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https://en.wikipedia.org/wiki/Hydroxymethylglutaryl-CoA%20synthase | In molecular biology, hydroxymethylglutaryl-CoA synthase or HMG-CoA synthase is an enzyme which catalyzes the reaction in which acetyl-CoA condenses with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). This reaction comprises the second step in the mevalonate-dependent isoprenoid biosynthesis pathway. HMG-CoA is an intermediate in both cholesterol synthesis and ketogenesis. This reaction is overactivated in patients with diabetes mellitus type 1 if left untreated, due to prolonged insulin deficiency and the exhaustion of substrates for gluconeogenesis and the TCA cycle, notably oxaloacetate. This results in shunting of excess acetyl-CoA into the ketone synthesis pathway via HMG-CoA, leading to the development of diabetic ketoacidosis.
The 3 substrates of this enzyme are acetyl-CoA, H2O, and acetoacetyl-CoA, whereas its two products are (S)-3-hydroxy-3-methylglutaryl-CoA and CoA.
In humans, the protein is encoded by the HMGCS1 gene on chromosome 5.
Classification
This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer.
Nomenclature
The systematic name of this enzyme class is acetyl-CoA:acetoacetyl-CoA C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming). Other names in common use include (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetyl-CoA-lyase, (CoA-acetylating), 3-hydroxy-3-methylglutaryl CoA synthetase, 3-hydroxy-3-methylglutaryl coenzyme A synthase, |
https://en.wikipedia.org/wiki/Mark%20Hone | Mark Joseph Hone (born 31 March 1968) is an English, retired, professional footballer who played in the Football League for Crystal Palace, Southend United and Lincoln City. Has been manager of Spalding United whilst his son Danny had played for Lincoln City and is currently at conference north side North Ferriby United.
Hone has recently worked in the media. Working for BBC radio Lincolnshire he is a regular on the Football live phone in debate on a Tuesday and Friday discussing issues with Lincoln City and also local non-league sides in the area. Hone has also been the expert summariser on Lincoln City games.
Playing career
A combative midfielder or central defender, Hone began his career at Crystal Palace making eight first team appearances before dropping into the non-league ranks with Welling United. In 1994, he had a second chance in the football league when Southend United paid £50,000 to secure his services.
He spent two years with Southend before moving north to Lincoln City for a further two seasons winning promotion with Lincoln in 1998.
Return to Non-League
He then dropped back into non-league football with a season at Kettering Town followed by a return to Welling United.
Residing just outside Lincoln, Hone reduced his travel commitments by linking up with Lincoln United in the summer of 2003, making his Northern Premier League debut in the 4–1 home victory over Witton Albion on 16 August 2003.
In February 2006, Hone moved to Spalding United where he fulfil |
https://en.wikipedia.org/wiki/Icosanoyl-CoA%20synthase | In enzymology, an icosanoyl-CoA synthase () is an enzyme that catalyzes the chemical reaction
stearoyl-CoA + malonyl-CoA + 2 NAD(P)H + 2 H+ icosanoyl-CoA + CO2 + CoA + 2 NAD(P)+ + H2O
The 5 substrates of this enzyme are stearoyl-CoA, malonyl-CoA, NADH, NADPH, and H+, whereas its 6 products are icosanoyl-CoA, CO2, CoA, NAD+, NADP+, and H2O.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is stearoyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing). Other names in common use include acyl-CoA elongase, C18-CoA elongase, and stearoyl-CoA elongase.
References
EC 2.3.1
NADPH-dependent enzymes
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Imidazole%20N-acetyltransferase | In enzymology, an imidazole N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + imidazole CoA + N-acetylimidazole
Thus, the two substrates of this enzyme are acetyl-CoA and imidazole, whereas its two products are CoA and N-acetylimidazole.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:imidazole N-acetyltransferase. Other names in common use include imidazole acetylase, and imidazole acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Indoleacetylglucose%E2%80%94inositol%20O-acyltransferase | In enzymology, an indoleacetylglucose-inositol O-acyltransferase () is an enzyme that catalyzes the chemical reaction
1-O-(indol-3-yl)acetyl-beta-D-glucose + myo-inositol D-glucose + O-(indol-3-yl)acetyl-myo-inositol
Thus, the two substrates of this enzyme are 1-O-(indol-3-yl)acetyl-beta-D-glucose and myo-inositol, whereas its two products are D-glucose and O-(indol-3-yl)acetyl-myo-inositol.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 1-O-(indol-3-yl)acetyl-beta-D-glucose:myo-inositol (indol-3-yl)acetyltransferase. Other names in common use include indole-3-acetyl-beta-1-D-glucoside:myo-inositol, indoleacetyltransferase, 1-O-(indol-3-ylacetyl)-beta-D-glucose:myo-inositol, and indole-3-ylacetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isocitrate%20O-dihydroxycinnamoyltransferase | In enzymology, an isocitrate O-dihydroxycinnamoyltransferase () is an enzyme that catalyzes the chemical reaction
caffeoyl-CoA + isocitrate CoA + 2-caffeoylisocitrate
Thus, the two substrates of this enzyme are caffeoyl-CoA and isocitrate, whereas its two products are CoA and 2-caffeoylisocitrate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is caffeoyl-CoA:isocitrate 3-O-(3,4-dihydroxycinnamoyl)transferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isoflavone-7-O-beta-glucoside%206%22-O-malonyltransferase | In enzymology, an isoflavone-7-O-beta-glucoside 6"-O-malonyltransferase () is an enzyme that catalyzes the chemical reaction
malonyl-CoA + biochanin A 7-O-beta-D-glucoside CoA + biochanin A 7-O-(6-O-malonyl-beta-D-glucoside)
Thus, the two substrates of this enzyme are malonyl-CoA and biochanin A 7-O-beta-D-glucoside, whereas its two products are CoA and biochanin A 7-O-(6-O-malonyl-beta-D-glucoside).
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl-CoA:isoflavone-7-O-beta-D-glucoside 6"-O-malonyltransferase. Other names in common use include flavone/flavonol 7-O-beta-D-glucoside malonyltransferase, flavone (flavonol) 7-O-glycoside malonyltransferase, malonyl-CoA:flavone/flavonol 7-O-glucoside malonyltransferase, MAT-7, malonyl-coenzyme A:isoflavone 7-O-glucoside-6"-malonyltransferase, and malonyl-coenzyme A:flavone/flavonol-7-O-glycoside malonyltransferase. This enzyme participates in flavonoid biosynthesis and isoflavonoid biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure
Isoflavones metabolism |
https://en.wikipedia.org/wiki/Isopenicillin%20N%20N-acyltransferase | In enzymology, an isopenicillin N N-acyltransferase () is an enzyme that catalyzes the chemical reaction
phenylacetyl-CoA + isopenicillin N + H2O CoA + penicillin G + L-2-aminohexanedioate
The 3 substrates of this enzyme are phenylacetyl-CoA, isopenicillin N, and H2O, whereas its 3 products are CoA, penicillin G, and L-2-aminohexanedioate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:isopenicillin N N-acyltransferase. Other names in common use include acyl-coenzyme A:isopenicillin N acyltransferase, and isopenicillin N:acyl-CoA: acyltransferase. This enzyme participates in hydrophobic penicillins biosynthesis.
References
Further reading
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Leucine%20N-acetyltransferase | In enzymology, a leucine N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + L-leucine CoA + N-acetyl-L-leucine
Thus, the two substrates of this enzyme are acetyl-CoA and L-leucine, whereas its two products are CoA and N-acetyl-L-leucine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:L-leucine N-acetyltransferase. This enzyme is also called leucine acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Leucyltransferase | In enzymology, a leucyltransferase () is an enzyme that catalyzes the chemical reaction
L-leucyl-tRNA + protein tRNA + L-leucyl-protein
Thus, the two substrates of this enzyme are L-leucyl-tRNA and protein, whereas its two products are tRNA and L-leucyl-protein.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is L-leucyl-tRNA:protein leucyltransferase. Other names in common use include leucyl, phenylalanine-tRNA-protein transferase, leucyl-phenylalanine-transfer ribonucleate-protein, aminoacyltransferase, and leucyl-phenylalanine-transfer ribonucleate-protein transferase.
Structural studies
As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Lipoyl%28octanoyl%29%20transferase | In enzymology, a lipoyl(octanoyl) transferase () is an enzyme that catalyzes the chemical reaction
octanoyl-[acyl-carrier-protein] + protein protein N6-(octanoyl)lysine + acyl carrier protein
Thus, the two substrates of this enzyme are octanoyl-[acyl-carrier-protein] and protein, whereas its two products are protein N6-(octanoyl)lysine and acyl carrier protein.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase. Other names in common use include LipB, lipoyl (octanoyl)-[acyl-carrier-protein]-protein, N-lipoyltransferase, lipoyl (octanoyl)-acyl carrier protein:protein transferase, lipoate/octanoate transferase, lipoyltransferase, octanoyl-[acyl carrier protein]-protein N-octanoyltransferase, and lipoyl(octanoyl)transferase. This enzyme participates in lipoic acid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Long-chain-alcohol%20O-fatty-acyltransferase | In enzymology, a long-chain-alcohol O-fatty-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + a long-chain alcohol CoA + a long-chain ester
Thus, the two substrates of this enzyme are acyl-CoA and long-chain alcohol, whereas its two products are CoA and long-chain ester.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:long-chain-alcohol O-acyltransferase. Other names in common use include wax synthase, and wax-ester synthase. In general, wax syntheses naturally accept acyl groups with carbon chain lengths of C16 or C18 and linear alcohols with carbon chain lengths ranging from C12 to C20.
Variation
There are three unrelated families of wax syntheses found in many organisms including bacteria, higher plants, and animals in two known distinct forms: either just as a wax synthase enzyme, which is found predominantly in eukaryotes, or as an enzyme with dual wax synthase and acyl CoA:diacylglycerol acyltransferase function, which is often the final enzyme in the biosynthetic pathway responsible for wax ester production from fatty alcohols and fatty acyl-CoAs and is found predominantly in prokaryotes.
Prokaryotic bacteria
Acinetobacter
There are frequent reports of wax esters biosynthesis in bacteria of the Acinetobacter genus. In particular, it has been shown that the Acinetobacter calcoaceticus ADP1 s |
https://en.wikipedia.org/wiki/Lovastatin%20nonaketide%20synthase | In enzymology, lovastatin nonaketide synthase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + 8 malonyl-CoA + 11 NADPH + 10 H+ + S-adenosyl-L-methionine dihydromonacolin L + 9 CoA + 8 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
The 5 substrates of this enzyme are acetyl-CoA, malonyl-CoA, NADPH, H+, and S-adenosyl-L-methionine, whereas its 6 products are dihydromonacolin L, CoA, CO2, NADP+, S-adenosyl-L-homocysteine, and H2O.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing, thioester-hydrolysing).
References
EC 2.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lysine%20N-acetyltransferase | In enzymology, a lysine N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl phosphate + L-lysine phosphate + N6-acetyl-L-lysine
Thus, the two substrates of this enzyme are acetyl phosphate and L-lysine, whereas its two products are phosphate and N6-acetyl-L-lysine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-phosphate:L-lysine N6-acetyltransferase. Other names in common use include lysine acetyltransferase, and acetyl-phosphate:L-lysine 6-N-acetyltransferase. This enzyme participates in lysine degradation.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lysyltransferase | In enzymology, a lysyltransferase () is an enzyme that catalyzes the chemical reaction
L-lysyl-tRNA + phosphatidylglycerol tRNA + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
Thus, the two substrates of this enzyme are L-lysyl-tRNA and phosphatidylglycerol, whereas its two products are tRNA and 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is L-lysyl-tRNA:phosphatidylglycerol 3-O-lysyltransferase.
References
EC 2.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Malate%20synthase | In enzymology, a malate synthase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + H2O + glyoxylate (S)-malate + CoA
The 3 substrates of this enzyme are acetyl-CoA, H2O, and glyoxylate, whereas its two products are (S)-malate and CoA. This enzyme participates in pyruvate metabolism and glyoxylate and dicarboxylate metabolism.
Nomenclature
This enzyme belongs to the family of transferases, specifically acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming). Other names in common use include L-malate glyoxylate-lyase (CoA-acetylating), glyoxylate transacetylase, glyoxylate transacetase, glyoxylic transacetase, malate condensing enzyme, malate synthetase, malic synthetase, and malic-condensing enzyme.
Structure
Malate synthases fall into two major families, isoforms A and G. Isoform G is monomeric with a size of about 80-kD and found exclusively in bacteria. Isoform A is about 65 kD per subunit and can form homomultimers in eukaryotes. This enzyme contains a central TIM barrel sandwiched between an N-terminal alpha-helical clasp and an alpha/beta domain stemming from two insertions into the TIM barrel sequence. The enzyme terminates with a C-terminal five-helix plug. The active site, where the acetyl-CoA and glyoxylate bind to the enzyme, lies between the TIM barrel and C-terminal plug. Upon binding, the a |
https://en.wikipedia.org/wiki/Maltose%20O-acetyltransferase | In enzymology, a maltose O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + maltose CoA + 6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-D-glucose
Thus, the two substrates of this enzyme are acetyl-CoA and maltose, whereas its two products are CoA and [[6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-D-glucose]].
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:maltose O-acetyltransferase. Other names in common use include maltose transacetylase, maltose O-acetyltransferase, and MAT.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Monoterpenol%20O-acetyltransferase | In enzymology, a monoterpenol O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + a monoterpenol CoA + a monoterpenol acetate ester
Thus, the two substrates of this enzyme are acetyl-CoA and monoterpenol, whereas its two products are CoA and monoterpenol acetate ester.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:monoterpenol O-acetyltransferase. This enzyme is also called menthol transacetylase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CXCR6 | C-X-C chemokine receptor type 6 is a protein that in humans is encoded by the CXCR6 gene. CXCR6 has also recently been designated CD186 (cluster of differentiation 186).
CXCR6 has been identified as an entry coreceptor used by HIV-1 and SIV to enter target cells, in conjunction with CD4. It is a minor coreceptor for HIV-1, nearly all strains of which use CCR5 and/or CXCR4. Most SIV strains can use CXCR6 and recent evidence suggests that in monkeys that serve as the natural hosts of SIV, CXCR6 may be a major coreceptor. CXCR6 was previously known as "Bonzo" and "STRL33" in the HIV/SIV field.
References
Further reading
External links
Clusters of differentiation
Chemokine receptors |
https://en.wikipedia.org/wiki/Mycocerosate%20synthase | In enzymology, a mycocerosate synthase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + n methylmalonyl-CoA + 2n NADPH + 2n H+ multi-methyl-branched acyl-CoA + n CoA + n CO2 + 2n NADP+
The 4 substrates of this enzyme are acyl-CoA, methylmalonyl-CoA, NADPH, and H+, whereas its 4 products are multi-methyl-branched acyl-CoA, CoA, CO2, and NADP+.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:methylmalonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing). This enzyme is also called mycocerosic acid synthase.
References
EC 2.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28myelin-proteolipid%29%20O-palmitoyltransferase | In enzymology, a [myelin-proteolipid] O-palmitoyltransferase () is an enzyme that catalyzes the chemical reaction
palmitoyl-CoA + [myelin proteolipid] CoA + O-palmitoyl-[myelin proteolipid]
Thus, the two substrates of this enzyme are palmitoyl-CoA and myelin proteolipid, whereas its two products are CoA and O-palmitoyl-myelin proteolipid.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is palmitoyl-CoA:[myelin-proteolipid] O-palmitoyltransferase. Other names in common use include myelin PLP acyltransferase, acyl-protein synthetase, and myelin-proteolipid O-palmitoyltransferase.
References
EC 2.3.1
Enzymes of unknown structure
Enzymes |
https://en.wikipedia.org/wiki/N6-hydroxylysine%20O-acetyltransferase | In enzymology, a N6-hydroxylysine O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + N6-hydroxy-L-lysine CoA + N6-acetyl-N6-hydroxy-L-lysine
Thus, the two substrates of this enzyme are acetyl-CoA and N6-hydroxy-L-lysine, whereas its two products are CoA and N6-acetyl-N6-hydroxy-L-lysine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:N6-hydroxy-L-lysine 6-acetyltransferase. Other names in common use include N6-hydroxylysine:acetyl CoA N6-transacetylase, N6-hydroxylysine acetylase, and acetyl-CoA:6-N-hydroxy-L-lysine 6-acetyltransferase. This enzyme participates in lysine degradation.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CCRL2 | C-C chemokine receptor-like 2 is a protein that in humans is encoded by the CCRL2 gene. Recently it was found that CCRL2 also acts as a receptor for the chemokine chemerin.
Function
This gene encodes a chemokine receptor like protein, which is predicted to be a seven transmembrane protein and most closely related to CCR1. Chemokines and their receptors mediated signal transduction are critical for the recruitment of effector immune cells to the site of inflammation. This gene is expressed at high levels in primary neutrophils and primary monocytes, and is further upregulated on neutrophil activation and during monocyte to macrophage differentiation. The function of this gene is unknown. This gene is mapped to the region where the chemokine receptor gene cluster is located.
References
External links
Further reading
Chemokine receptors |
https://en.wikipedia.org/wiki/LPAR3 | Lysophosphatidic acid receptor 3 also known as LPA3 is a protein that in humans is encoded by the LPAR3 gene. LPA3 is a G protein-coupled receptor that binds the lipid signaling molecule lysophosphatidic acid (LPA).
Function
This gene encodes a member of the G protein-coupled receptor family, as well as the EDG family of proteins. This protein functions as a cellular receptor for lysophosphatidic acid and mediates lysophosphatidic acid-evoked calcium mobilization. This receptor couples predominantly to G(q/11) alpha proteins.
See also
Lysophospholipid receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/N-acetylneuraminate%204-O-acetyltransferase | In enzymology, a N-acetylneuraminate 4-O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + N-acetylneuraminate CoA + N-acetyl-4-O-acetylneuraminate
Thus, the two substrates of this enzyme are acetyl-CoA and N-acetylneuraminate, whereas its two products are CoA and N-acetyl-4-O-acetylneuraminate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:N-acetylneuraminate 4-O-acetyltransferase. This enzyme is also called sialate O-acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetylneuraminate%207-O%28or%209-O%29-acetyltransferase | In enzymology, a N-acetylneuraminate 7-O(or 9-O)-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + N-acetylneuraminate CoA + N-acetyl-7-O(or 9-O)-acetylneuraminate
Thus, the two substrates of this enzyme are acetyl-CoA and N-acetylneuraminate, whereas its 3 products are CoA, N-acetyl-7-O-acetylneuraminate, and N-acetyl-9-O-acetylneuraminate.
Nomenclature
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:N-acetylneuraminate 7-O(or 9-O)-acetyltransferase. Other names in common use include N-acetylneuraminate 7(8)-O-acetyltransferase, sialate O-acetyltransferase, N-acetylneuraminate 7,8-O-acetyltransferase, acetyl-CoA:N-acetylneuraminate-7- or 8-O-acetyltransferase, acetyl-CoA:N-acetylneuraminate-7- and/or 8-O-acetyltransferase, glycoprotein 7(9)-O-acetyltransferase, acetyl-CoA:N-acetylneuraminate-9(7)-O-acetyltransferase, N-acetylneuraminate O7-(or O9-)acetyltransferase, and acetyl-CoA:N-acetylneuraminate-9(or 7)-O-acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-hydroxyarylamine%20O-acetyltransferase | In enzymology, a N-hydroxyarylamine O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + an N-hydroxyarylamine CoA + an N-acetoxyarylamine
Thus, the two substrates of this enzyme are acetyl-CoA and N-hydroxyarylamine, whereas its two products are CoA and N-acetoxyarylamine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:N-hydroxyarylamine O-acetyltransferase. Other names in common use include arylhydroxamate N,O-acetyltransferase, arylamine N-acetyltransferase, and N-hydroxy-2-aminofluorene-O-acetyltransferase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Ornithine%20N-benzoyltransferase | In enzymology, an ornithine N-benzoyltransferase () is an enzyme that catalyzes the chemical reaction
2 benzoyl-CoA + L-ornithine 2 CoA + N2,N5-dibenzoyl-L-ornithine
Thus, the two substrates of this enzyme are benzoyl-CoA and L-ornithine, whereas its two products are CoA and N2,N5-dibenzoyl-L-ornithine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is benzoyl-CoA:L-ornithine N-benzoyltransferase. This enzyme is also called ornithine N-acyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Peptide%20alpha-N-acetyltransferase | In enzymology, a peptide alpha-N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + peptide Nalpha-acetylpeptide + CoA
Thus, the two substrates of this enzyme are acetyl-CoA and peptide, whereas its two products are Nalpha-acetylpeptide and CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:peptide Nalpha-acetyltransferase. Other names in common use include beta-endorphin acetyltransferase, peptide acetyltransferase, protein N-terminal acetyltransferase, NAT, Nalpha-acetyltransferase, amino-terminal amino acid-acetylating enzyme, and acetyl-CoA:peptide alpha-N-acetyltransferase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phenylalanine%20N-acetyltransferase | In enzymology, a phenylalanine N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + L-phenylalanine CoA + N-acetyl-L-phenylalanine
Thus, the two substrates of this enzyme are acetyl-CoA and L-phenylalanine, whereas its two products are CoA and N-acetyl-L-phenylalanine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:L-phenylalanine N-acetyltransferase. This enzyme is also called acetyl-CoA-L-phenylalanine alpha-N-acetyltransferase. This enzyme participates in phenylalanine metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phloroisovalerophenone%20synthase | In enzymology, a phloroisovalerophenone synthase () is an enzyme that catalyzes the chemical reaction
isovaleryl-CoA + 3 malonyl-CoA 4 CoASH + 3 CO2 + 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one
Thus, the two substrates of this enzyme are isovaleryl-CoA and malonyl-CoA, whereas its 3 products are CoASH, CO2, and 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is isovaleryl-CoA:malonyl-CoA acyltransferase. Other names in common use include valerophenone synthase, and 3-methyl-1-(trihydroxyphenyl)butan-1-one synthase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphate%20acetyltransferase | In enzymology, a phosphate acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + phosphate CoA + acetyl phosphate
The substrates of this enzyme are acetyl-CoA and phosphate, whereas its two products are CoA and acetyl phosphate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:phosphate acetyltransferase. Other names in common use include phosphotransacetylase, phosphoacylase, and PTA. This enzyme participates in 3 metabolic pathways: taurine and hypotaurine metabolism, pyruvate metabolism, and propanoate metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 2.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phosphate%20butyryltransferase | In enzymology, a phosphate butyryltransferase () is an enzyme that catalyzes the chemical reaction
butanoyl-CoA + phosphate CoA + butanoyl phosphate
Thus, the two substrates of this enzyme are butanoyl-CoA and phosphate, whereas its two products are CoA and butanoyl phosphate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is butanoyl-CoA:phosphate butanoyltransferase. This enzyme is also called phosphotransbutyrylase. This enzyme participates in butanoate metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylcholine%E2%80%94dolichol%20O-acyltransferase | In enzymology, a phosphatidylcholine---dolichol O-acyltransferase () is an enzyme that catalyzes the chemical reaction
3-sn-phosphatidylcholine + dolichol 1-acyl-sn-glycero-3-phosphocholine + acyldolichol
Thus, the two substrates of this enzyme are 3-sn-phosphatidylcholine and dolichol, whereas its two products are 1-acyl-sn-glycero-3-phosphocholine and acyldolichol.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 3-sn-phosphatidylcholine:dolichol O-acyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylcholine%E2%80%94retinol%20O-acyltransferase | In enzymology, a phosphatidylcholine---retinol O-acyltransferase () is an enzyme that catalyzes the chemical reaction
phosphatidylcholine + retinol---[cellular-retinol-binding-protein] 2-acylglycerophosphocholine + retinyl-ester---[cellular-retinol-binding-protein]
Thus, the two substrates of this enzyme are phosphatidylcholine and [[retinol---[cellular-retinol-binding-protein]]], whereas its two products are 2-acylglycerophosphocholine and [[retinyl-ester---[cellular-retinol-binding-protein]]].
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is phosphatidylcholine:retinol---[cellular-retinol-binding-protein] O-acyltransferase. Other names in common use include lecithin---retinol acyltransferase, phosphatidylcholine:retinol-(cellular-retinol-binding-protein), and O-acyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylcholine%E2%80%94sterol%20O-acyltransferase | In enzymology, a phosphatidylcholine---sterol O-acyltransferase () is an enzyme that catalyzes the chemical reaction
phosphatidylcholine + a sterol 1-acylglycerophosphocholine + a sterol ester
Thus, the two substrates of this enzyme are phosphatidylcholine and sterol, whereas its two products are 1-acylglycerophosphocholine and sterol ester.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is phosphatidylcholine:sterol O-acyltransferase. Other names in common use include lecithin---cholesterol acyltransferase, phospholipid---cholesterol acyltransferase, LCAT (lecithin-cholesterol acyltransferase), lecithin:cholesterol acyltransferase, and lysolecithin acyltransferase. This enzyme participates in glycerophospholipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure
it:Fosfatidilcolina-sterolo O-aciltransferasi |
https://en.wikipedia.org/wiki/Phospholipid%3Adiacylglycerol%20acyltransferase | In enzymology, a phospholipid:diacylglycerol acyltransferase () is an enzyme that catalyzes the chemical reaction
phospholipid + 1,2-diacylglycerol lysophospholipid + triacylglycerol
Thus, the two substrates of this enzyme are phospholipid and 1,2-diacylglycerol, whereas its two products are lysophospholipid and triacylglycerol.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is phospholipid:1,2-diacyl-sn-glycerol O-acyltransferase. This enzyme is also called PDAT. This enzyme participates in glycerolipid metabolism.
An important human protein from this family is lecithin–cholesterol acyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pinosylvin%20synthase | In enzymology, a pinosylvin synthase () is an enzyme that catalyzes the chemical reaction
3 malonyl-CoA + cinnamoyl-CoA 4 CoA + pinosylvin + 4 CO2
Thus, the two substrates of this enzyme are malonyl-CoA and cinnamoyl-CoA, whereas its 3 products are CoA, pinosylvin, and CO2.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl-CoA:cinnamoyl-CoA malonyltransferase (cyclizing). Other names in common use include stilbene synthase, and pine stilbene synthase. This enzyme participates in phenylpropanoid biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure
Stilbenoids metabolism |
https://en.wikipedia.org/wiki/Piperidine%20N-piperoyltransferase | In enzymology, a piperidine N-piperoyltransferase () is an enzyme that catalyzes the chemical reaction
(E,E)-piperoyl-CoA + piperidine CoA + N-[(E,E)-piperoyl]-piperidine
Thus, the two substrates of this enzyme are (E,E)-piperoyl-CoA and piperidine, whereas its two products are CoA and [[N-[(E,E)-piperoyl]-piperidine]].
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is (E,E)-piperoyl-CoA:piperidine N-piperoyltransferase. Other names in common use include piperidine piperoyltransferase, and piperoyl-CoA:piperidine N-piperoyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Plasmalogen%20synthase | In enzymology, a plasmalogen synthase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + 1-O-alk-1-enyl-glycero-3-phosphocholine CoA + plasmenylcholine
Thus, the two substrates of this enzyme are acyl-CoA and 1-O-alk-1-enyl-glycero-3-phosphocholine, whereas its two products are CoA and plasmenylcholine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:1-O-alk-1-enyl-glycero-3-phosphocholine 2-O-acyltransferase. Other names in common use include lysoplasmenylcholine acyltransferase, O-1-alkenylglycero-3-phosphorylcholine acyltransferase, and 1-alkenyl-glycero-3-phosphorylcholine:acyl-CoA acyltransferase. This enzyme participates in ether lipid metabolism.
See also
1-alkenylglycerophosphocholine O-acyltransferase
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Platelet-activating%20factor%20acetyltransferase | In enzymology, a platelet-activating factor acetyltransferase () is an enzyme that catalyzes the chemical reaction
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phospholipid 1-organyl-2-lyso-sn-glycero-3-phosphocholine + 1-alkyl-2-acetyl-sn-glycero-3-phospholipid
Thus, the two substrates of this enzyme are 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine and 1-organyl-2-lyso-sn-glycero-3-phospholipid, whereas its two products are 1-organyl-2-lyso-sn-glycero-3-phosphocholine and 1-alkyl-2-acetyl-sn-glycero-3-phospholipid.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 1-alkyl-2-acyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-glyce ro-3-phospholipid acetyltransferase. This enzyme is also called PAF acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Polysialic-acid%20O-acetyltransferase | In enzymology, a polysialic-acid O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + an alpha-2,8-linked polymer of sialic acid CoA + polysialic acid acetylated on O-7 or O-9
Thus, the two substrates of this enzyme are acetyl-CoA and alpha-2,8-linked polymer of sialic acid, whereas its 3 products are CoA, polysialic acid acetylated on O-7, and polysialic acid acetylated on O-9.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:polysialic-acid O-acetyltransferase. Other names in common use include lecithin:retinol acyltransferase, lecithin-retinol acyltransferase, retinyl ester synthase, LRAT, and lecithin retinol acyl transferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Propanoyl-CoA%20C-acyltransferase | In enzymology, a propanoyl-CoA C-acyltransferase () is an enzyme that catalyzes the chemical reaction
3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA + propanoyl-CoA CoA + 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA
Thus, the two substrates of this enzyme are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA and propanoyl-CoA, whereas its two products are CoA and 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestanoyl-CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanoyl-CoA:propanoyl-CoA C-acyltransferase. Other names in common use include peroxisomal thiolase 2, sterol carrier protein-, SCP, and PTE-2 (ambiguous). This enzyme participates in ppar signaling pathway.
Propanoyl-CoA C-acyltransferase belongs to the thiolase family of enzymes.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Propionyl-CoA%20C2-trimethyltridecanoyltransferase | In enzymology, a propionyl-CoA C2-trimethyltridecanoyltransferase () is an enzyme that catalyzes the chemical reaction
4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA 3-oxopristanoyl-CoA + CoA
Thus, the two substrates of this enzyme are 4,8,12-trimethyltridecanoyl-CoA and propanoyl-CoA, whereas its two products are 3-oxopristanoyl-CoA and CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 4,8,12-trimethyltridecanoyl-CoA:propanoyl-CoA C2-4,8,12-trimethyltridecanoyltransferase. Other names in common use include 3-oxopristanoyl-CoA hydrolase, 3-oxopristanoyl-CoA thiolase, peroxisome sterol carrier protein thiolase, sterol carrier protein, oxopristanoyl-CoA thiolase, peroxisomal 3-oxoacyl coenzyme A thiolase, SCPx, 4,8,12-trimethyltridecanoyl-CoA:propanoyl-CoA, and 2-C-4,8,12-trimethyltridecanoyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Putrescine%20N-hydroxycinnamoyltransferase | In enzymology, a putrescine N-hydroxycinnamoyltransferase () is an enzyme that catalyzes the chemical reaction
caffeoyl-CoA + putrescine CoA + N-caffeoylputrescine
Thus, the two substrates of this enzyme are caffeoyl-CoA and putrescine, whereas its two products are CoA and N-caffeoylputrescine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is caffeoyl-CoA:putrescine N-(3,4-dihydroxycinnamoyl)transferase. Other names in common use include caffeoyl-CoA putrescine N-caffeoyl transferase, PHT, putrescine hydroxycinnamoyl transferase, hydroxycinnamoyl-CoA:putrescine hydroxycinnamoyltransferase, and putrescine hydroxycinnamoyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Quinate%20O-hydroxycinnamoyltransferase | In enzymology, a quinate O-hydroxycinnamoyltransferase () is an enzyme that catalyzes the chemical reaction
feruloyl-CoA + quinate CoA + O-feruloylquinate
Thus, the two substrates of this enzyme are feruloyl-CoA and quinate, whereas its two products are CoA and O-feruloylquinate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is feruloyl-CoA:quinate O-(hydroxycinnamoyl)transferase. This enzyme is also called hydroxycinnamoyl coenzyme A-quinate transferase. This enzyme participates in phenylpropanoid biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/Retinol%20O-fatty-acyltransferase | In enzymology, a retinol O-fatty-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + retinol CoA + retinyl ester
Thus, the two substrates of this enzyme are acyl-CoA and retinol, whereas its two products are CoA and retinyl ester.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:retinol O-acyltransferase. Other names in common use include retinol acyltransferase, and retinol fatty-acyltransferase. This enzyme participates in retinol metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ribosomal-protein-alanine%20N-acetyltransferase | In enzymology, a ribosomal-protein-alanine N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + ribosomal-protein L-alanine CoA + ribosomal-protein N-acetyl-L-alanine
Thus, the two substrates of this enzyme are acetyl-CoA and ribosomal-protein L-alanine, whereas its two products are CoA and ribosomal-protein N-acetyl-L-alanine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:ribosomal-protein-L-alanine N-acetyltransferase. This enzyme is also called ribosomal protein S18 acetyltransferase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Rosmarinate%20synthase | In enzymology, a rosmarinate synthase () is an enzyme that catalyzes the chemical reaction
caffeoyl-CoA + 3-(3,4-dihydroxyphenyl)lactate CoA + rosmarinate
Thus, the two substrates of this enzyme are caffeoyl-CoA and 3-(3,4-dihydroxyphenyl)lactate, whereas its two products are CoA and rosmarinate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is caffeoyl-CoA:3-(3,4-dihydroxyphenyl)lactate 2'-O-caffeoyl-transferase. Other names in common use include rosmarinic acid synthase, caffeoyl-coenzyme A:3,4-dihydroxyphenyllactic acid, caffeoyltransferase, and 4-coumaroyl-CoA:4-hydroxyphenyllactic acid 4-coumaroyl transferase. This enzyme participates in tyrosine metabolism.
References
EC 2.3.1
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/Salutaridinol%207-O-acetyltransferase | In enzymology, a salutaridinol 7-O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + salutaridinol CoA + 7-O-acetylsalutaridinol
Thus, the two substrates of this enzyme are acetyl-CoA and salutaridinol, whereas its two products are CoA and 7-O-acetylsalutaridinol.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:salutaridinol 7-O-acetyltransferase. This enzyme participates in alkaloid biosynthesis i.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Serine%20C-palmitoyltransferase | In enzymology, a serine C-palmitoyltransferase () is an enzyme that catalyzes the chemical reaction:
palmitoyl-CoA + L-serine CoA + 3-dehydro-D-sphinganine + CO2
Thus, the two substrates of this enzyme are palmitoyl-CoA and L-serine, whereas its 3 products are CoA, 3-dehydro-D-sphinganine, and CO2. This reaction is a key step in the biosynthesis of sphingosine which is a precursor of many other sphingolipids.
This enzyme participates in sphingolipid metabolism. It employs one cofactor, pyridoxal phosphate.
Nomenclature
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is palmitoyl-CoA:L-serine C-palmitoyltransferase (decarboxylating). Other names in common use include:
serine palmitoyltransferase,
SPT, 3-oxosphinganine synthetase, and
acyl-CoA:serine C-2 acyltransferase decarboxylating.
Structure
Serine C-palmitoyltransferase is a member of the AOS (a-oxoamine synthase) family of PLP-dependent enzymes, which catalyse the condensation of amino acids and acyl-CoA thioester substrates. The human enzyme is a heterodimer consisting of two monomeric subunits known as long chain base 1 and 2 (LCB1/2) encoded by separate genes. The active site of LCB2 contains lysine and other key catalytic residues that are not present in LCB1, which does not participate in catalysis but is nevertheless required for the synthesis and stability of the enzyme. |
https://en.wikipedia.org/wiki/Serine%20O-acetyltransferase | In enzymology, a serine O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + L-serine CoA + O-acetyl-L-serine
Thus, the two substrates of this enzyme are acetyl-CoA and L-serine, whereas its two products are CoA and O-acetyl-L-serine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:L-serine O-acetyltransferase. Other names in common use include SATase, L-serine acetyltransferase, serine acetyltransferase, and serine transacetylase. This enzyme participates in cysteine metabolism and sulfur metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
N terminal protein domain
In molecular biology, the protein domain SATase is short for Serine acetyltransferase and refers to an enzyme that catalyses the conversion of L-serine to L-cysteine in E. coli. More specifically, its role is to catalyse the activation of L-serine by acetyl-CoA.This entry refers to the N-terminus of the protein which has a sequence that is conserved in plants and bacteria.
Importance of function
The N-terminal domain of the protein Serine acetyltransferase helps catalyse acetyl transfer. This particular enzyme catalyses serine into cysteine which is eventually converted to the essential amino acid methionine. Of particular interest to |
https://en.wikipedia.org/wiki/Shikimate%20O-hydroxycinnamoyltransferase | In enzymology, a shikimate O-hydroxycinnamoyltransferase () is an enzyme that catalyzes the chemical reaction
4-coumaroyl-CoA + shikimate CoA + 4-coumaroylshikimate
Thus, the two substrates of this enzyme are 4-coumaroyl-CoA and shikimate, whereas its two products are CoA and 4-coumaroylshikimate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 4-coumaroyl-CoA:shikimate O-(hydroxycinnamoyl)transferase. This enzyme is also called shikimate hydroxycinnamoyltransferase. This enzyme participates in phenylpropanoid biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/Sinapoylglucose%E2%80%94choline%20O-sinapoyltransferase | In enzymology, a sinapoylglucose---choline O-sinapoyltransferase () is an enzyme that catalyzes the chemical reaction
1-O-sinapoyl-beta-D-glucose + choline D-glucose + sinapoylcholine
Thus, the two substrates of this enzyme are 1-O-sinapoyl-beta-D-glucose and choline, whereas its two products are D-glucose and sinapoylcholine (sinapine).
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)-beta-D-glucose:choline 1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)transferase. This enzyme is also called sinapine synthase. This enzyme participates in phenylpropanoid biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sinapoylglucose%E2%80%94malate%20O-sinapoyltransferase | In enzymology, a sinapoylglucose---malate O-sinapoyltransferase () is an enzyme that catalyzes the chemical reaction
1-O-sinapoyl-beta-D-glucose + (S)-malate D-glucose + sinapoyl-(S)-malate
Thus, the two substrates of this enzyme are 1-O-sinapoyl-beta-D-glucose and (S)-malate, whereas its two products are D-glucose and sinapoyl-(S)-malate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 1-O-sinapoyl-beta-D-glucose:(S)-malate O-sinapoyltransferase. Other names in common use include 1-sinapoylglucose-L-malate sinapoyltransferase, and sinapoylglucose:malate sinapoyltransferase. This enzyme participates in phenylpropanoid biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure
Hydroxycinnamic acids metabolism |
https://en.wikipedia.org/wiki/Sinapoylglucose%E2%80%94sinapoylglucose%20O-sinapoyltransferase | In enzymology, a sinapoylglucose---sinapoylglucose O-sinapoyltransferase () is an enzyme that catalyzes the chemical reaction
2 1-O-sinapoyl beta-D-glucoside D-glucose + 1,2-bis-O-sinapoyl beta-D-glucoside
Hence, this enzyme has one substrate, 1-O-sinapoyl beta-D-glucoside, and two products, D-glucose and 1,2-bis-O-sinapoyl beta-D-glucoside.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 1-O-(4-hydroxy-3,5-dimethoxycinnamoyl)-beta-D-glucoside:1-O-(4-hydro xy-3,5-dimethoxycinnamoyl-beta-D-glucoside 1-O-sinapoyltransferase. Other names in common use include hydroxycinnamoylglucose-hydroxycinnamoylglucose, hydroxycinnamoyltransferase, 1-(hydroxycinnamoyl)-glucose:1-(hydroxycinnamoyl)-glucose, and hydroxycinnamoyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sphingosine%20N-acyltransferase | In enzymology, sphingosine N-acyltransferases (ceramide synthases (CerS), ) are enzymes that catalyze the chemical reaction of synthesis of ceramide:
acyl-CoA + sphingosine CoA + N-acylsphingosine
Thus, the two substrates of this enzyme are acyl-CoA and sphingosine, whereas its two products are CoA and N-acylsphingosine.
Ceramide synthases are integral membrane proteins of the endoplasmic reticulum.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:sphingosine N-acyltransferase. Other names in common use include ceramide synthetase, and sphingosine acyltransferase. This enzyme participates in sphingolipid metabolism.
History
CerS were originally called Lass (Longevity assurance) genes because of their homology to the yeast protein, longevity assurance gene-1 (LAG1p), and they were later renamed due to the discovery of their biological function.
LAG1 in yeast was discovered in 1994 and named for the discovery that its deletion prolonged life span of Saccharomyces cerevisiae by almost 50%. In the following years, it and its homologs were shown to be required for the syntheses of ceramides found in yeast. Three years previously, the mammalian gene upstream of growth and differentiation factor-1 (UOG-1) was discovered, but it wasn't until 2005 that it was defined as the first mammalian CerS, when Sujoy Lahiri and Tony Futerman from th |
https://en.wikipedia.org/wiki/Sterol%20O-acyltransferase | Sterol O-acyltransferase (also called Acyl-CoA cholesterol acyltransferase, Acyl-CoA cholesterin acyltransferase or simply ACAT) is an intracellular protein located in the endoplasmic reticulum that forms cholesteryl esters from cholesterol.
Sterol O-acyltransferase catalyzes the chemical reaction:
acyl-CoA + cholesterol CoA + cholesterol ester
Thus, the two substrates of this enzyme are acyl-CoA and cholesterol, whereas its two products are CoA and cholesteryl ester.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups, the membrane-bound O-acyltransferases. This enzyme participates in bile acid biosynthesis.
Class and structure
Acyl-CoA cholesterol acyl transferase , more simply referred to as ACAT, also known as sterol O-acyltransferase (SOAT), belongs to the class of enzymes known as acyltransferases. The role of this enzyme is to transfer fatty acyl groups from one molecule to another. ACAT is an important enzyme in bile acid biosynthesis.
In nearly all mammalian cells, ACAT catalyzes the intracellular esterification of cholesterol and formation of cholesteryl esters. The esterification of cholesterol mediated by ACAT is functionally significant for several reasons. ACAT-mediated esterification of cholesterol limits its solubility in the cell membrane lipids and thus promotes accumulation of cholesterol ester in the fat droplets within cytoplasm; this process is important becaus |
https://en.wikipedia.org/wiki/Sulfoacetaldehyde%20acetyltransferase | In enzymology, a sulfoacetaldehyde acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl phosphate + sulfite 2-sulfoacetaldehyde + phosphate
Thus, the two substrates of this enzyme are acetyl phosphate and sulfite, whereas its two products are 2-sulfoacetaldehyde and phosphate.
This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-phosphate:sulfite S-acetyltransferase (acyl-phosphate hydrolysing, 2-oxoethyl-forming). This enzyme is also called Xsc. This enzyme participates in taurine and hypotaurine metabolism.
References
EC 2.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tartronate%20O-hydroxycinnamoyltransferase | In enzymology, a tartronate O-hydroxycinnamoyltransferase () is an enzyme that catalyzes the chemical reaction
sinapoyl-CoA + 2-hydroxymalonate CoA + sinapoyltartronate
Thus, the two substrates of this enzyme are sinapoyl-CoA and 2-hydroxymalonate, whereas its two products are CoA and sinapoyltartronate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is sinapoyl-CoA:2-hydroxymalonate O-(hydroxycinnamoyl)transferase. Other names in common use include tartronate sinapoyltransferase, and hydroxycinnamoyl-coenzyme-A:tartronate hydroxycinnamoyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Taxadien-5alpha-ol%20O-acetyltransferase | In enzymology, a taxadien-5alpha-ol O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + taxa-4(20),11-dien-5alpha-ol CoA + taxa-4(20),11-dien-5alpha-yl acetate
Thus, the two substrates of this enzyme are acetyl-CoA and taxa-4(20),11-dien-5alpha-ol, whereas its two products are CoA and taxa-4(20),11-dien-5alpha-yl acetate.
This enzyme participates in diterpenoid biosynthesis.
Nomenclature
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:taxa-4(20),11-dien-5alpha-ol O-acetyltransferase. Other names in common use include acetyl coenzyme A:taxa-4(20),11(12)-dien-5alpha-ol O-acetyl, and transferase.
References
Further reading
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tetrahydrodipicolinate%20N-acetyltransferase | In enzymology, a tetrahydrodipicolinate N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O CoA + L-2-acetamido-6-oxoheptanedioate
The 3 substrates of this enzyme are acetyl-CoA, (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, and H2O, whereas its two products are CoA and L-2-acetamido-6-oxoheptanedioate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N2-acetyltransferase. Other names in common use include tetrahydrodipicolinate acetylase, tetrahydrodipicolinate:acetyl-CoA acetyltransferase, acetyl-CoA:L-2,3,4,5-tetrahydrodipicolinate N2-acetyltransferase, acetyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, and 2-N-acetyltransferase. This enzyme participates in lysine biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thioethanolamine%20S-acetyltransferase | In enzymology, a thioethanolamine S-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + 2-aminoethanethiol CoA + S-(2-aminoethyl)thioacetate
Thus, the two substrates of this enzyme are acetyl-CoA and 2-aminoethanethiol, whereas its two products are CoA and S-(2-aminoethyl)thioacetate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:2-aminoethanethiol S-acetyltransferase. Other names in common use include thioltransacetylase B, thioethanolamine acetyltransferase, and acetyl-CoA:thioethanolamine S-acetyltransferase.
References
McElroy, W.D. and Glass, B. (Eds.), A Symposium on the Mechanism of Enzyme Action, Johns Hopkins Press, Baltimore, 1954, p. 545-580.
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trehalose%20O-mycolyltransferase | In enzymology, a trehalose O-mycolyltransferase () is an enzyme that catalyzes the chemical reaction
2 alpha,alpha-trehalose 6-mycolate alpha,alpha-trehalose + alpha,alpha-trehalose 6,6'-bismycolate
Hence, this enzyme has one substrate( alpha,alpha'-trehalose 6-mycolate) and two products ( alpha,alpha-trehalose and alpha,alpha'-trehalose 6,6'-bismycolate).
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is alpha,alpha-trehalose-6-mycolate:alpha,alpha-trehalose-6-mycolate 6'-mycolyltransferase. Other names in common use include alpha,alpha'-trehalose 6-monomycolate:alpha,alpha'-trehalose, mycolyltransferase, alpha,alpha'-trehalose-6-mycolate:alpha,alpha'-trehalose-6-mycolate, and 6'-mycolyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Triacylglycerol%E2%80%94sterol%20O-acyltransferase | In enzymology, a triacylglycerol---sterol O-acyltransferase () is an enzyme that catalyzes the chemical reaction
triacylglycerol + a 3beta-hydroxysterol diacylglycerol + a 3beta-hydroxysterol ester
Thus, the two substrates of this enzyme are triacylglycerol and 3beta-hydroxysterol, whereas its two products are diacylglycerol and 3beta-hydroxysterol ester.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is triacylglycerol:3beta-hydroxysterol O-acyltransferase. This enzyme is also called triacylglycerol:sterol acyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trihydroxystilbene%20synthase | In enzymology, a trihydroxystilbene synthase () is an enzyme that catalyzes the chemical reaction
3 malonyl-CoA + 4-coumaroyl-CoA 4 CoA + 3,4',5-trihydroxy-stilbene + 4 CO2
Thus, the two substrates of this enzyme are malonyl-CoA and 4-coumaroyl-CoA, whereas its 3 products are CoA, 3,4',5-trihydroxy-stilbene (resveratrol), and CO2.
This enzyme belongs to the family of transferases, To be specific those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing). Other names in common use include resveratrol synthase, and stilbene synthase. This enzyme participates in phenylpropanoid biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
Further reading
EC 2.3.1
Enzymes of known structure
Hydroxycinnamic acids metabolism
Stilbenoids metabolism |
https://en.wikipedia.org/wiki/Tyramine%20N-feruloyltransferase | In enzymology, a tyramine N-feruloyltransferase () is an enzyme that catalyzes the chemical reaction
feruloyl-CoA + tyramine CoA + N-feruloyltyramine
Thus, the two substrates of this enzyme are feruloyl-CoA and tyramine, whereas its two products are CoA and N-feruloyltyramine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is feruloyl-CoA:tyramine N-(hydroxycinnamoyl)transferase. Other names in common use include tyramine N-feruloyl-CoA transferase, feruloyltyramine synthase, feruloyl-CoA tyramine N-feruloyl-CoA transferase, and tyramine feruloyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-N-acetylmuramoylpentapeptide-lysine%20N6-alanyltransferase | In enzymology, an UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase () is an enzyme that catalyzes the chemical reaction
L-alanyl-tRNA + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine tRNA + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D- alanyl-D-alanine
Thus, the two substrates of this enzyme are L-alanyl-tRNA and UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, whereas its 3 products are tRNA, UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-N6-(L-alanyl)-L-lysyl-D-, and alanyl-D-alanine.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-ala nyl-D-alanine N6-alanyltransferase. Other names in common use include alanyl-transfer ribonucleate-uridine, diphosphoacetylmuramoylpentapeptide transferase, UDP-N-acetylmuramoylpentapeptide lysine N6-alanyltransferase, uridine diphosphoacetylmuramoylpentapeptide lysine, N6-alanyltransferase, L-alanyl-tRNA:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-, and alanyl-D-alanine 6-N-alanyltransferase. This enzyme participates in peptidoglycan biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 2.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Vinorine%20synthase | In enzymology, a vinorine synthase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + 16-epivellosimine CoA + vinorine
Thus, the two substrates of this enzyme are acetyl-CoA and 16-epivellosimine, whereas its two products are CoA and vinorine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:16-epivellosimine O-acetyltransferase (cyclizing). This enzyme participates in indole and ipecac alkaloid 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 2.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/1-deoxy-D-xylulose-5-phosphate%20synthase | {{DISPLAYTITLE: 1-deoxy-D-xylulose-5-phosphate synthase}}
In enzymology, a 1-deoxy--xylulose-5-phosphate synthase () is an enzyme in the non-mevalonate pathway that catalyzes the chemical reaction
pyruvate + -glyceraldehyde 3-phosphate 1-deoxy--xylulose 5-phosphate + CO2
Thus, the two substrates of this enzyme are pyruvate and -glyceraldehyde 3-phosphate, whereas its two products are 1-deoxy--xylulose 5-phosphate and CO2.
This enzyme belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). The systematic name of this enzyme class is pyruvate:-glyceraldehyde-3-phosphate acetaldehydetransferase (decarboxylating). Other names in common use include 1-deoxy--xylulose-5-phosphate pyruvate-lyase (carboxylating), and DXP-synthase. This enzyme participates in biosynthesis of steroids.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-hydroxy-3-oxoadipate%20synthase | In enzymology, a 2-hydroxy-3-oxoadipate synthase () is an enzyme that catalyzes the following chemical reaction:
2-oxoglutarate + glyoxylate 2-hydroxy-3-oxoadipate + CO2
The two substrates of this enzyme are 2-oxoglutarate and glyoxylate, whereas its two products are 2-hydroxy-3-oxoadipate and CO2.
This enzyme belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). Other names in common use include 2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating), alpha-ketoglutaric-glyoxylic carboligase, and oxoglutarate: glyoxylate carboligase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It employs one cofactor, thiamin diphosphate.
References
EC 2.2.1
Thiamine enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetoin%E2%80%94ribose-5-phosphate%20transaldolase | In enzymology, an acetoin-ribose-5-phosphate transaldolase () is an enzyme that catalyzes the chemical reaction
3-hydroxybutan-2-one + D-ribose 5-phosphate acetaldehyde + 1-deoxy-D-altro-heptulose 7-phosphate
Thus, the two substrates of this enzyme are 3-hydroxybutan-2-one and D-ribose 5-phosphate, whereas its two products are acetaldehyde and 1-deoxy-D-altro-heptulose 7-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). The systematic name of this enzyme class is 3-hydroxybutan-2-one:D-ribose-5-phosphate aldehydetransferase. Other names in common use include 1-deoxy-D-altro-heptulose-7-phosphate synthetase, 1-deoxy-D-altro-heptulose-7-phosphate synthase, 3-hydroxybutan-2-one:D-ribose-5-phosphate aldehydetransferase [wrong, and substrate name]. It employs one cofactor, thiamin diphosphate.
References
EC 2.2.1
Thiamine enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Fluorothreonine%20transaldolase | In enzymology, a fluorothreonine transaldolase () is an enzyme that catalyzes the chemical reaction
L-threonine + fluoroacetaldehyde acetaldehyde + 4-fluoro-L-threonine
Thus, the two substrates of this enzyme are L-threonine and fluoroacetaldehyde, whereas its two products are acetaldehyde and 4-fluoro-L-threonine.
This enzyme belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). The systematic name of this enzyme class is fluoroacetaldehyde:L-threonine aldehydetransferase.
References
EC 2.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Formaldehyde%20transketolase | In enzymology, a formaldehyde transketolase () is an enzyme that catalyzes the chemical reaction
D-xylulose 5-phosphate + formaldehyde glyceraldehyde 3-phosphate + glycerone
Thus, the two substrates of this enzyme are D-xylulose 5-phosphate and formaldehyde, whereas its two products are glyceraldehyde 3-phosphate and glycerone.
This enzyme belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). The systematic name of this enzyme class is D-xylulose-5-phosphate:formaldehyde glycolaldehydetransferase. This enzyme is also called dihydroxyacetone synthase. This enzyme participates in methane metabolism. It employs one cofactor, thiamin diphosphate.
References
EC 2.2.1
Thiamine enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-succinyl-6-hydroxy-2%2C4-cyclohexadiene-1-carboxylate%20synthase | 2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (EC 4.2.99.20), also known as SHCHC synthase is encoded by the menH gene in Escherichia coli and functions in the synthesis of vitamin K. The specific step in the synthetic pathway that SHCHC synthase catalyzes is the conversion of 5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3-ene-1-carboxylate to (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate and pyruvate.
Background
Vitamin K is a fat soluble vitamin known to aid in blood clotting. It is recommended that all newborns receive an injection of vitamin K in order to prevent excessive bleeding of the brain after birth. There are two major forms of vitamin K that occur naturally. Phylloquinone, also known as K1, is synthesized by plants and is the major form of vitamin K in the diet. Menaquinone, K2, includes a range of forms that are synthesized by bacteria in the gut.
Vitamin K is synthesized from the molecule chorismate in a nine step conversion process. SHCHC synthase catalyzes the third step in the process.
Chemistry
Reaction scheme
Enzyme Structure
The crystal structure of the MenH enzyme in E.coli (SHCHC synthase) exists as a complex of three protein molecules shown in the diagram. SHCHC synthase forms an alpha/beta hydrolase fold with a central set of seven parallel beta sheets surrounded by alpha helixes on both sides. A cap of five alpha helixes serves to enclose the active site. The enzyme exists in an open form until it binds the sub |
https://en.wikipedia.org/wiki/3-deoxy-8-phosphooctulonate%20synthase | In enzymology, a 3-deoxy-8-phosphooctulonate synthase () is an enzyme that catalyzes the chemical reaction
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
The 3 substrates of this enzyme are phosphoenolpyruvate, D-arabinose 5-phosphate, and H2O, whereas its two products are 2-dehydro-3-deoxy-D-octonate 8-phosphate and phosphate.
This enzyme participates in lipopolysaccharide biosynthesis.
Nomenclature
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is phosphoenolpyruvate:D-arabinose-5-phosphate C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming). Other names in common use include 2-dehydro-3-deoxy-D-octonate-8-phosphate, D-arabinose-5-phosphate-lyase (pyruvate-phosphorylating), 2-dehydro-3-deoxy-phosphooctonate aldolase, 2-keto-3-deoxy-8-phosphooctonic synthetase, 3-deoxy-D-manno-octulosonate-8-phosphate synthase, 3-deoxy-D-mannooctulosonate-8-phosphate synthetase, 3-deoxyoctulosonic 8-phosphate synthetase, KDOP synthase, and phospho-2-keto-3-deoxyoctonate aldolase.
References
Further reading
EC 2.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Adenosylmethionine%20cyclotransferase | In enzymology, an adenosylmethionine cyclotransferase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine 5'-methylthioadenosine + 2-aminobutan-4-olide
Hence, this enzyme has one substrate, S-adenosyl-L-methionine, and two products, 5'-methylthioadenosine and 2-aminobutan-4-olide.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosyl-L-methionine alkyltransferase (cyclizing). This enzyme is also called adenosylmethioninase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Adenylate%20dimethylallyltransferase | In enzymology, an adenylate dimethylallyltransferase () is an enzyme that catalyzes the chemical reaction
dimethylallyl diphosphate + AMP diphosphate + N6-(dimethylallyl)adenosine 5'-phosphate
Thus, the two substrates of this enzyme are dimethylallyl diphosphate and AMP, whereas its two products are diphosphate and N6-(dimethylallyl)adenosine 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is dimethylallyl-diphosphate:AMP dimethylallyltransferase. Other names in common use include cytokinin synthase, isopentenyltransferase, 2-isopentenyl-diphosphate:AMP Delta2-isopentenyltransferase, and adenylate isopentenyltransferase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aspulvinone%20dimethylallyltransferase | In enzymology, an aspulvinone dimethylallyltransferase () is an enzyme that catalyzes the chemical reaction
2 dimethylallyl diphosphate + aspulvinone E 2 diphosphate + aspulvinone H
Thus, the two substrates of this enzyme are dimethylallyl diphosphate and aspulvinone E, whereas its two products are diphosphate and aspulvinone H.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is dimethylallyl-diphosphate:aspulvinone-E dimethylallyltransferase. This enzyme is also called dimethylallyl pyrophosphate:aspulvinone dimethylallyltransferase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-pyrazolylalanine%20synthase | In enzymology, a beta-pyrazolylalanine synthase () is an enzyme that catalyzes the chemical reaction
O3-acetyl-L-serine + pyrazole 3-(pyrazol-1-yl)-L-alanine + acetate
Thus, the two substrates of this enzyme are O3-acetyl-L-serine and pyrazole, whereas its two products are 3-(pyrazol-1-yl)-L-alanine and acetate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O3-acetyl-L-serine:pyrazole 1-(2-amino-2-carboxyethyl)transferase. Other names in common use include beta-(1-pyrazolyl)alanine synthase, beta-pyrazolealanine synthase, beta-pyrazolylalanine synthase (acetylserine), O3-acetyl-L-serine acetate-lyase (adding pyrazole), BPA-synthase, pyrazolealanine synthase, pyrazolylalaninase, and 3-O-acetyl-L-serine:pyrazole 1-(2-amino-2-carboxyethyl)transferase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/MTV%27s%20Amp | MTV's Amp is a 1997 electronic album produced by the late-night show, MTV's Amp. It features many of the bigger hits in America, including tracks from the Chemical Brothers and Crystal Method.
Track listing
"Block Rockin' Beats" by The Chemical Brothers - 5:00
"Atom Bomb" by Fluke - 3:57
"Pearl's Girl" by Underworld - 4:25
"We Have Explosive" by The Future Sound of London - 6:22
"Ni Ten Ichi Ryu" by Photek - 5:58
"Girl/Boy Song" by Aphex Twin - 4:48
"The Box" by Orbital - 4:15
"We All Want To Be Free" by Tranquility Bass - 4:20
"Inner City Life" by Goldie - 3:14
"Voodoo People (Chemical Brothers remix)" by The Prodigy - 5:54
"Are You There?" by Josh Wink - 3:58
"Busy Child" by The Crystal Method - 4:07
"Sick To Death" by Atari Teenage Riot - 3:39
References
Techno compilation albums
Electronic compilation albums
1997 compilation albums
Drum and bass albums
House music albums
Industrial compilation albums |
https://en.wikipedia.org/wiki/Chlorophyll%20synthase | In enzymology, chlorophyll synthase () is an enzyme that catalyzes the chemical reaction
chlorophyllide a + phytyl diphosphate chlorophyll a + diphosphate
The two substrates of this enzyme are chlorophyllide a and phytyl diphosphate; its two products are chlorophyll a and diphosphate. The same enzyme can act on chlorophyllide b to form chlorophyll b and similarly for chlorophyll d and f.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is chlorophyllide-a:phytyl-diphosphate phytyltransferase. This reaction is the final step of the complete biosynthetic pathway to chlorophylls from glutamic acid.
See also
Biosynthesis of chlorophylls
References
Further reading
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chrysanthemyl%20diphosphate%20synthase | In enzymology, a chrysanthemyl diphosphate synthase () is an enzyme involved in the biosynthesis of terpenoids. This enzyme is also known as CPPase. It catalyzes the chemical reaction shown below (color-coded to show how precursors link):
The substrate of CPPase is dimethylallyl diphosphate. The two products are diphosphate and chrysanthemyl diphosphate.
This enzyme is involved in the biosynthesis of pyrethrins, highly potent insecticides found in some flowers. The systematic name of this enzyme class is dimethylallyl-diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (chrysanthemyl-diphosphate-forming).
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cystathionine%20gamma-synthase | In enzymology, a cystathionine gamma-synthase () is an enzyme that catalyzes the formation of cystathionine from cysteine and an activated derivative of homoserine, e.g.:
O4-succinyl-L-homoserine + L-cysteine L-cystathionine + succinate
In microorganisms, the activated substrate of this enzyme is O4-succinyl-L-homoserine or O4-acetyl-L-homoserine. Cystathionine gamma-synthase from plants uses L-homoserine phosphate instead.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O4-succinyl-L-homoserine:L-cysteine S-(3-amino-3-carboxypropyl)transferase. Other names in common use include O-succinyl-L-homoserine succinate-lyase (adding cysteine), O-succinylhomoserine (thiol)-lyase, homoserine O-transsuccinylase, O-succinylhomoserine synthase, O-succinylhomoserine synthetase, cystathionine synthase, cystathionine synthetase, homoserine transsuccinylase, 4-O-succinyl-L-homoserine:L-cysteine, and S-(3-amino-3-carboxypropyl)transferase. This enzyme participates in 4 metabolic pathways: methionine metabolism, cysteine metabolism, selenoamino acid metabolism, and sulfur metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 2.5.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cysteine%20synthase | In enzymology, a cysteine synthase () is an enzyme that catalyzes the chemical reaction
O3-acetyl-L-serine + hydrogen sulfide L-cysteine + acetate
Thus, the two substrates of this enzyme are O3-acetyl-L-serine and hydrogen sulfide, whereas its two products are L-cysteine and acetate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase. Other names in common use include O-acetyl-L-serine sulfhydrylase, O-acetyl-L-serine sulfohydrolase, O-acetylserine (thiol)-lyase, O-acetylserine (thiol)-lyase A, O-acetylserine sulfhydrylase, O3-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide), acetylserine sulfhydrylase, cysteine synthetase, S-sulfocysteine synthase, 3-O-acetyl-L-serine:hydrogen-sulfide, and 2-amino-2-carboxyethyltransferase. This enzyme participates in 3 metabolic pathways: cysteine metabolism, selenoamino acid metabolism, and sulfur metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , and .
References
EC 2.5.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Dimethylallylcistransferase | In enzymology, a dimethylallylcistransferase () is an enzyme that catalyzes the chemical reaction
dimethylallyl diphosphate + isopentenyl diphosphate diphosphate + neryl diphosphate
Thus, the two substrates of this enzyme are dimethylallyl diphosphate and isopentenyl diphosphate, whereas its two products are diphosphate and neryl diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is dimethylallyl-diphosphate:isopentenyl-diphosphate dimethylallylcistransferase. This enzyme is also called neryl-diphosphate synthase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Discadenine%20synthase | In enzymology, a discadenine synthase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + N6-(Delta2-isopentenyl)-adenine 5'-methylthioadenosine + discadenine
Thus, the two substrates of this enzyme are S-adenosyl-L-methionine and N6-(Delta2-isopentenyl)-adenine, whereas its two products are 5'-methylthioadenosine and discadenine.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosyl-L-methionine:N6-(Delta2-isopentenyl)-adenine 3-(3-amino-3-carboxypropyl)-transferase. Other names in common use include discadenine synthetase, S-adenosyl-L-methionine:6-N-(Delta2-isopentenyl)-adenine, and 3-(3-amino-3-carboxypropyl)-transferase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Di-trans%2Cpoly-cis-decaprenylcistransferase | In enzymology, a di-trans,poly-cis-decaprenylcistransferase () is an enzyme that catalyzes the chemical reaction
di-trans,poly-cis-decaprenyl diphosphate + isopentenyl diphosphate diphosphate + di-trans,poly-cis-undecaprenyl diphosphate
Thus, the two substrates of this enzyme are di-trans,poly-cis-decaprenyl diphosphate and isopentenyl diphosphate, whereas its two products are diphosphate and di-trans,poly-cis-undecaprenyl diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is di-trans,poly-cis-decaprenyl-diphosphate:isopentenyl-diphosphate undecaprenylcistransferase. Other names in common use include di-trans,poly-cis-undecaprenyl-diphosphate synthase, undecaprenyl-diphosphate synthase, bactoprenyl-diphosphate synthase, UPP synthetase, undecaprenyl diphosphate synthetase, and undecaprenyl pyrophosphate synthetase. This enzyme participates in terpenoid biosynthesis.
Structural studies
As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , and .
References
EC 2.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Farnesyltranstransferase | In enzymology, a farnesyltranstransferase () is an enzyme that catalyzes the chemical reaction.
trans,trans-farnesyl diphosphate + isopentenyl diphosphate diphosphate + geranylgeranyl diphosphate
Thus, the two substrates of this enzyme are trans,trans-farnesyl diphosphate and isopentenyl diphosphate, whereas its two products are diphosphate and geranylgeranyl diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is trans,trans-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase. Other names in common use include geranylgeranyl-diphosphate synthase, geranylgeranyl pyrophosphate synthetase, geranylgeranyl-PP synthetase, farnesyltransferase, and geranylgeranyl pyrophosphate synthase. This enzyme participates in biosynthesis of steroids and terpenoid biosynthesis.
This protein may use the morpheein model of allosteric regulation.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Galactose-6-sulfurylase | In enzymology, a galactose-6-sulfurylase () is an enzyme that catalyzes the chemical reaction
Eliminates sulfate from the D-galactose 6-sulfate residues of porphyran, producing 3,6-anhydrogalactose residues.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is D-galactose-6-sulfate:alkyltransferase (cyclizing). Other names in common use include porphyran sulfatase, galactose-6-sulfatase, and galactose 6-sulfatase.
Further reading
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Geranylgeranylglycerol-phosphate%20geranylgeranyltransferase | In enzymology, a geranylgeranylglycerol-phosphate geranylgeranyltransferase () is an enzyme that catalyzes the chemical reaction
geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate diphosphate + 2,3-bis-O-(geranylgeranyl)glycerol 1-phosphate
Thus, the two substrates of this enzyme are geranylgeranyl diphosphate and sn-3-O-(geranylgeranyl)glycerol 1-phosphate, whereas its two products are diphosphate and 2,3-bis-O-(geranylgeranyl)glycerol 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl groups or alkyl groups other than methyl groups. The systematic name of this enzyme class is geranylgeranyl diphosphate:sn-3-O-(geranylgeranyl)glycerol 1-phosphate geranylgeranyltransferase. Other names in common use include geranylgeranyloxyglycerol phosphate geranylgeranyltransferase, and geranylgeranyltransferase II.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Geranyltranstransferase | In enzymology, a geranyltranstransferase () is an enzyme that catalyzes the chemical reaction
geranyl diphosphate + isopentenyl diphosphate diphosphate + trans,trans-farnesyl diphosphate
Thus, the two substrates of this enzyme are geranyl diphosphate (a 10 carbon precursor) and isopentenyl diphosphate (a 5 carbon precursor) whereas its two products are diphosphate and trans,trans-farnesyl diphosphate (a 15 carbon product).
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups.
Nomenclature
The systematic name of this enzyme class is geranyl-diphosphate:isopentenyl-diphosphate geranyltranstransferase. Other names in common use include:
farnesyl-diphosphate synthase
geranyl transferase I
prenyltransferase
farnesyl pyrophosphate synthetase
farnesylpyrophosphate synthetase
Common abbreviations include: FPS, FDS, FPPS, and FDPS.
Structure
The structure and mechanism of farnesyl pyrophosphate synthase (FPPS), a type of geranyltranstransferase, is well characterized. FPPS is a ~30 kDa Mg2+ dependent homodimeric enzyme that synthesizes (E, E)-farnesyl pyrophosphate in a successive manner from two equivalents of isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP).
FPPS adopts a 3-layered α-helical fold characteristic of many prenyltransferases with 11 helices and flexible loops in between. The centrally located helices (α4 and α8) contain conserved aspartate motifs (DDXXD) |
https://en.wikipedia.org/wiki/Homospermidine%20synthase%20%28spermidine-specific%29 | In enzymology, a homospermidine synthase (spermidine-specific) () is an enzyme that catalyzes the chemical reaction
spermidine + putrescine sym-homospermidine + propane-1,3-diamine
Thus, the two substrates of this enzyme are spermidine and putrescine, whereas its two products are sym-homospermidine and propane-1,3-diamine.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is spermidine:putrescine 4-aminobutyltransferase (propane-1,3-diamine-forming).
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isonocardicin%20synthase | In enzymology, an isonocardicin synthase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + nocardicin E 5'-methylthioadenosine + isonocardicin A
Thus, the two substrates of this enzyme are S-adenosyl-L-methionine and nocardicin E, whereas its two products are 5'-methylthioadenosine and isonocardicin A.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosyl-L-methionine:nocardicin-E 3-amino-3-carboxypropyltransferase. This enzyme is also called nocardicin aminocarboxypropyltransferase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lavandulyl%20diphosphate%20synthase | In enzymology, a lavandulyl diphosphate synthase () is an enzyme that catalyzes the chemical reaction
2 dimethylallyl diphosphate diphosphate + lavandulyl diphosphate
Hence, this enzyme has one substrate, dimethylallyl diphosphate, and two products, diphosphate and lavandulyl diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is dimethylallyl-diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (lavandulyl-diphosphate-forming). This enzyme is also called FDS-5.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-mimosine%20synthase | In enzymology, a L-mimosine synthase () is an enzyme that catalyzes the chemical reaction
O3-acetyl-L-serine + 3,4-dihydroxypyridine 3-(3,4-dihydroxypyridin-1-yl)-L-alanine + acetate
Thus, the two substrates of this enzyme are O3-acetyl-L-serine and 3,4-dihydroxypyridine, whereas its two products are 3-(3,4-dihydroxypyridin-1-yl)-L-alanine and acetate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O3-acetyl-L-serine:3,4-dihydroxypyridine 1-(2-amino-2-carboxyethyl)transferase. Other names in common use include O3-acetyl-L-serine acetate-lyase (adding 3,4-dihydroxypyridin-1-yl), 3-O-acetyl-L-serine:3,4-dihydroxypyridine, and 1-(2-amino-2-carboxyethyl)transferase.
References
EC 2.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N2-%282-carboxyethyl%29arginine%20synthase | In enzymology, a N2-(2-carboxyethyl)arginine synthase () is an enzyme that catalyzes the chemical reaction
D-glyceraldehyde 3-phosphate + L-arginine N2-(2-carboxyethyl)-L-arginine + phosphate
Thus, the two substrates of this enzyme are D-glyceraldehyde 3-phosphate and L-arginine, whereas its two products are N2-(2-carboxyethyl)-L-arginine and phosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is glyceraldehyde-3-phosphate:L-arginine N2-(2-hydroxy-3-oxopropyl) transferase (2-carboxyethyl-forming). Other names in common use include CEAS, N2-(2-carboxyethyl)arginine synthetase, CEA synthetase, glyceraldehyde-3-phosphate:L-arginine 2-N-(2-hydroxy-3-oxopropyl), and transferase (2-carboxyethyl-forming). This enzyme participates in clavulanic acid biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acetylneuraminate%20synthase | In enzymology, a N-acetylneuraminate synthase () is an enzyme that catalyzes the chemical reaction
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O phosphate + N-acetylneuraminate
The 3 substrates of this enzyme are phosphoenolpyruvate, N-acetyl-D-mannosamine, and H2O, whereas its two products are phosphate and N-acetylneuraminate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is phosphoenolpyruvate:N-acetyl-D-mannosamine C-(1-carboxyvinyl)transferase (phosphate-hydrolysing, 2-carboxy-2-oxoethyl-forming). Other names in common use include (NANA)condensing enzyme, N-acetylneuraminate pyruvate-lyase (pyruvate-phosphorylating), and NeuAc synthase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acylneuraminate-9-phosphate%20synthase | In enzymology, a N-acylneuraminate-9-phosphate synthase () is an enzyme that catalyzes the chemical reaction
phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H2O N-acylneuraminate 9-phosphate + phosphate
The 3 substrates of this enzyme are phosphoenolpyruvate, N-acyl-D-mannosamine 6-phosphate, and H2O, whereas its two products are N-acylneuraminate 9-phosphate and phosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is phosphoenolpyruvate:N-acyl-D-mannosamine-6-phosphate 1-(2-carboxy-2-oxoethyl)transferase. Other names in common use include N-acetylneuraminate 9-phosphate lyase, N-acetylneuraminate 9-phosphate sialic acid 9-phosphate synthase, N-acetylneuraminate 9-phosphate synthetase, N-acylneuraminate-9-phosphate pyruvate-lyase, (pyruvate-phosphorylating), and sialic acid 9-phosphate synthetase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Naringenin%208-dimethylallyltransferase | In enzymology, a naringenin 8-dimethylallyltransferase () is an enzyme that catalyzes the chemical reaction
dimethylallyl diphosphate + (-)-(2S)-naringenin diphosphate + sophoraflavanone B
Thus, the two substrates of this enzyme are dimethylallyl diphosphate and (-)-(2S)-naringenin, whereas its two products are diphosphate and sophoraflavanone B.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is dimethylallyl-diphosphate:naringenin 8-dimethylallyltransferase. This enzyme is also called N8DT.
References
EC 2.5.1
Enzymes of unknown structure |
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