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https://en.wikipedia.org/wiki/Aldose-1-phosphate%20adenylyltransferase | In enzymology, an aldose-1-phosphate adenylyltransferase () is an enzyme that catalyzes the chemical reaction
ADP + alpha-D-aldose 1-phosphate phosphate + ADP-aldose
Thus, the two substrates of this enzyme are ADP and alpha-D-aldose 1-phosphate, whereas its two products are phosphate and ADP-aldose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ADP:alpha-D-aldose-1-phosphate adenylyltransferase. Other names in common use include sugar-1-phosphate adenylyltransferase, ADPaldose phosphorylase, adenosine diphosphosugar phosphorylase, ADP sugar phosphorylase, adenosine diphosphate glucose:orthophosphate adenylyltransferase, and ADP:aldose-1-phosphate adenylyltransferase.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aldose-1-phosphate%20nucleotidyltransferase | In enzymology, an aldose-1-phosphate nucleotidyltransferase () is an enzyme that catalyzes the chemical reaction
NDP + alpha-D-aldose 1-phosphate phosphate + NDP-aldose
Thus, the two substrates of this enzyme are NDP and alpha-D-aldose 1-phosphate, whereas its two products are phosphate and NDP-aldose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is NDP:alpha-D-aldose-1-phosphate nucleotidyltransferase. Other names in common use include sugar-1-phosphate nucleotidyltransferase, NDPaldose phosphorylase, glucose 1-phosphate inosityltransferase, NDP sugar phosphorylase, nucleoside diphosphosugar phosphorylase, sugar phosphate nucleotidyltransferase, nucleoside diphosphate sugar:orthophosphate nucleotidyltransferase, sugar nucleotide phosphorylase, and NDP:aldose-1-phosphate nucleotidyltransferase. This enzyme participates in nucleotide sugars metabolism.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alkylglycerol%20kinase | In enzymology, an alkylglycerol kinase () is an enzyme that catalyzes the chemical reaction
ATP + 1-O-alkyl-sn-glycerol ADP + 1-O-alkyl-sn-glycerol 3-phosphate
Thus, the two substrates of this enzyme are ATP and 1-O-alkyl-sn-glycerol, whereas its two products are ADP and 1-O-alkyl-sn-glycerol 3-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1-O-alkyl-sn-glycerol 3-phosphotransferase. Other names in common use include 1-alkylglycerol kinase (phosphorylating), ATP-alkylglycerol phosphotransferase, alkylglycerol phosphotransferase, and ATP: 1-alkyl-sn-glycerol phosphotransferase. This enzyme participates in ether lipid metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alkylglycerone%20kinase | In enzymology, an alkylglycerone kinase () is an enzyme that catalyzes the chemical reaction
ATP + O-alkylglycerone ADP + O-alkylglycerone phosphate
Thus, the two substrates of this enzyme are ATP and O-alkylglycerone, whereas its two products are ADP and O-alkylglycerone phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:O-alkylglycerone phosphotransferase. Other names in common use include alkyldihydroxyacetone kinase (phosphorylating), and alkyldihydroxyacetone kinase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Allose%20kinase | In enzymology, an allose kinase () is an enzyme that catalyzes the chemical reaction
ATP + D-allose ADP + D-allose 6-phosphate
Thus, the two substrates of this enzyme are ATP and D-allose, whereas its two products are ADP and D-allose 6-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-allose 6-phosphotransferase. Other names in common use include allokinase (phosphorylating), allokinase, D-allokinase, and D-allose-6-kinase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alpha-glucan%2C%20water%20dikinase | In enzymology, an alpha-glucan, water dikinase () is an enzyme that catalyzes the chemical reaction
ATP + alpha-glucan + H2O AMP + phospho-alpha-glucan + phosphate
The 3 substrates of this enzyme are ATP, alpha-glucan, and H2O, whereas its 3 products are AMP, phospho-alpha-glucan, and phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with paired acceptors (dikinases). The systematic name of this enzyme class is ATP:alpha-glucan, water phosphotransferase. This enzyme is also called starch-related R1 protein, GWD.
References
EC 2.7.9
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ammonia%20kinase | In enzymology, an ammonia kinase () is an enzyme that catalyzes the chemical reaction
ATP + NH3 ADP + phosphoramide
Thus, the two substrates of this enzyme are ATP and NH3, whereas its two products are ADP and phosphoramide.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:ammonia phosphotransferase. Other names in common use include phosphoramidate-adenosine diphosphate phosphotransferase, and phosphoramidate-ADP-phosphotransferase.
References
EC 2.7.3
Enzymes of unknown structure
Ammonia |
https://en.wikipedia.org/wiki/AMP%E2%80%94thymidine%20kinase | In enzymology, an AMP—thymidine kinase () is an enzyme that catalyzes the chemical reaction
AMP + thymidine adenosine + thymidine 5'-phosphate
Thus, the two substrates of this enzyme are AMP and thymidine, whereas its two products are adenosine and thymidine 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is AMP:thymidine 5'-phosphotransferase. This enzyme is also called adenylate-nucleoside phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Anthranilate%20adenylyltransferase | In enzymology, an anthranilate adenylyltransferase () is an enzyme that catalyzes the chemical reaction
ATP + anthranilate diphosphate + N-adenylylanthranilate
Thus, the two substrates of this enzyme are ATP and anthranilate, whereas its two products are diphosphate and N-adenylylanthranilate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:anthranilate N-adenylyltransferase. This enzyme is also called anthranilic acid adenylyltransferase.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Arginine%20kinase | In enzymology, arginine kinase () is an enzyme that catalyzes the chemical reaction
ATP + L-arginine ADP + Nω-phospho-L-arginine
Thus, the two substrates of this enzyme are ATP and L-arginine, whereas its two products are ADP and Nω-phospho-L-arginine. Unlike the phosphoester bond, formed during the phosphorylation of serine, threonine or tyrosine residues, the phosphoramidate (P-N bond) in phospho-arginine is unstable at low pH (<8), making it difficult to detect with the traditional mass spectrometry protocols.
Arginine kinase belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. This enzyme participates in arginine and proline metabolism.
Nomenclature
The systematic name of this enzyme class is
ATP:L-arginine Nω-phosphotransferase
Other names in common use include
arginine phosphokinase,
adenosine 5'-triphosphate: L-arginine phosphotransferase,
adenosine 5'-triphosphate-arginine phosphotransferase,
ATP:L-arginine N-phosphotransferasel ATP:L-arginine, and
ω-N-phosphotransferase.
Function
In Gram-positive bacteria, such as Bacillus subtilis, the arginine kinase McsB phosphorylates the arginine residues on incorrectly folded or aggregated proteins to target them for degradation by the bacterial protease ClpC-ClpP (ClpCP).The phospho-arginine (pArg) modification is recognised by the N-terminal domain of ClpC, the protein-unfolding subunit of the ClpCP pr |
https://en.wikipedia.org/wiki/ATP%20adenylyltransferase | In enzymology, an ATP adenylyltransferase () is an enzyme that catalyzes the chemical reaction
ADP + ATP phosphate + P1,P4-bis(5'-adenosyl) tetraphosphate
Thus, the two substrates of this enzyme are ADP and ATP, whereas its two products are phosphate and P1,P4-bis(5'-adenosyl) tetraphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ADP:ATP adenylyltransferase. Other names in common use include bis(5'-nucleosyl)-tetraphosphate phosphorylase (NDP-forming), diadenosinetetraphosphate alphabeta-phosphorylase, adenine triphosphate adenylyltransferase, diadenosine 5',5'"-P1,P4-tetraphosphate alphabeta-phosphorylase, (ADP-forming), and dinucleoside oligophosphate alphabeta-phosphorylase. This enzyme participates in purine metabolism.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-adrenergic-receptor%20kinase | In enzymology, a beta-adrenergic-receptor kinase () is an enzyme that catalyzes the chemical reaction:
ATP + [beta-adrenergic receptor] ADP + phospho-[beta-adrenergic receptor]
Thus, the two substrates of this enzyme are ATP and beta-adrenergic receptor, whereas its two products are ADP and phospho-beta-adrenergic receptor.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[beta-adrenergic receptor] phosphotransferase. Other names in common use include ATP:beta-adrenergic-receptor phosphotransferase, [beta-adrenergic-receptor] kinase, beta-adrenergic receptor-specific kinase, beta-AR kinase, beta-ARK, beta-ARK 1, beta-ARK 2, beta-receptor kinase, GRK2, GRK3, beta-adrenergic-receptor kinase (phosphorylating), beta2ARK, betaARK1, beta-adrenoceptor kinase, beta-adrenoceptor kinase 1, beta-adrenoceptor kinase 2, ADRBK1, BARK1, adrenergic receptor kinase, and STK15. Several compounds are known to inhibit this enzyme, including Zinc, and Digitonin.
References
External links
EC 2.7.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-glucoside%20kinase | In enzymology, a beta-glucoside kinase () is an enzyme that catalyzes the chemical reaction
ATP + cellobiose ADP + 6-phospho-beta-D-glucosyl-(1,4)-D-glucose
Thus, the two substrates of this enzyme are ATP and cellobiose, whereas its two products are ADP and 6-phospho-beta-D-glucosyl-(1,4)-D-glucose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:cellobiose 6-phosphotransferase. This enzyme is also called beta-D-glucoside kinase (phosphorylating).
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Branched-chain-fatty-acid%20kinase | In enzymology, a branched-chain-fatty-acid kinase () is an enzyme that catalyzes the chemical reaction
ATP + 2-methylpropanoate ADP + 2-methylpropanoyl phosphate
Thus, the two substrates of this enzyme are ATP and 2-methylpropanoate, whereas its two products are ADP and 2-methylpropanoyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:branched-chain-fatty-acid 1-phosphotransferase. This enzyme is also called isobutyrate kinase.
References
EC 2.7.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Butyrate%20kinase | In enzymology, a butyrate kinase () is an enzyme that catalyzes the chemical reaction
ADP + butyryl-phosphate ATP + butyrate
Thus, the two substrates of this enzyme are ADP and butyryl-phosphate, whereas its two products are ATP and butyrate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:butanoate 1-phosphotransferase. This enzyme participates in butyrate metabolism.
This enzyme is transcribed from the gene buk, which is part of the ASKHA super family.
Mechanism
ADP + butyryl-phosphate ATP + butyrate
The reaction above is a nucleophilic substitution reaction. An electron pair from an oxygen on ADP attacks the phosphorus on butyryl-phosphate, breaking the bond between phosphorus and oxygen to create ATP and butyrate. The arrow-pushing mechanism is shown above.
The reaction can also occur in the reverse direction, as shown below, under certain fermentation conditions.
ATP + butyrate ADP + butyryl-phosphate
Structure
As of 2015, two structures have been solved for this class of enzymes, with PDB accession codes and . The study conducted to solve 1SAZ was retracted in 2012 due to fact that the data was used without the permission of the sole custodian.
The investigators of the study that produced the crystallization of 1X9J hypothesized that the enzyme was an octomer formed from dimers. Th |
https://en.wikipedia.org/wiki/Carbamate%20kinase | In enzymology, a carbamate kinase () is an enzyme that catalyzes the chemical reaction
ATP + NH3 + CO2 ADP + carbamoyl phosphate
The 3 substrates of this enzyme are ATP, NH3, and CO2, whereas its two products are ADP and carbamoyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:carbamate phosphotransferase. Other names in common use include CKase, carbamoyl phosphokinase, and carbamyl phosphokinase. This enzyme participates in 4 metabolic pathways: purine metabolism, glutamate metabolism, arginine and proline metabolism, and nitrogen metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.7.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Carboxyvinyl-carboxyphosphonate%20phosphorylmutase | In enzymology, a carboxyvinyl-carboxyphosphonate phosphorylmutase () is an enzyme that catalyzes the chemical reaction
1-carboxyvinyl carboxyphosphonate 3-(hydrohydroxyphosphoryl)pyruvate + CO2
Hence, this enzyme has one substrate, 1-carboxyvinyl carboxyphosphonate, and two products, 3-(hydrohydroxyphosphoryl)pyruvate and CO2.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is 1-carboxyvinyl carboxyphosphonate phosphorylmutase (decarboxylating).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.7.8
Enzymes of known structure |
https://en.wikipedia.org/wiki/CDP-diacylglycerol%E2%80%94glycerol-3-phosphate%203-phosphatidyltransferase | In enzymology, a CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase () is an enzyme that catalyzes the chemical reaction
CDP-diacylglycerol + sn-glycerol 3-phosphate CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate
Thus, the two substrates of this enzyme are CDP-diacylglycerol and sn-glycerol 3-phosphate, whereas its two products are CMP and 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. This enzyme participates in glycerophospholipid metabolism.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CDP-diacylglycerol%E2%80%94inositol%203-phosphatidyltransferase | In enzymology, a CDP-diacylglycerol—inositol 3-phosphatidyltransferase () is an enzyme that catalyzes the chemical reaction
CDP-diacylglycerol + myo-inositol CMP + phosphatidyl-1D-myo-inositol
Thus, the two substrates of this enzyme are CDP-diacylglycerol and myo-inositol, whereas its two products are CMP and phosphatidyl-1D-myo-inositol.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-diacylglycerol:myo-inositol 3-phosphatidyltransferase. Other names in common use include CDP-diglyceride-inositol phosphatidyltransferase, phosphatidylinositol synthase, CDP-diacylglycerol-inositol phosphatidyltransferase, CDP-diglyceride:inositol transferase, cytidine 5'-diphospho-1,2-diacyl-sn-glycerol:myo-inositol, 3-phosphatidyltransferase, CDP-DG:inositol transferase, cytidine diphosphodiglyceride-inositol phosphatidyltransferase, CDP-diacylglycerol:myo-inositol-3-phosphatidyltransferase, CDP-diglyceride-inositol transferase, cytidine diphosphoglyceride-inositol phosphatidyltransferase, and cytidine diphosphoglyceride-inositol transferase. This enzyme participates in glycerophospholipid metabolism and phosphatidylinositol signaling system.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CDP-diacylglycerol%E2%80%94serine%20O-phosphatidyltransferase | In enzymology, a CDP-diacylglycerol—serine O-phosphatidyltransferase () is an enzyme that catalyzes the chemical reaction
CDP-diacylglycerol + L-serine CMP + (3-sn-phosphatidyl)-L-serine
Thus, the two substrates of this enzyme are CDP-diacylglycerol and L-serine, whereas its two products are CMP and (3-sn-phosphatidyl)-L-serine.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-diacylglycerol:L-serine 3-sn-phosphatidyltransferase. Other names in common use include phosphatidylserine synthase, CDPdiglyceride-serine O-phosphatidyltransferase, PS synthase, cytidine 5'-diphospho-1,2-diacyl-sn-glycerol, (CDPdiglyceride):L-serine O-phosphatidyltransferase, phosphatidylserine synthetase, CDP-diacylglycerol-L-serine O-phosphatidyltransferase, cytidine diphosphoglyceride-serine O-phosphatidyltransferase, CDP-diglyceride-L-serine phosphatidyltransferase, CDP-diglyceride:serine phosphatidyltransferase, cytidine 5'-diphospho-1,2-diacyl-sn-glycerol:L-serine, O-phosphatidyltransferase, and CDP-diacylglycerol:L-serine 3-O-phosphatidyltransferase. This enzyme participates in glycine, serine and threonine metabolism and glycerophospholipid metabolism.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CDP-glycerol%20glycerophosphotransferase | In enzymology, a CDP-glycerol glycerophosphotransferase () is an enzyme that catalyzes the chemical reaction
CDP-glycerol + (glycerophosphate)n CMP + (glycerophosphate)n+1
Thus, the two substrates of this enzyme are CDP-glycerol and (glycerophosphate)n, whereas its two products are CMP and (glycerophosphate)n+1.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase. Other names in common use include teichoic-acid synthase, cytidine diphosphoglycerol glycerophosphotransferase, poly(glycerol phosphate) polymerase, teichoic acid glycerol transferase, glycerophosphate synthetase, and CGPTase.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CDP-ribitol%20ribitolphosphotransferase | In enzymology, a CDP-ribitol ribitolphosphotransferase () is an enzyme that catalyzes the chemical reaction
CDP-ribitol + (ribitol phosphate)n CMP + (ribitol phosphate)n+1
Thus, the two substrates of this enzyme are CDP-ribitol and (ribitol phosphate)n, whereas its two products are CMP and (ribitol phosphate)n+1.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-ribitol:poly(ribitol phosphate) ribitolphosphotransferase. Other names in common use include teichoic-acid synthase, polyribitol phosphate synthetase, teichoate synthetase, poly(ribitol phosphate) synthetase, polyribitol phosphate polymerase, and teichoate synthase.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ceramide%20cholinephosphotransferase | In enzymology, a ceramide cholinephosphotransferase () is an enzyme that catalyzes the chemical reaction
CDP-choline + N-acylsphingosine CMP + sphingomyelin
Thus, the two substrates of this enzyme are CDP-choline and N-acylsphingosine, whereas its two products are CMP and sphingomyelin.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-choline:N-acylsphingosine cholinephosphotransferase. This enzyme is also called phosphorylcholine-ceramide transferase. This enzyme participates in sphingolipid metabolism.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ceramide%20kinase | In enzymology, a ceramide kinase, also abbreviated as CERK, () is an enzyme that catalyzes the chemical reaction:
ATP + ceramide ADP + ceramide 1-phosphate
Thus, the two substrates of this enzyme are ATP and ceramide, whereas its two products are ADP and ceramide-1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:ceramide 1-phosphotransferase. This enzyme is also called acylsphingosine kinase. This enzyme participates in sphingolipid metabolism.
Gene
CERK is encoded by the CERK gene. The CERK gene is located on human chromosome 22q13, contains 13 exons, and is approximately 4.5kb in length. CERK shares sequence homology with sphingosine kinase type I, including an N-terminal pleckstrin homology (PH) domain and a diacylglycerol kinase domain. BLAST searches of expressed sequence tag (ESTs) by Sugiura and colleagues have yielded results showing orthologous CERK genes in other eukaryotes including Drosophila melanogaster, Caenorhabditis elegans, and Oryza sativa. A mouse homolog has been cloned as well.
The complete gene of human CERK contains 4459bp, which consists of a 123bp-5’-untranslated region, a 2772bp 3’-non-coding, and a 1611bp open reading frame. Sequence analysis of CERK putatively suggests that the following post-translational modification sites exist: 4 N-glycosylation sites, 1 |
https://en.wikipedia.org/wiki/Choline%20kinase | Choline kinase (also known as CK, ChoK and choline phosphokinase) is an enzyme which catalyzes the first reaction in the choline pathway for phosphatidylcholine (PC) biosynthesis. This reaction involves the transfer of a phosphate group from adenosine triphosphate (ATP) to choline in order to form phosphocholine.
ATP + choline ADP + O-phosphocholine
Thus, the two substrates of this enzyme are ATP and choline, whereas its two products are adenosine diphosphate (ADP) and O-phosphocholine. Choline kinase requires magnesium ions (+2) as a cofactor for this reaction. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The first detailed investigation of the enzyme was conducted by McCamen in 1962, where it was shown that the brain is the richest source of the enzyme in mammalian tissue. A related enzyme, ethanolamine kinase, tends to co-purify with choline kinase leading to a suggestion that the two activities are mediated by two distinct active sites on a single protein. The systematic name of this enzyme class is ATP:choline phosphotransferase. These enzymes participate in glycine, serine and threonine metabolism and glycerophospholipid metabolism.
In mammalian cells, the enzyme exists as three isoforms: CKα-1, CKα-2 and CKβ. These isoforms are encoded by two separate genes, CHKA and CHKB and are only active in their homodimeric, heterodimeric and oligomeric for |
https://en.wikipedia.org/wiki/Choline-phosphate%20cytidylyltransferase | Choline-phosphate cytidylyltransferase () is an enzyme that catalyzes the chemical reaction
CTP + choline phosphate diphosphate + CDP-choline
where the two substrates of this enzyme are CTP and choline phosphate, and the two products are diphosphate and CDP-choline. It is responsible for regulating phosphatidylcholine content in membranes.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:choline-phosphate cytidylyltransferase. Other names in common use include phosphorylcholine transferase, CDP-choline pyrophosphorylase, CDP-choline synthetase, choline phosphate cytidylyltransferase, CTP-phosphocholine cytidylyltransferase, CTP:phosphorylcholine cytidylyltransferase, cytidine diphosphocholine pyrophosphorylase, phosphocholine cytidylyltransferase, phosphorylcholine cytidylyltransferase, and phosphorylcholine:CTP cytidylyltransferase. This enzyme participates in aminophosphonate metabolism and glycerophospholipid metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Insert%20%28molecular%20biology%29 | In Molecular biology, an insert is a piece of DNA that is inserted into a larger DNA vector by a recombinant DNA technique, such as ligation or recombination. This allows it to be multiplied, selected, further manipulated or expressed in a host organism.
Inserts can range from physical nucleotide additions using a technique system or the addition of artificial structures on a molecule via mutagenic chemicals, such as ethidium bromide or crystals.
Inserts into the genome of an organism normally occur due to natural causes. These causes include environmental conditions and intracellular processes. Environmental inserts range from exposure to radioactive radiation such as Ultraviolet, mutagenic chemicals, or DNA viruses. Intracellular inserts can occur through heritable changes in parent cells or errors in DNA replication or DNA repair.
Gene insertion techniques can be used for characteristic mutations in an organism for a desired phenotypic gene expression. A gene insert change can be expressed in a large variety of ends. These variants can range from the loss, or gain, of protein function to changes in physical structure i.e., hair, or eye, color. The goal of changes in expression are focused on a gain of function in proteins for regulation or to termination of cellular function for prevention of disease. The results of the variations are dependent on the place in the genome the addition, or mutation is located. The aim is to learn, understand, and possibly predict the expr |
https://en.wikipedia.org/wiki/Cytidylate%20kinase | In enzymology, a cytidylate kinase () is an enzyme that catalyzes the chemical reaction
ATP + (d)CMP ADP + (d)CDP
Thus, the two substrates of this enzyme are ATP and dCMP, whereas its two products are ADP and dCDP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:CMP phosphotransferase. Other names in common use include: deoxycytidylate kinase, deoxycytidylate kinase, CMP kinase, CTP:CMP phosphotransferase, dCMP kinase, deoxycytidine monophosphokinase, UMP-CMP kinase, ATP:UMP-CMP phosphotransferase, and pyrimidine nucleoside monophosphate kinase. This enzyme participates in pyrimidine metabolism.
References
Further reading
EC 2.7.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/D-arabinokinase | In enzymology, a D-arabinokinase () is an enzyme that catalyzes the chemical reaction
ATP + D-arabinose ADP + D-arabinose 5-phosphate
Thus, the two substrates of this enzyme are ATP and D-arabinose, whereas its two products are ADP and D-arabinose 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-arabinose 5-phosphotransferase. This enzyme is also called D-arabinokinase (phosphorylating).
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dehydrogluconokinase | In enzymology, a dehydrogluconokinase () is an enzyme that catalyzes the chemical reaction
ATP + 2-dehydro-D-gluconate ADP + 6-phospho-2-dehydro-D-gluconate
Thus, the two substrates of this enzyme are ATP and 2-dehydro-D-gluconate, whereas its two products are ADP and 6-phospho-2-dehydro-D-gluconate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:2-dehydro-D-gluconate 6-phosphotransferase. Other names in common use include ketogluconokinase, 2-ketogluconate kinase, ketogluconokinase (phosphorylating), and 2-ketogluconokinase. This enzyme participates in pentose phosphate pathway.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deoxyadenosine%20kinase | In enzymology, a deoxyadenosine kinase () is an enzyme that catalyzes the chemical reaction
ATP + deoxyadenosine ADP + dAMP
Thus, the two substrates of this enzyme are ATP and deoxyadenosine, whereas its two products are ADP and dAMP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:deoxyadenosine 5'-phosphotransferase. This enzyme is also called purine-deoxyribonucleoside kinase. This enzyme participates in purine 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 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28deoxy%29adenylate%20kinase | In enzymology, a (deoxy)adenylate kinase () is an enzyme that catalyzes the chemical reaction
ATP + dAMP ADP + dADP
Thus, the two substrates of this enzyme are ATP and dAMP, whereas its two products are ADP and dADP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:(d)AMP phosphotransferase. This enzyme participates in purine metabolism.
References
EC 2.7.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deoxyguanosine%20kinase | In enzymology, a deoxyguanosine kinase () is an enzyme that catalyzes the chemical reaction
ATP + deoxyguanosine ADP + dGMP
Thus, the two substrates of this enzyme are ATP and deoxyguanosine, whereas its two products are ADP and dGMP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:deoxyguanosine 5'-phosphotransferase. Other names in common use include deoxyguanosine kinase (phosphorylating), (dihydroxypropoxymethyl)guanine kinase, 2'-deoxyguanosine kinase, and NTP-deoxyguanosine 5'-phosphotransferase. This enzyme participates in purine metabolism.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
Clinical
Mutations in this gene have been linked to inherited mitochondrial DNA depletion syndromes, neonatal liver failure, nystagmus and hypotonia.
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Deoxynucleoside%20kinase | In enzymology, a deoxynucleoside kinase () is an enzyme that catalyzes the chemical reaction
ATP + 2'-deoxynucleoside ADP + 2'-deoxynucleoside 5'-phosphate
Thus, the two substrates of this enzyme are ATP and 2'-deoxynucleoside, whereas its two products are ADP and 2'-deoxynucleoside 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:deoxynucleoside 5'-phosphotransferase. Other names in common use include multispecific deoxynucleoside kinase, ms-dNK, multisubstrate deoxyribonucleoside kinase, multifunctional deoxynucleoside kinase, D. melanogaster deoxynucleoside kinase, and Dm-dNK.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28deoxy%29nucleoside-phosphate%20kinase | In enzymology, a (deoxy)nucleoside-phosphate kinase () is an enzyme that catalyzes the chemical reaction
ATP + deoxynucleoside phosphate ADP + deoxynucleoside diphosphate
Thus, the two substrates of this enzyme are ATP and deoxynucleoside phosphate, whereas its two products are ADP and deoxynucleoside diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:deoxynucleoside-phosphate phosphotransferase. Other names in common use include deoxynucleoside monophosphate kinase, deoxyribonucleoside monophosphokinase, and deoxynucleoside-5'-monophosphate kinase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.7.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Dephospho-CoA%20kinase | In enzymology, a dephospho-CoA kinase () is an enzyme that catalyzes the chemical reaction
ATP + dephospho-CoA ADP + CoA
Thus, the two substrates of this enzyme are ATP and dephospho-CoA, whereas its two products are ADP and CoA.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:dephospho-CoA 3'-phosphotransferase. Other names in common use include dephosphocoenzyme A kinase (phosphorylating), 3'-dephospho-CoA kinase, and dephosphocoenzyme A kinase. This enzyme participates in pantothenate and coa biosynthesis.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Dephospho-%28reductase%20kinase%29%20kinase | In enzymology, a dephospho-[reductase kinase] kinase () is an enzyme that catalyzes the chemical reaction
ATP + dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} ADP + {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}
Thus, the two substrates of this enzyme are ATP and [[dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}]], whereas its two products are ADP and [[{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}]].
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} phosphotransferase. Other names in common use include AMP-activated kinase, AMP-activated protein kinase kinase, hydroxymethylglutaryl coenzyme A reductase kinase kinase, hydroxymethylglutaryl coenzyme A reductase kinase kinase, (phosphorylating), reductase kinase, reductase kinase kinase, and STK30.
References
EC 2.7.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diacylglycerol%20cholinephosphotransferase | In enzymology, a diacylglycerol cholinephosphotransferase () is an enzyme that catalyzes the chemical reaction
CDP-choline + 1,2-diacylglycerol CMP + a phosphatidylcholine
Thus, the two substrates of this enzyme are CDP-choline and 1,2-diacylglycerol, whereas its two products are CMP and phosphatidylcholine.
Classification
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups.
Nomenclature
The systematic name of this enzyme class is CDP choline:1,2-diacylglycerol cholinephosphotransferase. Other names in common use include:
1-alkyl-2-acetyl-m-glycerol:CDPcholine choline phosphotransferase,
1-alkyl-2-acetyl-sn-glycerol cholinephosphotransferase,
1-alkyl-2-acetylglycerol cholinephosphotransferase,
alkylacylglycerol choline phosphotransferase,
alkylacylglycerol cholinephosphotransferase,
CDP-choline diglyceride phosphotransferase,
cholinephosphotransferase,
CPT,
cytidine diphosphocholine glyceride transferase,
cytidine diphosphorylcholine diglyceride transferase,
diacylglycerol choline phosphotransferase,
phosphocholine diacylglyceroltransferase,
phosphorylcholine-glyceride transferase, and
sn-1,2-diacylglycerol cholinephosphotransferase.
Biological role
This enzyme participates in 3 metabolic pathways: aminophosphonate metabolism, glycerophospholipid metabolism, and ether lipid metabolism.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydrostreptomycin-6-phosphate%203%27alpha-kinase | In enzymology, a dihydrostreptomycin-6-phosphate 3'alpha-kinase () is an enzyme that catalyzes the chemical reaction
ATP + dihydrostreptomycin 6-phosphate ADP + dihydrostreptomycin 3'alpha,6-bisphosphate
Thus, the two substrates of this enzyme are ATP and dihydrostreptomycin 6-phosphate, whereas its two products are ADP and dihydrostreptomycin 3'alpha,6-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:dihydrostreptomycin-6-phosphate 3'alpha-phosphotransferase. Other names in common use include dihydrostreptomycin 6-phosphate kinase (phosphorylating), and ATP:dihydrostreptomycin-6-P 3'alpha-phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Selectfluor | Selectfluor, a trademark of Air Products and Chemicals, is a reagent in chemistry that is used as a fluorine donor. This compound is a derivative of the nucleophillic base DABCO. It is a colourless salt that tolerates air and even water. It has been commercialized for use for electrophilic fluorination.
Preparation
Selectfluor is synthesized by the N-alkylation of diazabicyclo[2.2.2]octane (DABCO) with dichloromethane, followed by ion exchange with sodium tetrafluoroborate (replacing the chloride counterion for the tetrafluoroborate). The resulting salt is treated with elemental fluorine and sodium tetrafluoroborate:
The cation is often depicted with one skewed ethylene ((CH2)2) group. In fact, these pairs of CH2 groups are eclipsed so that the cation has idealized C3h symmetry.
Mechanism of fluorination
Electrophilic fluorinating reagents could in principle operate by electron transfer pathways or an SN2 attack at fluorine. This distinction has not been decided. By using a charge-spin separated probe, it was possible to show that the electrophilic fluorination of stilbenes with Selectfluor proceeds through an SET/fluorine atom transfer mechanism.
In certain cases Selectfluor can transfer fluorine to alkyl radicals.
Applications
The conventional source of "electrophilic fluorine", i.e. the equivalent to the superelectrophile F+, is gaseous fluorine, which requires specialised equipment for manipulation. Selectfluor reagent is a salt, the use of which requires only ro |
https://en.wikipedia.org/wiki/Sodium%20tetrafluoroborate | Sodium tetrafluoroborate is an inorganic compound with formula NaBF4. It is a salt that forms colorless or white water-soluble rhombic crystals and is soluble in water (108 g/100 mL) but less soluble in organic solvents.
Sodium tetrafluoroborate is used in some fluxes used for brazing and to produce boron trifluoride.
Preparation
Sodium tetrafluoroborate can be prepared by neutralizing tetrafluoroboric acid with sodium carbonate or sodium hydroxide.
NaOH + HBF4 → NaBF4 + H2O
Na2CO3 + 2 HBF4 → 2 NaBF4 + H2O + CO2
Alternatively the chemical can be synthesized from boric acid, hydrofluoric acid, and sodium carbonate:
2H3BO3 + 8HF + Na2CO3 → 2NaBF4 + 7H2O + CO2
Reactions and uses
On heating to its melting point, sodium tetrafluoroborate decomposes to sodium fluoride and boron trifluoride:
NaBF4 → NaF + BF3
It is a source of tetrafluoroborate anion, which is used in organic chemistry for the preparation of salts. Sodium tetrafluoroborate can be used for synthesis of ionic liquids, where tetrafluoroborate is the anion.
References
Tetrafluoroborates
Sodium compounds
Brazing and soldering |
https://en.wikipedia.org/wiki/Diphosphate%E2%80%94glycerol%20phosphotransferase | In enzymology, a diphosphate-glycerol phosphotransferase () is an enzyme that catalyzes the chemical reaction
diphosphate + glycerol phosphate + glycerol 1-phosphate
Thus, the two substrates of this enzyme are diphosphate and glycerol, whereas its two products are phosphate and glycerol 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is diphosphate:glycerol 1-phosphotransferase. Other names in common use include PPi-glycerol phosphotransferase, and pyrophosphate-glycerol phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diphosphate-purine%20nucleoside%20kinase | In enzymology, a diphosphate-purine nucleoside kinase () is an enzyme that catalyzes the chemical reaction
diphosphate + a purine nucleoside phosphate + a purine mononucleotide
Thus, the two substrates of this enzyme are diphosphate and purine nucleoside, whereas its two products are phosphate and purine mononucleotide.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is diphosphate:purine nucleoside phosphotransferase. This enzyme is also called pyrophosphate-purine nucleoside kinase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diphosphate%E2%80%94serine%20phosphotransferase | In enzymology, a diphosphate-serine phosphotransferase () is an enzyme that catalyzes the chemical reaction
diphosphate + L-serine phosphate + O-phospho-L-serine
Thus, the two substrates of this enzyme are diphosphate and L-serine, whereas its two products are phosphate and O-phospho-L-serine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is diphosphate:L-serine O-phosphotransferase. Other names in common use include pyrophosphate-serine phosphotransferase, and pyrophosphate-L-serine phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diphosphoinositol-pentakisphosphate%20kinase | In enzymology, a diphosphoinositol-pentakisphosphate kinase () is an enzyme that catalyzes the chemical reaction
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate (isomeric configuration unknown)
Thus, the two substrates of this enzyme are ATP and 1D-myo-inositol 5-diphosphate pentakisphosphate, whereas its 3 products are ADP, 1D-myo-inositol bisdiphosphate tetrakisphosphate and (isomeric configuration unknown).
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:1D-myo-inositol-5-diphosphate-pentakisphosphate phosphotransferase. Other names in common use include PP-IP5 kinase, diphosphoinositol pentakisphosphate kinase, and ATP:5-diphospho-1D-myo-inositol-pentakisphosphate phosphotransferase.
References
EC 2.7.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dolichol%20kinase | In enzymology, a dolichol kinase () is an enzyme that catalyzes the chemical reaction
CTP + dolichol CDP + dolichyl phosphate
Thus, the two substrates of this enzyme are CTP and dolichol, whereas its two products are CDP and dolichyl phosphate.
This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is CTP:dolichol O-phosphotransferase. This enzyme is also called dolichol phosphokinase. This enzyme participates in N-glycan biosynthesis.
In humans dolichol kinase is encoded by the DOLK gene.
Function
Dolichyl monophosphate is an essential glycosyl carrier lipid for C- and O-mannosylation and N-glycosylation of proteins and for biosynthesis of glycosylphosphatidylinositol anchors in endoplasmic reticulum (ER). Dolichol kinase catalyzes CTP-mediated phosphorylation of dolichol, the terminal step in de novo dolichyl monophosphate biosynthesis.
Clinical significance
Mutations in DOLK cause a subtype of the congenital disorders of glycosylation, DOLK-CDG (CDG-Im).
See also
Dolichol kinase deficiency
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dolichyl-diphosphate%E2%80%94polyphosphate%20phosphotransferase | In enzymology, a dolichyl-diphosphate-polyphosphate phosphotransferase () is an enzyme that catalyzes the chemical reaction
dolichyl diphosphate + (phosphate)n dolichyl phosphate + (phosphate)n+1
Thus, the two substrates of this enzyme are dolichyl diphosphate and (phosphate)n, whereas its two products are dolichyl phosphate and (phosphate)n+1.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is dolichyl-diphosphate:polyphosphate phosphotransferase. This enzyme is also called dolichylpyrophosphate:polyphosphate phosphotransferase.
References
EC 2.7.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-ribitol-5-phosphate%20cytidylyltransferase | In enzymology, a D-ribitol-5-phosphate cytidylyltransferase () is an enzyme that catalyzes the chemical reaction
CTP + D-ribitol 5-phosphate diphosphate + CDP-ribitol
Thus, the two substrates of this enzyme are CTP and D-ribitol 5-phosphate, whereas its two products are diphosphate and CDP-ribitol.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:D-ribitol-5-phosphate cytidylyltransferase. Other names in common use include CDP ribitol pyrophosphorylase, cytidine diphosphate ribitol pyrophosphorylase, ribitol 5-phosphate cytidylyltransferase, and cytidine diphosphoribitol pyrophosphorylase. This enzyme participates in pentose and glucuronate interconversions.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-ribulokinase | In enzymology, a D-ribulokinase () is an enzyme that catalyzes the chemical reaction
ATP + D-ribulose ADP + D-ribulose 5-phosphate
Thus, the two substrates of this enzyme are ATP and D-ribulose, whereas its two products are ADP and D-ribulose 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-ribulose 5-phosphotransferase. This enzyme is also called D-ribulokinase (phosphorylating). This enzyme participates in pentose and glucuronate interconversions.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Elongation%20factor%202%20kinase | In enzymology, an elongation factor 2 kinase () is an enzyme that catalyzes the chemical reaction:
ATP + [elongation factor 2] ADP + [elongation factor 2] phosphate.
Thus, the two substrates of this enzyme are ATP and elongation factor 2, whereas its two products are adenosine diphosphate (ADP) and elongation factor 2 phosphate.
Nomenclature
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is "ATP:[elongation factor 2] phosphotransferase". Other names in common use include Ca/CaM-kinase III, calmodulin-dependent protein kinase III, CaM kinase III, eEF2 kinase, eEF-2K, eEF2K, EF2K, and STK19.
Function
The only known physiological substrate of eEF-2K is eEF-2. Phosphorylation of eEF-2 at Thr-56 by eEF-2K leads to inhibition of the elongation phase of protein synthesis. Phosphorylation of Thr-56 is thought to reduce the affinity of eEF-2 for the ribosome, thereby slowing down the overall rate of elongation. However, there is growing evidence to suggest that translation of certain mRNAs is actually increased by phosphorylation of eEF-2 by eEF-2K, especially in a neuronal context.
Activation
The activity of eEF-2K is dependent on calcium and calmodulin. Activation of eEF-2K proceeds by a sequential two-step mechanism. First, calcium-calmodulin binds with high affinity t |
https://en.wikipedia.org/wiki/Erythritol%20kinase | In enzymology, an erythritol kinase () is an enzyme that catalyzes the chemical reaction
ATP + erythritol ADP + D-erythritol 4-phosphate
Thus, the two substrates of this enzyme are ATP and erythritol, whereas its two products are ADP and D-erythritol 4-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:erythritol 4-phosphotransferase. This enzyme is also called erythritol kinase (phosphorylating).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/The%20Toynbee%20Convector%20%28short%20story%20collection%29 | The Toynbee Convector is a short story collection by American writer Ray Bradbury. Several of the stories are original to this collection. Others originally appeared in the magazines Playboy, Omni, Gallery, Ellery Queen's Mystery Magazine, Woman's Day, and Weird Tales.
Contents
"The Toynbee Convector"
"Trapdoor"
"On the Orient, North"
"One Night in Your Life"
"West of October"
"The Last Circus"
"The Laurel and Hardy Love Affair"
"I Suppose You Are Wondering Why We Are Here?"
"Lafayette, Farewell"
"Banshee"
"Promises, Promises"
"The Love Affair"
"One for His Lordship, and One for the Road!"
"At Midnight, in the Month of June"
"Bless Me Father, for I Have Sinned"
"By the Numbers!"
"A Touch of Petulance"
"Long Division"
"Come, and Bring Constance!"
"Junior"
"The Tombstone"
"The Thing at the Top of the Stairs"
"Colonel Stonesteel’s Genuine Home-Made Truly Egyptian Mummy"
References
External links
1988 short story collections
Short story collections by Ray Bradbury |
https://en.wikipedia.org/wiki/Ethanolamine%20kinase | In enzymology, an ethanolamine kinase () is an enzyme that catalyzes the chemical reaction
ATP + ethanolamine ADP + O-phosphoethanolamine
Thus, the two substrates of this enzyme are ATP and ethanolamine, whereas its two products are ADP and O-phosphoethanolamine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:ethanolamine O-phosphotransferase. Other names in common use include ethanolamine kinase (phosphorylating), and ethanolamine phosphokinase. This enzyme participates in glycerophospholipid metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ethanolamine-phosphate%20cytidylyltransferase | In enzymology, an ethanolamine-phosphate cytidylyltransferase () is an enzyme that catalyzes the chemical reaction
CTP + ethanolamine phosphate diphosphate + CDP-ethanolamine
Thus, the two substrates of this enzyme are CTP and ethanolamine phosphate, whereas its two products are diphosphate and CDP-ethanolamine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:ethanolamine-phosphate cytidylyltransferase. Other names in common use include phosphorylethanolamine transferase, ET, CTP-phosphoethanolamine cytidylyltransferase, phosphoethanolamine cytidylyltransferase, and ethanolamine phosphate cytidylyltransferase. This enzyme participates in aminophosphonate metabolism and glycerophospholipid metabolism.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diacylglycerol%20ethanolaminephosphotransferase | In enzymology, an ethanolaminephosphotransferase () is an enzyme that catalyzes the chemical reaction
CDP-ethanolamine + 1,2-diacylglycerol CMP + a phosphatidylethanolamine
Thus, the two substrates of this enzyme are CDP-ethanolamine and 1,2-diacylglycerol, whereas its two products are CMP and phosphatidylethanolamine.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-ethanolamine:1,2-diacylglycerol ethanolaminephosphotransferase. Other names in common use include EPT, diacylglycerol ethanolaminephosphotransferase, CDPethanolamine diglyceride phosphotransferase, and phosphorylethanolamine-glyceride transferase. This enzyme participates in 3 metabolic pathways: aminophosphonate metabolism, glycerophospholipid metabolism, and ether lipid metabolism.
References
EC 2.7.8
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Farnesyl-diphosphate%20kinase | In enzymology, a farnesyl-diphosphate kinase () is an enzyme that catalyzes the chemical reaction
ATP + farnesyl diphosphate ADP + farnesyl triphosphate
Thus, the two substrates of this enzyme are ATP and farnesyl diphosphate, whereas its two products are ADP and farnesyl triphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:farnesyl-diphosphate phosphotransferase. This enzyme is also called farnesyl pyrophosphate kinase.
References
EC 2.7.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/FMN%20adenylyltransferase | In enzymology, a FMN adenylyltransferase () is an enzyme that catalyzes the chemical reaction
ATP + FMN diphosphate + FAD
Thus, the two substrates of this enzyme are ATP and FMN, whereas its two products are diphosphate and FAD.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:FMN adenylyltransferase. This enzyme participates in riboflavin metabolism.
Other names
Other names in common use include
FAD pyrophosphorylase
riboflavin mononucleotide adenylyltransferase
adenosine triphosphate-riboflavin mononucleotide transadenylase
adenosine triphosphate-riboflavine mononucleotide transadenylase
FAD synthetase
riboflavin adenine dinucleotide pyrophosphorylase
riboflavine
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Formate%20kinase | In enzymology, a formate kinase () is an enzyme that catalyzes the chemical reaction
ATP + formate ADP + formyl phosphate
Thus, the two substrates of this enzyme are ATP and formate, whereas its two products are ADP and formyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:formate phosphotransferase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 2.7.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Fucokinase | In enzymology, a fucokinase () is an enzyme that catalyzes the chemical reaction
ATP + L-fucose ADP + beta-L-fucose 1-phosphate
Thus, the two substrates of this enzyme are ATP and L-fucose, whereas its two products are ADP and beta-L-fucose 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:beta-L-fucose 1-phosphotransferase. Other names in common use include fucokinase (phosphorylating), fucose kinase, L-fucose kinase, L-fucokinase, ATP:6-deoxy-L-fucose 1-phosphotransferase, and ATP:L-fucose 1-phosphotransferase. Fucokinase is commonly abbreviated as fuc-K. This enzyme participates in fructose and mannose metabolism. Fucokinase is the only enzyme that is converting L-fucose to fucose-1-phosphate and it can be further used for synthesizing GDP-fucose, which is the donor substrate for all fucosyltransferase.
L-Fucokinase activity can be detected in varied tissues within an animal. For instance, rats and mice contain L-fucokinase widely distributed throughout tissues especially higher in the brain. However, the levels of L-fucokinase in the brain is widely different among species.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Fucose-1-phosphate%20guanylyltransferase | In enzymology, a fucose-1-phosphate guanylyltransferase () is an enzyme that catalyzes the chemical reaction
GTP + beta-L-fucose 1-phosphate diphosphate + GDP-L-fucose
Thus, the two substrates of this enzyme are GTP and beta-L-fucose 1-phosphate, whereas its two products are diphosphate and GDP-L-fucose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GTP:beta-L-fucose-1-phosphate guanylyltransferase. Other names in common use include GDP fucose pyrophosphorylase, guanosine diphosphate L-fucose pyrophosphorylase, GDP-L-fucose pyrophosphorylase, GDP-fucose pyrophosphorylase, and GTP:L-fucose-1-phosphate guanylyltransferase. This enzyme participates in fructose and mannose metabolism.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Galactose-1-phosphate%20thymidylyltransferase | In enzymology, a galactose-1-phosphate thymidylyltransferase () is an enzyme that catalyzes the chemical reaction
dTTP + alpha-D-galactose 1-phosphate diphosphate + dTDP-galactose
Thus, the two substrates of this enzyme are dTTP and alpha-D-galactose 1-phosphate, whereas its two products are diphosphate and dTDP-galactose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is dTTP:alpha-D-galactose-1-phosphate thymidylyltransferase. Other names in common use include dTDP galactose pyrophosphorylase, galactose 1-phosphate thymidylyl transferase, thymidine diphosphogalactose pyrophosphorylase, thymidine triphosphate:alpha-D-galactose 1-phosphate, and thymidylyltransferase. This enzyme participates in nucleotide sugars metabolism.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Galacturonokinase | In enzymology, a galacturonokinase () is an enzyme that catalyzes the chemical reaction
ATP + D-galacturonate ADP + 1-phospho-alpha-D-galacturonate
Thus, the two substrates of this enzyme are ATP and D-galacturonate, whereas its two products are ADP and 1-phospho-alpha-D-galacturonate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-galacturonate 1-phosphotransferase. This enzyme is also called galacturonokinase (phosphorylating) D-galacturonic acid kinase. This enzyme participates in nucleotide sugars metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Gentamicin%202%22-nucleotidyltransferase | In enzymology, a gentamicin 2"-nucleotidyltransferase () is an enzyme that catalyzes the chemical reaction
nucleoside triphosphate + gentamicin diphosphate + 2"-nucleotidylgentamicin
Thus, the two substrates of this enzyme are nucleoside triphosphate and gentamicin, whereas its two products are diphosphate and 2''-nucleotidylgentamicin.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is NTP:gentamicin 2"-nucleotidyltransferase. Other names in common use include gentamicin 2"-adenylyltransferase, aminoglycoside adenylyltransferase, and gentamicin 2"-nucleotidyltransferase.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Gluconokinase | In enzymology, a gluconokinase () is an enzyme that catalyzes the chemical reaction
ATP + D-gluconate ADP + 6-phospho-D-gluconate
Thus, the two substrates of this enzyme are ATP and D-gluconate, whereas its two products are ADP and 6-phospho-D-gluconate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-gluconate 6-phosphotransferase. Other names in common use include gluconokinase (phosphorylating), and gluconate kinase. This enzyme participates in pentose phosphate pathway.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Nitronium%20tetrafluoroborate | Nitronium tetrafluoroborate is an inorganic compound with formula NO2BF4. It is a salt of nitronium cation and tetrafluoroborate anion. It is a colorless crystalline solid, which reacts with water to form the corrosive acids HF and HNO3. As such, it must be handled under water-free conditions. It is sparsely soluble in many organic solvents.
Preparation
Nitronium tetrafluoroborate can be prepared by adding a mixture of anhydrous hydrogen fluoride and boron trifluoride to a nitromethane solution of nitric acid or dinitrogen pentoxide.
Applications
Nitronium tetrafluoroborate is used as a nitration agent.
References
Tetrafluoroborates
Nitronium compounds |
https://en.wikipedia.org/wiki/Glucosamine%20kinase | In enzymology, a glucosamine kinase () is an enzyme that catalyzes the chemical reaction
ATP + D-glucosamine ADP + D-glucosamine phosphate
Thus, the two substrates of this enzyme are ATP and D-glucosamine, whereas its two products are ADP and D-glucosamine phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-glucosamine phosphotransferase. Other names in common use include glucosamine kinase (phosphorylating), ATP:2-amino-2-deoxy-D-glucose-6-phosphotransferase, and aminodeoxyglucose kinase. This enzyme participates in aminosugars metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucose-1-phosphate%20adenylyltransferase | In enzymology, a glucose-1-phosphate adenylyltransferase () is an enzyme that catalyzes the chemical reaction
ATP + alpha-D-glucose 1-phosphate diphosphate + ADP-glucose
Thus, the two substrates of this enzyme are ATP and alpha-D-glucose 1-phosphate, whereas its two products are diphosphate and ADP-glucose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:alpha-D-glucose-1-phosphate adenylyltransferase. Other names in common use include ADP glucose pyrophosphorylase, glucose 1-phosphate adenylyltransferase, adenosine diphosphate glucose pyrophosphorylase, adenosine diphosphoglucose pyrophosphorylase, ADP-glucose pyrophosphorylase, ADP-glucose synthase, ADP-glucose synthetase, ADPG pyrophosphorylase, ADP:alpha-D-glucose-1-phosphate adenylyltransferase and AGPase. This enzyme participates in starch and sucrose metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glucose-1-phosphate%20cytidylyltransferase | In enzymology, a glucose-1-phosphate cytidylyltransferase () is an enzyme that catalyzes the chemical reaction
CTP + alpha-D-glucose 1-phosphate diphosphate + CDP-glucose
Thus, the two substrates of this enzyme are CTP and alpha-D-glucose 1-phosphate, whereas its two products are diphosphate and CDP-glucose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:alpha-D-glucose-1-phosphate cytidylyltransferase. Other names in common use include CDP glucose pyrophosphorylase, cytidine diphosphoglucose pyrophosphorylase, cytidine diphosphate glucose pyrophosphorylase, cytidine diphosphate-D-glucose pyrophosphorylase, and CTP:D-glucose-1-phosphate cytidylyltransferase. This enzyme participates in starch and sucrose metabolism and nucleotide sugars metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glucose-1-phosphate%20guanylyltransferase | In enzymology, a glucose-1-phosphate guanylyltransferase () is an enzyme that catalyzes the chemical reaction
GTP + alpha-D-glucose 1-phosphate diphosphate + GDP-glucose
Thus, the two substrates of this enzyme are GTP and alpha-D-glucose 1-phosphate, whereas its two products are diphosphate and GDP-glucose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GTP:alpha-D-glucose-1-phosphate guanylyltransferase. Other names in common use include GDP glucose pyrophosphorylase, and guanosine diphosphoglucose pyrophosphorylase. This enzyme participates in starch and sucrose metabolism.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucose-1-phosphate%20phosphodismutase | In enzymology, a glucose-1-phosphate phosphodismutase () is an enzyme that catalyzes the chemical reaction
2 D-glucose 1-phosphate D-glucose + D-glucose 1,6-bisphosphate
Hence, this enzyme has one substrate, D-glucose 1-phosphate, and two products, D-glucose and D-glucose 1,6-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is D-glucose-1-phosphate:D-glucose-1-phosphate 6-phosphotransferase. This enzyme participates in glycolysis / gluconeogenesis and starch and sucrose metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucose-1-phosphate%20thymidylyltransferase | In enzymology, a glucose-1-phosphate thymidylyltransferase () is an enzyme that catalyzes the chemical reaction
dTTP + alpha-D-glucose 1-phosphate diphosphate + dTDP-glucose
Thus, the two substrates of this enzyme are dTTP and alpha-D-glucose 1-phosphate, whereas its two products are pyrophosphate and dTDP-glucose.
This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). This enzyme participates in 3 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, and polyketide sugar unit biosynthesis.
Nomenclature
The systematic name of this enzyme class is dTTP:alpha-D-glucose-1-phosphate thymidylyltransferase. Other names in common use include:
glucose 1-phosphate thymidylyltransferase,
dTDP-glucose synthase, dTDP-glucose pyrophosphorylase,
thymidine diphosphoglucose pyrophosphorylase,
thymidine diphosphate glucose pyrophosphorylase, and
TDP-glucose pyrophosphorylase.
Structural studies
As of late 2007, 19 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , and .
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glucuronate-1-phosphate%20uridylyltransferase | In enzymology, a glucuronate-1-phosphate uridylyltransferase () is an enzyme that catalyzes the chemical reaction
UTP + 1-phospho-alpha-D-glucuronate diphosphate + UDP-glucuronate
Thus, the two substrates of this enzyme are UTP and 1-phospho-alpha-D-glucuronate, whereas its two products are diphosphate and UDP-glucuronate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UTP:1-phospho-alpha-D-glucuronate uridylyltransferase. Other names in common use include UDP-glucuronate pyrophosphorylase, UDP-D-glucuronic acid pyrophosphorylase, UDP-glucuronic acid pyrophosphorylase, and uridine diphosphoglucuronic pyrophosphorylase. This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucuronokinase | In enzymology, a glucuronokinase () is an enzyme that catalyzes the chemical reaction
ATP + D-glucuronate ADP + 1-phospho-alpha-D-glucuronate
Thus, the two substrates of this enzyme are ATP and D-glucuronate, whereas its two products are ADP and 1-phospho-alpha-D-glucuronate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-glucuronate 1-phosphotransferase. Other names in common use include glucuronokinase (phosphorylating), and glucurono-glucuronokinase. This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutamate%201-kinase | In enzymology, a glutamate 1-kinase () is an enzyme that catalyzes the chemical reaction
ATP + L-glutamate ADP + alpha-L-glutamyl phosphate
Thus, the two substrates of this enzyme are ATP and L-glutamate, whereas its two products are ADP and alpha-L-glutamyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:L-glutamate 1-phosphotransferase.
References
EC 2.7.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutamate%205-kinase | In enzymology, a glutamate 5-kinase () is an enzyme that catalyzes the chemical reaction
ATP + L-glutamate ADP + L-glutamate 5-phosphate
Thus, the two substrates of this enzyme are ATP and L-glutamate, whereas its two products are ADP and L-glutamate 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:L-glutamate 5-phosphotransferase. Other names in common use include ATP-L-glutamate 5-phosphotransferase, ATP:gamma-L-glutamate phosphotransferase, gamma-glutamate kinase, gamma-glutamyl kinase, and glutamate kinase. This enzyme participates in urea cycle and metabolism of amino groups.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.7.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28glutamate%E2%80%94ammonia-ligase%29%20adenylyltransferase | In enzymology, a [glutamate—ammonia-ligase] adenylyltransferase () is an enzyme that catalyzes the chemical reaction
ATP + [L-glutamate:ammonia ligase (ADP-forming)] diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]
Thus, the two substrates of this enzyme are ATP and L-glutamate:ammonia ligase (ADP-forming), whereas its two products are diphosphate and adenylyl-[L-glutamate:ammonia ligase (ADP-forming)].
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase. Other names in common use include glutamine-synthetase adenylyltransferase, ATP:glutamine synthetase adenylyltransferase, and adenosine triphosphate:glutamine synthetase adenylyltransferase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
Glutamate-ammonia-ligase
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glycerate%20kinase | In enzymology, a glycerate kinase () is an enzyme that catalyzes the chemical reaction
ATP + (R)-glycerate ADP + 3-phospho-(R)-glycerate
or
ATP + (R)-glycerate ADP + 2-phospho-(R)-glycerate
Thus, the two substrates of this enzyme are ATP and (R)-glycerate, whereas its two products are ADP and either 3-phospho-(R)-glycerate or 2-phospho-(R)-glycerate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:(R)-glycerate 3-phosphotransferase. Other names in common use include glycerate kinase (phosphorylating), D-glycerate 3-kinase, D-glycerate kinase, glycerate-3-kinase, GK, D-glyceric acid kinase, and ATP:D-glycerate 2-phosphotransferase. This enzyme participates in 3 metabolic pathways: serine/glycine/threonine metabolism, glycerolipid metabolism, and glyoxylate-dicarboxylate metabolism.
This enzyme had been thought to produce 3-phosphoglycerate, but some glycerate kinases produce 2-phosphoglycerate instead.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glycerol-3-phosphate%20cytidylyltransferase | In enzymology, a glycerol-3-phosphate cytidylyltransferase () is an enzyme that catalyzes the chemical reaction
CTP + sn-glycerol 3-phosphate diphosphate + CDP-glycerol
Thus, the two substrates of this enzyme are CTP and sn-glycerol 3-phosphate, whereas its two products are diphosphate and CDP-glycerol.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:sn-glycerol-3-phosphate cytidylyltransferase. Other names in common use include CDP-glycerol pyrophosphorylase, cytidine diphosphoglycerol pyrophosphorylase, cytidine diphosphate glycerol pyrophosphorylase, CTP:glycerol 3-phosphate cytidylyltransferase, and Gro-PCT. This enzyme participates in glycerophospholipid metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glycerol-3-phosphate%E2%80%94glucose%20phosphotransferase | In enzymology, a glycerol-3-phosphate-glucose phosphotransferase () is an enzyme that catalyzes the chemical reaction
sn-glycerol 3-phosphate + D-glucose glycerol + D-glucose 6-phosphate
Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and D-glucose, whereas its two products are glycerol and D-glucose 6-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is sn-glycerol-3-phosphate:D-glucose 6-phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerone%20kinase | In enzymology, a glycerone kinase () is an enzyme that catalyzes the chemical reaction
ATP + glycerone ADP + glycerone phosphate
Thus, the two substrates of this enzyme are ATP and glycerone, whereas its two products are ADP and glycerone phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:glycerone phosphotransferase. Other names in common use include dihydroxyacetone kinase, acetol kinase, and acetol kinase (phosphorylating). This enzyme participates in glycerolipid metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Goodpasture-antigen-binding%20protein%20kinase | In enzymology, a Goodpasture-antigen-binding protein kinase () is an enzyme that catalyzes the chemical reaction
ATP + Goodpasture antigen-binding protein ADP + [Goodpasture antigen-binding phosphoprotein]
Thus, the two substrates of this enzyme are ATP and Goodpasture antigen-binding protein, whereas its two products are ADP and Goodpasture antigen-binding phosphoprotein.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[Goodpasture antigen-binding protein] phosphotransferase. Other names in common use include GPBPK, GPBP kinase, STK11, and Goodpasture antigen-binding protein kinase. This enzyme participates in mTOR signaling pathway and adipocytokine signaling pathway.
References
EC 2.7.11
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/GTP%20diphosphokinase | In enzymology, a GTP diphosphokinase () is an enzyme that catalyzes the chemical reaction
ATP + GTP AMP + guanosine 3'-diphosphate 5'-triphosphate
Thus, the two substrates of this enzyme are ATP and GTP, whereas its two products are AMP and guanosine 3'-diphosphate 5'-triphosphate.
This enzyme belongs to the family of transferases, specifically those transferring two phosphorus-containing groups (diphosphotransferases). The systematic name of this enzyme class is ATP:GTP 3'-diphosphotransferase. Other names in common use include stringent factor, guanosine 3',5'-polyphosphate synthase, GTP pyrophosphokinase, ATP-GTP 3'-diphosphotransferase, guanosine 5',3'-polyphosphate synthetase, (p)ppGpp synthetase I, (p)ppGpp synthetase II, guanosine pentaphosphate synthetase, GPSI, and GPSII. This enzyme participates in purine metabolism.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 2.7.6
Enzymes of known structure |
https://en.wikipedia.org/wiki/Guanidinoacetate%20kinase | In enzymology, a guanidinoacetate kinase () is an enzyme that catalyzes the chemical reaction
ATP + guanidinoacetate ADP + phosphoguanidinoacetate
Thus, the two substrates of this enzyme are ATP and guanidinoacetate, whereas its two products are ADP and phosphoguanidinoacetate.
Guanidinoacetate kinase belongs to the family of transferases, specifically those that transfer phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:guanidinoacetate N-phosphotransferase. This enzyme is also called glycocyamine kinase. This enzyme participates in arginine and proline metabolism.
References
EC 2.7.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ch%C3%A2teau%20La%20Mission%20Haut-Brion | Château la Mission Haut-Brion is a Bordeaux wine from the Pessac-Léognan appellation, classed among the Crus Classés in the Graves classification of 1953. La Mission Haut-Brion is the sister property of the First Growth Château Haut-Brion. The winery, located in close vicinity of the city of Bordeaux, belongs to the wine region Graves, in the commune of Talence with additional property in Pessac.
The château also produces a second wine from younger vines, La Chapelle de la Mission, since the 1991 vintage, and the dry white wine Château La Mission Haut-Brion Blanc since the 2010 merger of Château Laville Haut-Brion.
History
In the early 16th century, the land belonged to the family de Rostaing, of the house of de la Tour d'Esquivens, then called Arrejedhuys, planted with vines before it was passed to the Lestonnac family in 1540. In 1650, Olive de Lestonnac bequeathed an annuity to a religious order for their works of Christian charity in the countryside around Bordeaux. Her daughter-in-law, Catherine de Mullet, was the executor of Olive's will and the annuity was settled on the Congregation for the Clergy, then transferred, in 1682, to the Lazarists Fathers. The priests cultivated grapes for nearly 130 years, until the French Revolution, leaving behind monastic foundations that were expropriated by the state. It was acquired by Martial-Victor Vaillant in November 1792 for 302,000 livres, and for nearly one hundred years it was owned by the Chiapella family.
In 1919 it wa |
https://en.wikipedia.org/wiki/Guanosine-triphosphate%20guanylyltransferase | In enzymology, a guanosine-triphosphate guanylyltransferase () is an enzyme that catalyzes the chemical reaction
2 GTP diphosphate + P1,P4-bis(5'-guanosyl) tetraphosphate
Hence, this enzyme has one substrate, GTP, and two products, diphosphate and P1,P4-bis(5'-guanosyl) tetraphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GTP:GTP guanylyltransferase. Other names in common use include diguanosine tetraphosphate synthetase, GTP-GTP guanylyltransferase, Gp4G synthetase, and guanosine triphosphate-guanose triphosphate guanylyltransferase.
References
EC 2.7.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Guanylate%20kinase | In enzymology, a guanylate kinase () is an enzyme that catalyzes the chemical reaction
ATP + GMP ADP + GDP
Thus, the two substrates of this enzyme are ATP and GMP, whereas its two products are ADP and GDP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. This enzyme participates in purine metabolism.
Guanylate kinase catalyzes the ATP-dependent phosphorylation of GMP into GDP. It is essential for recycling GMP and indirectly, cGMP. In prokaryotes (such as Escherichia coli), lower eukaryotes (such as yeast) and in vertebrates, GK is a highly conserved monomeric protein of about 200 amino acids. GK has been shown to be structurally similar to protein A57R (or SalG2R) from various strains of Vaccinia virus.
Systems biology analyses carried out by the team of Andreas Dräger also identified a pivotal role of this enzyme in the replication of SARS-CoV-2 within the human airways.
Nomenclature
The systematic name of this enzyme class is ATP:(d)GMP phosphotransferase. Other names in common use include"
deoxyguanylate kinase,
5'-GMP kinase,
GMP kinase,
guanosine monophosphate kinase, and
ATP:GMP phosphotransferase.
References
Further reading
EC 2.7.4
Enzymes of known structure
Protein domains |
https://en.wikipedia.org/wiki/Hamamelose%20kinase | In enzymology, a hamamelose kinase () is an enzyme that catalyzes the chemical reaction
ATP + D-hamamelose ADP + D-hamamelose 2'-phosphate
Thus, the two substrates of this enzyme are ATP and D-hamamelose, whereas its two products are ADP and D-hamamelose 2'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-hamamelose 2'-phosphotransferase. Other names in common use include hamamelose kinase (phosphorylating), hamamelosekinase (ATP: hamamelose 2'-phosphotransferase), and ATP/hamamelose 2'-phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Histidine%20kinase | Histidine kinases (HK) are multifunctional, and in non-animal kingdoms, typically transmembrane, proteins of the transferase class of enzymes that play a role in signal transduction across the cellular membrane. The vast majority of HKs are homodimers that exhibit autokinase, phosphotransfer, and phosphatase activity. HKs can act as cellular receptors for signaling molecules in a way analogous to tyrosine kinase receptors (RTK). Multifunctional receptor molecules such as HKs and RTKs typically have portions on the outside of the cell (extracellular domain) that bind to hormone- or growth factor-like molecules, portions that span the cell membrane (transmembrane domain), and portions within the cell (intracellular domain) that contain the enzymatic activity. In addition to kinase activity, the intracellular domains typically have regions that bind to a secondary effector molecule or complex of molecules that further propagate signal transduction within the cell. Distinct from other classes of protein kinases, HKs are usually parts of a two-component signal transduction mechanisms in which HK transfers a phosphate group from ATP to a histidine residue within the kinase, and then to an aspartate residue on the receiver domain of a response regulator protein (or sometimes on the kinase itself). More recently, the widespread existence of protein histidine phosphorylation distinct from that of two-component histidine kinases has been recognised in human cells. In marked contrast t |
https://en.wikipedia.org/wiki/Holo-ACP%20synthase | In enzymology, a holo-ACP synthase () is an enzyme that catalyzes the chemical reaction
2'-(5"-triphosphoribosyl)-3'-dephospho-CoA + apo-citrate lyase holo-citrate lyase + diphosphate
Thus, the two substrates of this enzyme are 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA and apo-citrate lyase, whereas its two products are holo-citrate lyase and diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase adenylyltransferase. Other names in common use include 2'-(5"-phosphoribosyl)-3'-dephospho-CoA transferase, 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase, and CitX. This enzyme participates in two-component system - general.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.7.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Holo-%28acyl-carrier-protein%29%20synthase | In enzymology and molecular biology, a holo-[acyl-carrier-protein] synthase (ACPS, ) is an enzyme that catalyzes the chemical reaction:
CoA-[4'-phosphopantetheine] + apo-acyl carrier protein adenosine 3',5'-bisphosphate + holo-acyl carrier protein
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. It is also known as 4'-phosphopantetheinyl transferase after the group it transfers.
Function
All ACPS enzymes known so far are evolutionally related to each other in a single superfamily of proteins. It transfers a 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to an invariant serine in an acyl carrier protein (ACP), a small protein responsible for acyl group activation in fatty acid biosynthesis. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. This superfamily consists of two subtypes: the trimeric ACPS type such as E. coli ACPS and the monomeric Sfp (PCP-synthesizing) type such as B. subtilis SFP. Structures from both families are now known. The active site accommodates a magnesium ion. The most highly conserved regions of the protein are involved in binding the magnesium ion.
Nomenclature
The systematic name of this enzyme class is CoA-[4'-phosphopantetheine]:apo-[acyl-carrier-protein] 4'-pantetheinephosphotransferase. Other names in common use, disregarding the synthetase/synthase spelling d |
https://en.wikipedia.org/wiki/Homoserine%20kinase | In enzymology, a homoserine kinase () is an enzyme that catalyzes the chemical reaction
ATP + L-homoserine ADP + O-phospho-L-homoserine
Thus, the two substrates of this enzyme are ATP and L-homoserine, whereas its two products are ADP and O-phospho-L-homoserine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:L-homoserine O-phosphotransferase. Other names in common use include homoserine kinase (phosphorylating), and HSK. This enzyme participates in glycine, serine and threonine metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Hydroxyethylthiazole%20kinase | In enzymology, a hydroxyethylthiazole kinase () is an enzyme that catalyzes the chemical reaction
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
Thus, the two substrates of this enzyme are ATP and 4-methyl-5-(2-hydroxyethyl)thiazole, whereas its two products are ADP and 4-methyl-5-(2-phosphonooxyethyl)thiazole.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:4-methyl-5-(2-hydroxyethyl)thiazole 2-phosphotransferase. Other names in common use include hydroxyethylthiazole kinase (phosphorylating), and 4-methyl-5-(beta-hydroxyethyl)thiazole kinase. This enzyme participates in thiamine metabolism. Thiamine pyrophosphate (TPP), a required cofactor for many enzymes in the cell, is synthesised de novo in Salmonella typhimurium.
In Saccharomyces cerevisiae, hydroxyethylthiazole kinase expression is regulated at the mRNA level by intracellular thiamin pyrophosphate.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
Further reading
EC 2.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Hydroxylysine%20kinase | In enzymology, a hydroxylysine kinase () is an enzyme that catalyzes the chemical reaction
GTP + 5-hydroxy-L-lysine GDP + 5-phosphonooxy-L-lysine
Thus, the two substrates of this enzyme are GTP and 5-hydroxy-L-lysine, whereas its two products are GDP and 5-phosphonooxy-L-lysine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is GTP:5-hydroxy-L-lysine O-phosphotransferase. Other names in common use include hydroxylysine kinase (phosphorylating), and guanosine triphosphate:5-hydroxy-L-lysine O-phosphotransferase. This enzyme participates in lysine degradation.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroxymethylpyrimidine%20kinase | In enzymology, a hydroxymethylpyrimidine kinase () is an enzyme that catalyzes the chemical reaction
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine
Thus, the two substrates of this enzyme are ATP and 4-amino-5-hydroxymethyl-2-methylpyrimidine, whereas its two products are ADP and 4-amino-5-phosphonooxymethyl-2-methylpyrimidine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:4-amino-5-hydroxymethyl-2-methylpyrimidine 5-phosphotransferase. This enzyme is also called hydroxymethylpyrimidine kinase (phosphorylating). This enzyme participates in thiamine metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hygromycin-B%20kinase | In enzymology, a hygromycin-B kinase () is an enzyme that catalyzes the chemical reaction
ATP + hygromycin B ADP + 7"-O-phosphohygromycin
Thus, the two substrates of this enzyme are ATP and hygromycin B, whereas its two products are ADP and 7''-O-phosphohygromycin.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:hygromycin-B 7"-O-phosphotransferase. This enzyme is also called hygromycin B phosphotransferase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hypotaurocyamine%20kinase | In enzymology, a hypotaurocyamine kinase () is an enzyme that catalyzes the chemical reaction
ATP + hypotaurocyamine ADP + Nomega-phosphohypotaurocyamine
Thus, the two substrates of this enzyme are ATP and hypotaurocyamine, whereas its two products are ADP and Nomega-phosphohypotaurocyamine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:hypotaurocyamine N-phosphotransferase.
References
EC 2.7.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Inosine%20kinase | In enzymology, an inosine kinase () is an enzyme that catalyzes the chemical reaction
ATP + inosine ADP + IMP
Thus, the two substrates of this enzyme are ATP and inosine, whereas its two products are ADP and IMP.
Inosine kinase belongs to the phosphofructokinase B (PfkB) family of sugar kinases. Other members of this family (also known as the Ribokinase family) include ribokinase (RK) adenosine kinase (AK), fructokinase, and 1-phosphofructokinase. The members of the PfkB/RK family are identified by the presence of three conserved sequence motifs. The structures of several PfK family of proteins have been determined from a number of organisms and the enzymatic activity of this family of this family of protein shows a dependence on the presence of pentavalent ions. Despite low sequence similarity between inosine kinase and other PfkB family of proteins, these proteins are quite similar at structural levels. Other names in common use include inosine-guanosine kinase, and inosine kinase (phosphorylating). This enzyme participates in purine metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Inositol%203-kinase | In enzymology, an inositol 3-kinase () is an enzyme that catalyzes the chemical reaction
ATP + myo-inositol ADP + 1D-myo-inositol 3-phosphate
Thus, the two substrates of this enzyme are ATP and myo-inositol, whereas its two products are ADP and 1D-myo-inositol 3-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:myo-inositol 1-phosphotransferase. Other names in common use include inositol-1-kinase (phosphorylating), myoinositol kinase, and myo-inositol 1-kinase. This enzyme participates in inositol phosphate metabolism.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Inositol-pentakisphosphate%202-kinase | In enzymology, an inositol-pentakisphosphate 2-kinase () is an enzyme that catalyzes the chemical reaction
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate ADP + 1D-myo-inositol hexakisphosphate
Thus, the two substrates of this enzyme are ATP and 1D-myo-inositol 1,3,4,5,6-pentakisphosphate, whereas its two products are ADP and 1D-myo-inositol hexakisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1D-myo-inositol 1,3,4,5,6-pentakisphosphate 2-phosphotransferase. Other names in common use include IP5 2-kinase, Gsl1p, Ipk1p, inositol polyphosphate kinase, inositol 1,3,4,5,6-pentakisphosphate 2-kinase, and Ins(1,3,4,5,6)P5 2-kinase.
References
EC 2.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Inositol-tetrakisphosphate%201-kinase | In enzymology, an inositol-tetrakisphosphate 1-kinase () is an enzyme that catalyzes the chemical reaction
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
Thus, the two substrates of this enzyme are ATP and 1D-myo-inositol 3,4,5,6-tetrakisphosphate, whereas its two products are ADP and 1D-myo-inositol 1,3,4,5,6-pentakisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1D-myo-inositol-3,4,5,6-tetrakisphosphate 1-phosphotransferase. Other names in common use include 1D-myo-inositol-tetrakisphosphate 1-kinase, inositol-trisphosphate 6-kinase, 1D-myo-inositol-trisphosphate 6-kinase, ATP:1D-myo-inositol-1,3,4-trisphosphate 6-phosphotransferase, inositol-trisphosphate 5-kinase, 1D-myo-inositol-trisphosphate 5-kinase, and ATP:1D-myo-inositol-1,3,4-trisphosphate 5-phosphotransferase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 2.7.1
Enzymes of known structure |
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