IRF3 degradation is dependent on the presence of NSP1 and the integrity of the N-terminal zinc-binding domain, coupled with the regulated stability of IRF3 and NSP1 by the proteasome, collectively support the hypothesis that NSP1 is an E3 ubiquitin ligase.
NSP1 could mediates the degradation of IRF3, IRF5, and IRF7 by recognizing a common element of IRF proteins, thereby allowing NSP1 to act as a broad-spectrum antagonist of IRF function.
NSP1 also inhibits activation of NFkappaB
NSP1 inhibits cellular apoptosis by directly intera |
https://en.wikipedia.org/wiki/Pethidine%20intermediate%20A | Pethidine intermediate A is a 4-phenylpiperidine derivative that is a precursor to the opioid analgesic drug pethidine (meperidine). It is not known to have any analgesic activity in its own right, however other derivatives of pethidine with a 4-cyano group in place of the carboxylate ethyl ester have been found to be active, so pethidine intermediate A might also show opioid effects. It is scheduled by UN Single Convention on Narcotic Drugs. It is a Schedule II Narcotic controlled substance in the United States and has an ACSCN of 9232. The 2014 annual manufacturing quota was 6 grammes (as an end product, presumably for research use).
See also
Moramide intermediate
Methadone intermediate
Pethidine intermediate B (norpethidine)
Pethidine intermediate C (pethidinic acid)
References
Synthetic opioids
4-Phenylpiperidines
Nitriles |
https://en.wikipedia.org/wiki/Nseluka | Nseluka is a small town in northern Zambia. It is on the M1 road, which heads to Kasama in the south and Mbala/Mpulungu in the north.
Statistics
elevation –
Transport
It has a station on the TAZARA railway. It is the proposed junction for a branch railway to Mpulungu on the shores of Lake Tanganyika.
See also
Transport in Zambia
References
Populated places in Northern Province, Zambia |
https://en.wikipedia.org/wiki/NSP2%20%28rotavirus%29 | NSP2 (NS35), is a rotavirus nonstructural RNA-binding protein that accumulates in cytoplasmic inclusions (viroplasms) and is required for genome replication. NSP2 is closely associated in vivo with the viral replicase. The non-structural protein NSP5 plays a role in the structure of viroplasms mediated by its interaction with NSP2.
References
Rotaviruses
Viral nonstructural proteins |
https://en.wikipedia.org/wiki/NSP3%20%28rotavirus%29 | Rotavirus protein NSP3 (NS34) is bound to the 3' end consensus sequence of viral mRNAs in infected cells.
Four nucleotides are the minimal requirement for RNA recognition by rotavirus nonstructural protein NSP3: using short oligoribonucleotides, it was established that the minimal RNA sequence required for binding of NSP3A is GACC.
Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A)-binding protein from eIF4F. And NSP3A, by taking the place of PABP on eIF4GI, is responsible for the shut-off of cellular protein synthesis.
Expression of NSP3 in mammalian cells allows the efficient translation of virus-like mRNA: NSP3 forms a link between viral mRNA and the cellular translation machinery and hence is a functional analogue of cellular poly(A)-binding protein.
Site-directed mutagenesis and isothermal titration calorimetry documented that NSP3 and PABP use analogous eIF4G recognition strategies, despite marked differences in tertiary structure.
Using the yeast two-hybrid assay, RoXan a novel cellular protein was found to bind NSP3. The interaction between NSP3 and RoXaN does not impair the interaction between NSP3 and eIF4GI, and a ternary complex made of NSP3, RoXaN, and eIF4G I can be detected in rotavirus-infected cells, implicating RoXaN in translation regulation.
References
Rotaviruses
RNA-binding proteins
Viral nonstructural proteins |
https://en.wikipedia.org/wiki/Recombinase-mediated%20cassette%20exchange | RMCE (recombinase-mediated cassette exchange) is a procedure in reverse genetics allowing the systematic, repeated modification of higher eukaryotic genomes by targeted integration, based on the features of site-specific recombination processes (SSRs). For RMCE, this is achieved by the clean exchange of a preexisting gene cassette for an analogous cassette carrying the "gene of interest" (GOI).
The genetic modification of mammalian cells is a standard procedure for the production of correctly modified proteins with pharmaceutical relevance. To be successful, the transfer and expression of the transgene has to be highly efficient and should have a largely predictable outcome. Current developments in the field of gene therapy are based on the same principles. Traditional procedures used for transfer of GOIs are not sufficiently reliable, mostly because the relevant epigenetic influences have not been sufficiently explored: transgenes integrate into chromosomes with low efficiency and at loci that provide only sub-optimal conditions for their expression. As a consequence the newly introduced information may not be realized (expressed), the gene(s) may be lost and/or re-insert and they may render the target cells in unstable state. It is exactly this point where RMCE enters the field. The procedure was introduced in 1994 and it uses the tools yeasts and bacteriophages have evolved for the efficient replication of important genetic information:
General principles
Most yeast s |
https://en.wikipedia.org/wiki/M/M/1%20queue | In queueing theory, a discipline within the mathematical theory of probability, an M/M/1 queue represents the queue length in a system having a single server, where arrivals are determined by a Poisson process and job service times have an exponential distribution. The model name is written in Kendall's notation. The model is the most elementary of queueing models and an attractive object of study as closed-form expressions can be obtained for many metrics of interest in this model. An extension of this model with more than one server is the M/M/c queue.
Model definition
An M/M/1 queue is a stochastic process whose state space is the set {0,1,2,3,...} where the value corresponds to the number of customers in the system, including any currently in service.
Arrivals occur at rate λ according to a Poisson process and move the process from state i to i + 1.
Service times have an exponential distribution with rate parameter μ in the M/M/1 queue, where 1/μ is the mean service time.
All arrival times and services times are (usually) assumed to be independent of one another.
A single server serves customers one at a time from the front of the queue, according to a first-come, first-served discipline. When the service is complete the customer leaves the queue and the number of customers in the system reduces by one.
The buffer is of infinite size, so there is no limit on the number of customers it can contain.
The model can be described as a continuous time Markov chain with |
https://en.wikipedia.org/wiki/NSP4%20%28rotavirus%29 | The rotavirus nonstructural protein NSP4 was the first viral enterotoxin discovered. It is a viroporin and induces diarrhea and causes Ca2+-dependent transepithelial secretion.
A transmembrane glycoprotein, NSP4 is organized into three main domains: a three-helical TM domain in the N-terminus (also a viroporin domain), a central cytoplasmic coiled-coil domain for multimerization, and an C-terminal flexible region. It can also be secreted out of the cell. As of 2019, only structures of the central domain, which is responsible for diarrhea, has been solved. It oligomerizes into dimeric, tetrameric, pentameric, and even higher-order forms.
References
Rotaviruses
Viral nonstructural proteins |
https://en.wikipedia.org/wiki/NSP5%20%28rotavirus%29 | NSP5 (nonstructural protein 5) encoded by genome segment 11 of group A rotaviruses. In virus-infected cells NSP5 accumulates in the viroplasms. NSP5 has been shown to be autophosphorylated.
Interaction of NSP5 with NSP2 was also demonstrated. In rotavirus-infected cells, the non-structural proteins NSP5 and NSP2 localize in complexes called viroplasms, where replication and assembly occur and they can drive the formation of viroplasm-like structures in the absence of other rotaviral proteins and rotavirus replication.
There is no atomic-resolution structure of NSP5 determined as of June 2019. However, the low resolution three-dimensional structure of the NSP2-NSP5 assembly has been observed by cryo-EM. NSP5 occupies the same site as RNA when binding to NSP2. The EM data from this 2006 study has not been published.
References
Rotaviruses
Viral nonstructural proteins |
https://en.wikipedia.org/wiki/NSP6%20%28rotavirus%29 | Putative transmembrane domain more commonly known as Non-structural Protein 6 (NSP6) is one of the two non-structural proteins that gene 11 in rotavirus encodes for alongside NSP5. NSP6 is composed of six transmembrane domains and a C terminal tail. In contrast to the other rotavirus non-structural proteins, NSP6 was found to have a high rate of turnover, being completely degraded within 2 hours of synthesis. NSP6 was found to be a sequence-independent nucleic acid binding protein, with similar affinities for ssRNA and dsRNA
It has been determined that NSP6 has three crucial functions that it conducts. As messages flow among the replication organelle and the endoplasmic reticulum (ER) NSP6 acts as a filter. In this case, NSP6 hinders the access of ER luminal proteins to the DMVs but permits the passing of lipids. Next NSP6 arranges DMV clusters, since the DMV clusters are organized by NSP6 it can reconstruct them with LD-derived Lipids. Lastly, through LD-tethering complex DFCP1-RAB18 intervenes in the contact of lipid droplets (LDs).
Since NSP6 is one of two non-structural proteins that gene 11 codes for NSP6 is found in both α and β coronaviruses and produces autophagosomes. While NSP6 is found to produce a substantial amount of autophagosomes, through the analysis of MAP1LC3B puncta it is observed that autophagosomes produced by NSP6 are much smaller in size. As indicated by the statistical analysis of WIPI2 puncta the size of NSP6-produced autophagosomes is restricted |
https://en.wikipedia.org/wiki/SHC1 | SHC-transforming protein 1 is a protein that in humans is encoded by the SHC1 gene. SHC has been found to be important in the regulation of apoptosis and drug resistance in mammalian cells.
SCOP classifies the 3D structure as belonging to the SH2 domain family.
Gene and expression
The gene SHC1 is located on chromosome 1 and encodes 3 main protein isoforms: p66SHC, p52SHC and p46SHC. These proteins differ in activity and subcellular locations, p66 is the longest and while the p52 and p46 link activated receptor tyrosine kinase to the RAS pathway. The protein SHC1 also acts as a scaffold protein which is used in cell surface receptors. The three proteins that SHC1 codes for have distinctly different molecular weights. All three SHC1 proteins share the same domain arrangement consisting of an N-terminal phosphotyrosine-binding(PTB) domain and a C-terminal Src-homology2(SH2) domain. Both of the domains for the three proteins can bind to tyrosine-phosphorylated proteins but they are different in their phosphopeptide-binding specificities. P66SHC is characterized by having an additional N-terminal CH2 domain.
Function
Overexpression of SHC proteins are associated with cancer mitogenesis, carcinogenesis and metastasis. The SHC and its adaptor proteins transmit signaling of the cell surface receptors such as EGFR, erbV-2 and insulin receptors. p52SHC and p46SHC activate the Ras-ERK pathway. p66SHC inhibits ERK1/2 activity and antagonize mitogenic and survival abilities of T- |
https://en.wikipedia.org/wiki/Caveolin%201 | Caveolin-1 is a protein that in humans is encoded by the CAV1 gene.
Function
The scaffolding protein encoded by this gene is the main component of the caveolae plasma membranes found in most cell types. The protein links integrin subunits to the tyrosine kinase FYN, an initiating step in coupling integrins to the Ras-ERK pathway and promoting cell cycle progression. The gene is a tumor suppressor gene candidate and a negative regulator of the Ras-p42/44 MAP kinase cascade. CAV1 and CAV2 are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex. By using alternative initiation codons in the same reading frame, two isoforms (alpha and beta) are encoded by a single transcript from this gene.
Interactions
Caveolin 1 has been shown to interact with heterotrimeric G proteins,
Src tyrosine kinases (Src, Lyn) and H-Ras,
cholesterol,
TGF beta receptor 1,
endothelial NOS,
androgen receptor,
amyloid precursor protein,
gap junction protein, alpha 1,
nitric oxide synthase 2A, epidermal growth factor receptor, endothelin receptor type B, PDGFRB, PDGFRA, PTGS2, TRAF2, estrogen receptor alpha, caveolin 2, PLD2, Bruton's tyrosine kinase, and SCP2. All these interactions are through a caveolin-scaffolding domain (CSD) within caveolin-1 molecule. Molecules that interact with caveolin-1 contain caveolin-binding motifs (CBM).
See also
Caveolin
References
Further reading
Genes
Human proteins |
https://en.wikipedia.org/wiki/Nitric%20oxide%20synthase%202%20%28inducible%29 | Nitric oxide synthase, inducible is an enzyme which is encoded by the NOS2 gene in humans and mice.
Genetics
Three related pseudogenes are located within the Smith-Magenis syndrome region on chromosome 17. Alternative splicing of this gene results in two transcript variants encoding different isoforms.
Location
Nitric oxide synthase is expressed in epithelial cells of the liver, lung and bone marrow. It is inducible by a combination of lipopolysaccharide and certain cytokines.
Function
Nitric oxide is a reactive free radical mediating in neurotransmission, antimicrobial and antitumoral activities.
In mice, the function of Nos2 in immunity against a number of viruses, bacteria, fungi, and parasites has been well characterized, whereas in humans the role of NOS2 has remained elusive and controversial. Nos2 is important for protective immunity against CMV.
Caveolin 1 has been shown to interact with Nitric oxide synthase 2A. and Rac2.
Deficiency
Autosomal recessive NOS2 deficiency has been described in mice. They lack the gene encoding nitric oxide synthase 2 (Nos2) and are susceptible to murine CMV infection.
In February 2020, the same autosomal recessive, complete NOS2 deficiency was described in a human. A 51-year-old previously healthy person died after 29 months of progressive CMV infection due to respiratory failure secondary to CMV pneumonitis, CMV encephalitis, and hemophagocytic lymphohistiocytosis. Whole-exome sequencing on genomic DNA from his blood showed he h |
https://en.wikipedia.org/wiki/Endothelin%201 | Endothelin 1 (ET-1), also known as preproendothelin-1 (PPET1), is a potent vasoconstrictor peptide produced by vascular endothelial cells. The protein encoded by this gene EDN1 is proteolytically processed to release endothelin 1. Endothelin 1 is one of three isoforms of human endothelin.
Sources
Preproendothelin is precursor of the peptide ET-1. Endothelial cells convert preproendothelin to proendothelin and subsequently to mature endothelin, which the cells release.
Clinical significance
Endothelin-1 receptor antagonists (Bosentan) are used in the treatment of pulmonary hypertension. Use of these antagonists prevents pulmonary arterial constriction and thus inhibits pulmonary hypertension.
As of 2020, the role of endothelin-1 in affecting lipid metabolism and insulin resistance in obesity mechanisms was under clinical research.
References
External links
Endothelin receptor agonists |
https://en.wikipedia.org/wiki/GJB2 | Gap junction beta-2 protein (GJB2), also known as connexin 26 (Cx26) — is a protein that in humans is encoded by the GJB2 gene.
Clinical significance
Defects in this gene lead to the most common form of congenital deafness in developed countries, called DFNB1 (also known as connexin 26 deafness or GJB2-related deafness). One fairly common mutation is the deletion of one guanine from a string of six, resulting in a frameshift and termination of the protein at amino acid number 13. Having two copies of this mutation results in deafness.
Connexin 26 also plays a role in tumor suppression through mediation of the cell cycle. The abnormal expression of Cx26, correlated with several types of human cancers, may serve as a prognostic factor for cancers such as colorectal cancer, breast cancer, and bladder cancer. Furthermore, Cx26 over-expression is suggested to promote cancer development by facilitating cell migration and invasion and by stimulating the self-perpetuation ability of cancer stem cells.
Function
Gap junctions were first characterized by electron microscopy as regionally specialized structures on plasma membranes of contacting adherent cells. These structures were shown to consist of cell-to-cell channels. Proteins, called connexins, purified from fractions of enriched gap junctions from different tissues differ. The connexins are designated by their molecular mass. Another system of nomenclature divides gap junction proteins into two categories, alpha and beta, a |
https://en.wikipedia.org/wiki/C.%20M.%20Gupta | Chhitar Mal Gupta (born 1944) is an Indian molecular biologist and academic, known for researches on transbilayer phospholipid asymmetry in biological membranes., drug targeting in parasitic diseases and characterization of structure and function of Leishmania actin and actin binding proteins. He is former director of the Central Drug Research Institute, Lucknow and the Institute of Microbial Technology, Chandigarh. A Distinguished Biotechnology Fellow and Distinguished Biotechnology Research Professor of the Department of Biotechnology, Government of India, he is an elected fellow of The World Academy of Sciences, Indian Academy of Sciences, Indian National Science Academy, National Academy of Sciences, India and the National Academy of Medical Sciences. The Council of Scientific and Industrial Research, the apex agency of the Government of India for scientific research, awarded him the Shanti Swarup Bhatnagar Prize for Science and Technology, one of the highest Indian science awards, in 1985, for his contributions to biological sciences.
Education and research
Gupta graduated in medicinal chemistry from the Central Drug Research Institute, Lucknow, India with the degrees MSc and PhD. He served as the director of the Institute of Microbial Technology, Chandigarh for five years, and director of the Central Drug Research Institute (CDRI), Lucknow for over ten years.
After his superannuation, he continued to work at CDRI first as distinguished biotechnologist and then as d |
https://en.wikipedia.org/wiki/ORAI1 | Calcium release-activated calcium channel protein 1 is a calcium selective ion channel that in humans is encoded by the ORAI1 gene. Orai channels play an important role in the activation of T-lymphocytes. The loss of function mutation of Orai1 causes severe combined immunodeficiency (SCID) in humans The mammalian orai family has two additional homologs, Orai2 and Orai3. Orai proteins share no homology with any other ion channel family of any other known proteins. They have 4 transmembrane domains and form hexamers.
Structure and function
Orai channels are activated upon the depletion of internal calcium stores, which is called the "store-operated" or the "capacitative" mechanism. They are molecular constituents of the "calcium release activated calcium currents" (ICRAC). Upon activation of phospholipase C by various cell surface receptors, inositol trisphosphate is formed that releases calcium from the endoplasmic reticulum. The decreased calcium concentration in the endoplasmic reticulum is sensed by the STIM1 protein. STIM1 clusters upon the depletion of the calcium stores and forms "puncta", and relocates near the plasma membrane, where it activates Orai1 via protein-protein interaction.
In 2012, a 3.35-angstrom (Å) crystal structure of the Drosophila Orai channel, which shares 73% sequence identity with human Orai1 within its transmembrane region, was published. The structure, thought to show the closed state of the channel, revealed that a single channel is composed |
https://en.wikipedia.org/wiki/Nucleic%20acid%20analogue | Nucleic acid analogues are compounds which are analogous (structurally similar) to naturally occurring RNA and DNA, used in medicine and in molecular biology research.
Nucleic acids are chains of nucleotides, which are composed of three parts: a phosphate backbone, a pentose sugar, either ribose or deoxyribose, and one of four nucleobases.
An analogue may have any of these altered. Typically the analogue nucleobases confer, among other things, different base pairing and base stacking properties. Examples include universal bases, which can pair with all four canonical bases, and phosphate-sugar backbone analogues such as PNA, which affect the properties of the chain (PNA can even form a triple helix).
Nucleic acid analogues are also called Xeno Nucleic Acid and represent one of the main pillars of xenobiology, the design of new-to-nature forms of life based on alternative biochemistries.
Artificial nucleic acids include peptide nucleic acid (PNA), Morpholino and locked nucleic acid (LNA), as well as glycol nucleic acid (GNA), threose nucleic acid (TNA) and hexitol nucleic acids (HNA). Each of these is distinguished from naturally occurring DNA or RNA by changes to the backbone of the molecule.
In May 2014, researchers announced that they had successfully introduced two new artificial nucleotides into bacterial DNA, and by including individual artificial nucleotides in the culture media, were able to passage the bacteria 24 times; they did not create mRNA or proteins able to |
https://en.wikipedia.org/wiki/KiSS1-derived%20peptide%20receptor | The KiSS1-derived peptide receptor (also known as GPR54 or the Kisspeptin receptor) is a G protein-coupled receptor which binds the peptide hormone kisspeptin (metastin). Kisspeptin is encoded by the metastasis suppressor gene KISS1, which is expressed in a variety of endocrine and gonadal tissues. Activation of the kisspeptin receptor is linked to the phospholipase C and inositol trisphosphate second messenger cascades inside the cell.
Kisspeptins are neuropeptides synthesized in the hypothalamus and encoded by the KISS1 gene. The KISS1 gene encodes the G protein-coupled receptor 54 (known as KISS1R or GPR54) and plays a crucial role in regulating reproduction, pubertal maturation, and metabolic function. KISS1 neurons located in the arcuate nucleus (ARC) of the mediobasal hypothalamus (MBH) project to GnRH neurons in the median eminence, which expresses KISS1R, to stimulate LH secretions in a pulsatile manner from the anterior pituitary to initiate ovulation/ pubertal maturation. The KISS1 and KISS1R/GPR54 genes have been detected in the brain, pituitary, placenta, pancreas, liver, and small intestine.
Function
Kisspeptin is involved in the regulation of endocrine function and the onset of puberty, with activation of the kisspeptin receptor triggering release of gonadotropin-releasing hormone (GnRH), and release of kisspeptin itself being inhibited by oestradiol but enhanced by GnRH. Reductions in kisspeptin levels with age may conversely be one of the reasons behind age |
https://en.wikipedia.org/wiki/1%2C2-dihydrovomilenine%20reductase | In enzymology, a 1,2-dihydrovomilenine reductase () is an enzyme that catalyzes the chemical reaction
17-O-acetylnorajmaline + NADP 1,2-dihydrovomilenine + NADPH + H
Thus, the two substrates of this enzyme are 17-O-acetylnorajmaline and NADP, whereas its 3 products are 1,2-dihydrovomilenine, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 17-O-acetylnorajmaline:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1%2C2-dihydroxy-6-methylcyclohexa-3%2C5-dienecarboxylate%20dehydrogenase | In enzymology, a 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction
1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate + NAD 3-methylcatechol + NADH + CO
Thus, the two substrates of this enzyme are 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate and NAD, whereas its 3 products are 3-methylcatechol, NADH, and CO.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate:NAD+ oxidoreductase (decarboxylating). This enzyme participates in toluene and xylene degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/12-oxophytodienoate%20reductase | 12-oxophytodienoate reductase (OPRs) is an enzyme of the family of Old Yellow Enzymes (OYE). OPRs are grouped into two groups: OPRI and OPRII – the second group is the focus of this article, as the function of the first group is unknown, but is the subject of current research. The OPR enzyme utilizes the cofactor flavin mononucleotide (FMN) and catalyzes the following reaction in the jasmonic acid synthesis pathway:
This reaction occurs in peroxisomes in plants. Several isozymes have been discovered, with varying substrate stereospecificity: three in Solanum lycopersicum, 13 in Oryza sativa, and five in Arabidopsis thaliana. The OPR3 isozyme is most extensively studied because it can reduce all 4 stereoisomers of the substrate, OPDA and because it has shown to be the most significant enzyme in the jasmonic acid synthesis pathway.
Structure
12-oxophytodienoate reductase structure resembles OYE enzymes and has been elucidated by x-ray crystal structures. The cDNA encodes 372 amino acids for this enzyme. It exhibits a barrel fold of eight parallel beta-strands surrounded by eight alpha-helices to create a barrel shape. Turns at the N-terminus loops of the beta-strands have been shown to contain three to four amino acid residues and the C-terminus loops range between three and 47 amino acid residues. The C-terminus loops largely make up the active site and the larger range of the amount of residues is due to the diversity in the different isozyme active sites.
OPR3, the most |
https://en.wikipedia.org/wiki/15%2C16-dihydrobiliverdin%3Aferredoxin%20oxidoreductase | 15,16-dihydrobiliverdin:ferredoxin oxidoreductase () is an enzyme that catalyzes the following chemical reaction
15,16-dihydrobiliverdin + oxidized ferredoxin biliverdin IXalpha + reduced ferredoxin
The two substrates of this enzyme are 15,16-dihydrobiliverdin and oxidized ferredoxin, whereas its two products are biliverdin IXalpha and reduced ferredoxin.
Classification
15,16-dihydrobiliverdin:ferredoxin oxidoreductase belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is 15,16-dihydrobiliverdin:ferredoxin oxidoreductase. This enzyme is also called PebA. This enzyme participates in porphyrin and chlorophyll metabolism.
References
EC 1.3.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/15-oxoprostaglandin%2013-oxidase | In enzymology, a 15-oxoprostaglandin 13-oxidase () is an enzyme that catalyzes the chemical reaction
(5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprostanoate + NAD(P)+ (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprosta-13-enoate + NAD(P)H + H+
The 3 substrates of this enzyme are (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprostanoate, NAD+, and NADP+, whereas its 4 products are (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprosta-13-enoate, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (5Z)-(15S)-11alpha-hydroxy-9,15-dioxoprostanoate:NAD(P)+ Delta13-oxidoreductase. Other names in common use include 15-oxo-Delta13-prostaglandin reductase, Delta13-15-ketoprostaglandin reductase, 15-ketoprostaglandin Delta13-reductase, prostaglandin Delta13-reductase, prostaglandin 13-reductase, and 15-ketoprostaglandin Delta13-reductase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/1%2C6-dihydroxycyclohexa-2%2C4-diene-1-carboxylate%20dehydrogenase | In enzymology, a 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD catechol + CO + NADH + H
Thus, the two substrates of this enzyme are (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate and NAD, whereas its 4 products are catechol, CO, NADH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (1R,6R)-1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating). Other names in common use include 3,5-cyclohexadiene-1,2-diol-1-carboxylate dehydrogenase, 3,5-cyclohexadiene-1,2-diol-1-carboxylic acid dehydrogenase, dihydrodihydroxybenzoate dehydrogenase, DHBDH, cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase, 2-hydro-1,2-dihydroxybenzoate dehydrogenase, cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate:NAD+, oxidoreductase, and dihydrodihydroxybenzoate dehydrogenase. This enzyme participates in benzoate degradation via hydroxylation and benzoate degradation via coa ligation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%2C3-dihydro-2%2C3-dihydroxybenzoate%20dehydrogenase | In enzymology, a 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
2,3-dihydro-2,3-dihydroxybenzoate + NAD+ 2,3-dihydroxybenzoate + NADH + H+
Thus, the two substrates of this enzyme are 2,3-dihydro-2,3-dihydroxybenzoate and NAD+, whereas its 3 products are 2,3-dihydroxybenzoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2,3-dihydro-2,3-dihydroxybenzoate:NAD+ oxidoreductase. This enzyme is also called 2,3-diDHB dehydrogenase. This enzyme participates in biosynthesis of siderophore group nonribosomal.
Structure
2,3-diDHB dehydrogenase is a tetramer protein with dimension 65x69x43 Å. It has a crystallographic 222 symmetry, which exhibited for other members of short-chain oxireductase (SCOR) family of enzymes. The length of each monomer is 248 residues and the weight of the protein is 24647 Da. Each monomer consists of 7 beta-pleated sheets and 6 alpha helices.
Although the structure of the binding protein is not clearly defined, it was proposed that the binding pocket is made out of Leu83, Met85, Arg138, Gly140, Met141, Ser176, Met181, Gln182 and Leu185. It was also speculated that Arg138 is a likely subunit that interacts with the carboxyl group of 2,3-diDHB. Since there was a strong indication of oxidation at C3 position, Ser176 and Gln182 interact with the C2-hyd |
https://en.wikipedia.org/wiki/2%2C3-dihydroxy-2%2C3-dihydro-p-cumate%20dehydrogenase | In enzymology, a 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase () is an enzyme that catalyzes the chemical reaction
cis-5,6-dihydroxy-4-isopropylcyclohexa-1,3-dienecarboxylate + NAD+ 2,3-dihydroxy-p-cumate + NADH + H+
Thus, the two substrates of this enzyme are cis-5,6-dihydroxy-4-isopropylcyclohexa-1,3-dienecarboxylate and NAD+, whereas its 3 products are 2,3-dihydroxy-p-cumate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is cis-2,3-dihydroxy-2,3-dihydro-p-cumate:NAD+ oxidoreductase. This enzyme participates in biphenyl degradation.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%2C4-dichlorobenzoyl-CoA%20reductase | In enzymology, a 2,4-dichlorobenzoyl-CoA reductase () is an enzyme that catalyzes the chemical reaction
4-chlorobenzoyl-CoA + NADP+ + HCl 2,4-dichlorobenzoyl-CoA + NADPH + H+
The 3 substrates of this enzyme are 4-chlorobenzoyl-CoA, NADP+, and HCl, whereas its 3 products are 2,4-dichlorobenzoyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 4-chlorobenzoyl-CoA:NADP+ oxidoreductase (halogenating). This enzyme participates in 2,4-dichlorobenzoate degradation.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-alkenal%20reductase | In enzymology, a 2-alkenal reductase () is an enzyme that catalyzes the chemical reaction
n-alkanal + NAD(P)+ alk-2-enal + NAD(P)H + H+
The 3 substrates of this enzyme are n-alkanal, NAD+, and NADP+, whereas its 4 products are alk-2-enal, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is n-alkanal:NAD(P)+ 2-oxidoreductase. Other names in common use include NAD(P)H-dependent alkenal/one oxidoreductase, and NADPH:2-alkenal alpha,beta-hydrogenase.
Structural studies
As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-Coumarate%20reductase | In enzymology, a 2-coumarate reductase or melilotate dehydrogenase () is an enzyme that catalyzes the chemical reaction
3-(2-hydroxyphenyl)propanoate + NAD+ 2-coumarate + NADH + H+
Thus, the two substrates of this enzyme are 3-(2-hydroxyphenyl)propanoate and NAD+, whereas its 3 products are 2-coumarate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-(2-hydroxyphenyl)propanoate:NAD+ oxidoreductase. This enzyme participates in phenylalanine metabolism.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/2-enoate%20reductase | In enzymology, a 2-enoate reductase () is an enzyme that catalyzes the chemical reaction
butanoate + NAD+ 2-butenoate + NADH + H+
Thus, the two substrates of this enzyme are butanoate and NAD+, whereas its 3 products are 2-butenoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is butanoate:NAD+ Delta2-oxidoreductase. This enzyme is also called enoate reductase. This enzyme participates in phenylalanine metabolism. It has 4 cofactors: FAD, Iron, Sulfur, and Iron-sulfur.
References
EC 1.3.1
NADH-dependent enzymes
Flavoproteins
Iron enzymes
Sulfur enzymes
Iron-sulfur enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-furoyl-CoA%20dehydrogenase | In enzymology, a 2-furoyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-furoyl-CoA + H2O + acceptor S-(5-hydroxy-2-furoyl)-CoA + reduced acceptor
The 3 substrates of this enzyme are 2-furoyl-CoA, H2O, and acceptor, whereas its two products are S-(5-hydroxy-2-furoyl)-CoA and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 2-furoyl-CoA:acceptor 5-oxidoreductase (hydroxylating). Other names in common use include furoyl-CoA hydroxylase, 2-furoyl coenzyme A hydroxylase, 2-furoyl coenzyme A dehydrogenase, and 2-furoyl-CoA:(acceptor) 5-oxidoreductase (hydroxylating). It employs one cofactor, copper.
References
EC 1.3.99
Copper enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-hexadecenal%20reductase | In enzymology, a 2-hexadecenal reductase () is an enzyme that catalyzes the chemical reaction
hexadecanal + NADP+ 2-trans-hexadecenal + NADPH + H+
Thus, the two substrates of this enzyme are hexadecanal and NADP+, whereas its 3 products are 2-trans-hexadecenal, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hexadecanal:NADP+ Delta2-oxidoreductase. Other names in common use include 2-alkenal reductase, and hexadecanal: NADP+ oxidoreductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-hydroxy-6-oxo-6-phenylhexa-2%2C4-dienoate%20reductase | In enzymology, a 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate reductase () is an enzyme that catalyzes the chemical reaction
2,6-dioxo-6-phenylhexanoate + NADP+ 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + NADPH + H+
Thus, the two substrates of this enzyme are 2,6-dioxo-6-phenylhexanoate and NADP+, whereas its 3 products are 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2,6-dioxo-6-phenylhexanoate:NADP+ Delta2-oxidoreductase. Other names in common use include 2-hydroxy-6-oxo-phenylhexa-2,4-dienoate (reduced nicotinamide, and adenine dinucleotide phosphate) reductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%27-hydroxydaidzein%20reductase | In enzymology, a 2'-hydroxydaidzein reductase () is an enzyme that catalyzes the chemical reaction
2'-hydroxy-2,3-dihydrodaidzein + NADP+ 2'-hydroxydaidzein + NADPH + H+
Thus, the two substrates of this enzyme are 2'-hydroxy-2,3-dihydrodaidzein and NADP+, whereas its 3 products are 2'-hydroxydaidzein, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2'-hydroxy-2,3-dihydrodaidzein:NADP+ 2'-oxidoreductase. Other names in common use include NADPH:2'-hydroxydaidzein oxidoreductase, HDR, and 2'-hydroxydihydrodaidzein:NADP+ 2'-oxidoreductase. This enzyme participates in isoflavonoid biosynthesis.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure
Isoflavonoids metabolism |
https://en.wikipedia.org/wiki/2%27-Hydroxyisoflavone%20reductase | In enzymology, a 2'-hydroxyisoflavone reductase () is an enzyme that catalyzes the chemical reaction
vestitone + NADP+ 2'-hydroxyformononetin + NADPH + H+
Thus, the two substrates of this enzyme are vestitone and NADP+, whereas its 3 products are 2'-hydroxyformononetin, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is vestitone:NADP+ oxidoreductase. Other names in common use include NADPH:2'-hydroxyisoflavone oxidoreductase, isoflavone reductase, and 2',7-dihydroxy-4',5'-methylenedioxyisoflavone reductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-methylacyl-CoA%20dehydrogenase | In enzymology, a 2-methylacyl-CoA dehydrogenase () is an enzyme that catalyzes the chemical reaction
2-methylbutanoyl-CoA + acceptor 2-methylbut-2-enoyl-CoA + reduced acceptor
Thus, the two substrates of this enzyme are 2-methylbutanoyl-CoA and acceptor, whereas its two products are 2-methylbut-2-enoyl-CoA and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 2-methylbutanoyl-CoA:acceptor oxidoreductase. Other names in common use include branched-chain acyl-CoA dehydrogenase, 2-methyl branched chain acyl-CoA dehydrogenase, and 2-methylbutanoyl-CoA:(acceptor) oxidoreductase. This enzyme participates in valine, leucine and isoleucine degradation.
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-methyl-branched-chain-enoyl-CoA%20reductase | In enzymology, a 2-methyl-branched-chain-enoyl-CoA reductase () is an enzyme that catalyzes the chemical reaction
2-methylbutanoyl-CoA + electron transfer flavoprotein 2-methylcrotonoyl-CoA + reduced electron transfer flavoprotein + H+
Thus, the two substrates of this enzyme are 2-methylbutanoyl-CoA and an electron transfer flavoprotein, whereas its 3 products are 2-methylcrotonoyl-CoA, reduced electron transfer flavoprotein, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donors with flavin as acceptor. The systematic name of this enzyme class is 2-methyl-branched-chain-acyl-CoA:electron-transfer flavoprotein 2-oxidoreductase . This enzyme participates in the degradation of isoleucine. It employs one cofactor, FAD.
References
EC 1.3.8
Flavoproteins
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-methyleneoxindole%20reductase | In enzymology, a 3-methyleneoxindole reductase () is an enzyme that catalyzes the chemical reaction
3-methyl-1,3-dihydroindol-2-one + NADP+ 3-methylene-1,3-dihydro-2H-indol-2-one + NADPH + H+
Thus, the two substrates of this enzyme are 3-methyl-1,3-dihydroindol-2-one and NADP+, whereas its three products are 3-methylene-1,3-dihydro-2H-indol-2-one, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-methyl-1,3-dihydroindol-2-one:NADP+ oxidoreductase. This enzyme is also termed 3-methyloxindole:NADP+ oxidoreductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tumor%20necrosis%20factor%20receptor%201 | Tumor necrosis factor receptor 1 (TNFR1), also known as tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) and CD120a, is a ubiquitous membrane receptor that binds tumor necrosis factor-alpha (TNFα).
Function
The protein encoded by this gene is a member of the tumor necrosis factor receptor superfamily, which also contains TNFRSF1B. This protein is one of the major receptors for the tumor necrosis factor-alpha. This receptor can activate the transcription factor NF-κB, mediate apoptosis, and function as a regulator of inflammation. Antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRADD and TRAF2 have been shown to interact with this receptor, and thus play regulatory roles in the signal transduction mediated by the receptor.
Clinical significance
Germline mutations of the extracellular domains of this receptor were found to be associated with the human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS) or periodic fever syndrome. Impaired receptor clearance is thought to be a mechanism of the disease.
Mutations in the TNFRSF1A gene are associated with elevated risk of multiple sclerosis.
Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder, and high levels are associated with more severe psychotic symptoms.
High serum levels are also associated with cognitive impairment and dementia.
Interactions
TNFRSF1A has been shown to interact with:
BAG4,
CASP10,
FADD, |
https://en.wikipedia.org/wiki/3-oxo-5beta-steroid%204-dehydrogenase | In enzymology, a 3-oxo-5beta-steroid 4-dehydrogenase () is an enzyme that catalyzes the chemical reaction
a 3-oxo-5beta-steroid + acceptor a 3-oxo-Delta4-steroid + reduced acceptor
Thus, the two substrates of this enzyme are 3-oxo-5beta-steroid and acceptor, whereas its two products are 3-oxo-Delta4-steroid and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 3-oxo-5beta-steroid:acceptor Delta4-oxidoreductase. This enzyme is also called 3-oxo-5beta-steroid:(acceptor) Delta4-oxidoreductase. This enzyme participates in 3 metabolic pathways: bile acid biosynthesis, c21-steroid hormone metabolism, and androgen and estrogen metabolism.
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-oxosteroid%201-dehydrogenase | In enzymology, a 3-oxosteroid 1-dehydrogenase () is an enzyme that catalyzes the chemical reaction
a 3-oxosteroid + acceptor a 3-oxo-Delta1-steroid + reduced acceptor
Thus, the two substrates of this enzyme are 3-oxosteroid and acceptor, whereas its two products are 3-oxo-Delta1-steroid and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 3-oxosteroid:acceptor Delta1-oxidoreductase. Other names in common use include 3-oxosteroid Delta1-dehydrogenase, Delta1-dehydrogenase, 3-ketosteroid-1-en-dehydrogenase, 3-ketosteroid-Delta1-dehydrogenase, 1-ene-dehydrogenase, 3-oxosteroid:(2,6-dichlorphenolindophenol) Delta1-oxidoreductase, 4-en-3-oxosteroid:(acceptor)-1-en-oxido-reductase, Delta1-steroid reductase, and 3-oxosteroid:(acceptor) Delta1-oxidoreductase.
References
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%283S%2C4R%29-3%2C4-dihydroxycyclohexa-1%2C5-diene-1%2C4-dicarboxylate%20dehydrogenase | In enzymology, a (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction
(3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate + NAD 3,4-dihydroxybenzoate + CO + NADH
Thus, the two substrates of this enzyme are (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate and NAD, whereas its 3 products are 3,4-dihydroxybenzoate, CO, and NADH.
This enzyme is a part of the terephthalate degradation pathway in bacteria.
Family
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate:NAD+ oxidoreductase. Another name in common use is (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase. This enzyme employs one cofactor, iron.
References
EC 1.3.1
NADH-dependent enzymes
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-hydroxybenzoyl-CoA%20reductase | In enzymology, a 4-hydroxybenzoyl-CoA reductase () is an enzyme found in some bacteria and archaea that catalyzes the chemical reaction
benzoyl-CoA + acceptor + H2O 4-hydroxybenzoyl-CoA + reduced acceptor
The 3 substrates of this enzyme are benzoyl-CoA, acceptor, and H2O, whereas its two products are 4-hydroxybenzoyl-CoA and reduced acceptor.
This enzyme participates in benzoate degradation via coa ligation.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is benzoyl-CoA:acceptor oxidoreductase. Other names in common use include:
4-hydroxybenzoyl-CoA reductase (dehydroxylating), and
4-hydroxybenzoyl-CoA:(acceptor) oxidoreductase.
References
Further reading
EC 1.3.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/5%2C6-dihydroxy-3-methyl-2-oxo-1%2C2%2C5%2C6-tetrahydroquinoline%20dehydrogenase | In enzymology, a 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline dehydrogenase () is an enzyme that catalyzes the chemical reaction
5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline + NAD+ 5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline + NADH + H+
Thus, the two substrates of this enzyme are 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline and NAD+, whereas its 3 products are 5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline:NAD+ oxidoreductase.
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6-hydroxynicotinate%20reductase | In enzymology, a 6-hydroxynicotinate reductase () is an enzyme that catalyzes the chemical reaction
6-oxo-1,4,5,6-tetrahydronicotinate + oxidized ferredoxin 6-hydroxynicotinate + reduced ferredoxin
Thus, the two substrates of this enzyme are 6-oxo-1,4,5,6-tetrahydronicotinate and oxidized ferredoxin, whereas its two products are 6-hydroxynicotinate and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is 6-oxo-1,4,5,6-tetrahydronicotinate:ferredoxin oxidoreductase. Other names in common use include 6-oxotetrahydronicotinate dehydrogenase, 6-hydroxynicotinic reductase, HNA reductase, and 1,4,5,6-tetrahydro-6-oxonicotinate:ferredoxin oxidoreductase.
References
EC 1.3.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acyl-CoA%20dehydrogenase%20%28NADP%2B%29 | In enzymology, an acyl-CoA dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
acyl-CoA + NADP+ 2,3-dehydroacyl-CoA + NADPH + H+
Thus, the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are 2,3-dehydroacyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-CoA:NADP+ 2-oxidoreductase. Other names in common use include 2-enoyl-CoA reductase, dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide, phosphate), enoyl coenzyme A reductase, crotonyl coenzyme A reductase, crotonyl-CoA reductase, and acyl-CoA dehydrogenase (NADP+).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acyl-CoA%20oxidase | In enzymology, an acyl-CoA oxidase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + O2 trans-2,3-dehydroacyl-CoA + H2O2
Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2,3-dehydroacyl-CoA and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is acyl-CoA:oxygen 2-oxidoreductase. Other names in common use include fatty acyl-CoA oxidase, acyl coenzyme A oxidase, and fatty acyl-coenzyme A oxidase. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
See also
ACOX1
ACOX3
References
EC 1.3.3
Flavoproteins
Enzymes of known structure |
https://en.wikipedia.org/wiki/All-trans-retinol%2013%2C14-reductase | In enzymology, an all-trans-retinol 13,14-reductase () is an enzyme, encoded by the RETSAT gene, that catalyzes the chemical reaction
all-trans-13,14-dihydroretinol + acceptor all-trans-retinol + reduced acceptor
Thus, the two substrates of this enzyme are all-trans-13,14-dihydroretinol and acceptor, whereas its two products are all-trans-retinol and reduced acceptor. Under physiological conditions the reaction proceeds in the opposite direction catalyzing the saturation of the 13-14 double bond of all-trans-retinol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is all-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase. Other names in common use include retinol saturase, RetSat, (13,14)-all-trans-retinol saturase, and all-trans-retinol:all-trans-13,14-dihydroretinol saturase.
The gene has also been called PPAR-alpha-regulated and starvation-induced gene protein.
References
Further reading
EC 1.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alpha-santonin%201%2C2-reductase | In enzymology, an alpha-santonin 1,2-reductase () is an enzyme that catalyzes the chemical reaction
1,2-dihydrosantonin + NAD(P)+ alpha-santonin + NAD(P)H + H+
The 3 substrates of this enzyme are 1,2-dihydrosantonin, NAD+, and NADP+, whereas its 4 products are alpha-santonin, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1,2-dihydrosantonin:NAD(P)+ 1,2-oxidoreductase.
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Anthocyanidin%20reductase | In enzymology, an anthocyanidin reductase () is an enzyme that catalyzes the chemical reaction
a flavan-3-ol + 2 NAD(P)+ an anthocyanidin + 2 NAD(P)H + H+
The 3 substrates of this enzyme are flavan-3-ol, NAD+, and NADP+, whereas its 4 products are anthocyanidin, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is flavan-3-ol:NAD(P)+ oxidoreductase. Other names in common use include AtANR, and MtANR. This enzyme participates in flavonoid biosynthesis.
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure
Flavanols metabolism
Anthocyanins metabolism |
https://en.wikipedia.org/wiki/Arogenate%20dehydrogenase | In enzymology, an arogenate dehydrogenase () is an enzyme that catalyzes the chemical reaction
L-arogenate + NAD+ L-tyrosine + NADH + CO2
Thus, the two substrates of this enzyme are L-arogenate and NAD+, whereas its 3 products are L-tyrosine, NADH, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arogenate:NAD+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), cyclohexadienyl dehydrogenase, pretyrosine dehydrogenase (ambiguous), and L-arogenate:NAD+ oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and novobiocin biosynthesis.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 1.3.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Arogenate%20dehydrogenase%20%28NAD%28P%29%2B%29 | In enzymology, an arogenate dehydrogenase [NAD(P)+] () is an enzyme that catalyzes the chemical reaction
L-arogenate + NAD(P)+ L-tyrosine + NAD(P)H + CO2
The 3 substrates of this enzyme are L-arogenate, NAD+, and NADP+, whereas its 4 products are L-tyrosine, NADH, NADPH, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arogenate:NAD(P)+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), cyclohexadienyl dehydrogenase, and pretyrosine dehydrogenase (ambiguous).
References
EC 1.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Arogenate%20dehydrogenase%20%28NADP%2B%29 | In enzymology, an arogenate dehydrogenase (NADP+) () is an enzyme that catalyzes the chemical reaction
L-arogenate + NADP+ L-tyrosine + NADPH + CO2
Thus, the two substrates of this enzyme are L-arogenate and NADP+, whereas its 3 products are L-tyrosine, NADPH, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-arogenate:NADP+ oxidoreductase (decarboxylating). Other names in common use include arogenic dehydrogenase (ambiguous), pretyrosine dehydrogenase (ambiguous), TyrAAT1, TyrAAT2, and TyrAa.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Benzoyl-CoA%20reductase | In enzymology, a benzoyl-CoA reductase () is an enzyme that catalyzes the chemical reaction
benzoyl-CoA + reduced acceptor + 2 ATP + 2 H2O cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2 phosphate
The 4 substrates of this enzyme are benzoyl-CoA, reduced acceptor, ATP, and H2O, whereas its 4 products are cyclohexa-1,5-diene-1-carbonyl-CoA, acceptor, ADP, and phosphate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is cyclohexa-1,5-diene-1-carbonyl-CoA:acceptor oxidoreductase (aromatizing, ATP-forming). This enzyme is also called benzoyl-CoA reductase (dearomatizing). This enzyme participates in benzoate degradation via CoA ligation. It has two cofactors: manganese, and magnesium.
References
EC 1.3.7
Manganese enzymes
Magnesium enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-nitroacrylate%20reductase | In enzymology, a beta-nitroacrylate reductase () is an enzyme that catalyzes the chemical reaction
3-nitropropanoate + NADP+ 3-nitroacrylate + NADPH + H+
Thus, the two substrates of this enzyme are 3-nitropropanoate and NADP+, whereas its 3 products are 3-nitroacrylate, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-nitropropanoate:NADP+ oxidoreductase.
References
EC 1.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
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