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https://en.wikipedia.org/wiki/Inositol-3-phosphate%20synthase | In enzymology, an inositol-3-phosphate synthase () is an enzyme that catalyzes the chemical reaction
D-glucose 6-phosphate 1D-myo-inositol 3-phosphate
Hence, this enzyme has one substrate, D-glucose 6-phosphate, and one product, 1D-myo-inositol 3-phosphate.
This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is 1D-myo-inositol-3-phosphate lyase (isomerizing). Other names in common use include myo-inositol-1-phosphate synthase, D-glucose 6-phosphate cycloaldolase, inositol 1-phosphate synthatase, glucose 6-phosphate cyclase, inositol 1-phosphate synthetase, glucose-6-phosphate inositol monophosphate cycloaldolase, glucocycloaldolase, and 1L-myo-inositol-1-phosphate lyase (isomerizing).
This enzyme participates in streptomycin biosynthesis and inositol phosphate metabolism. It employs one cofactor, NAD+. The reaction this enzyme catalyses represents the first committed step in the production of all inositol-containing compounds, including phospholipids, either directly or by salvage. The enzyme exists in a cytoplasmic form in a wide range of plants, animals, and fungi. It has also been detected in several bacteria and a chloroplast form is observed in alga and higher plants. Inositol phosphates play an important role in signal transduction.
In Saccharomyces cerevisiae (Baker's yeast), the transcriptional regulation of the INO1 gene encoding inositol-3-phosphate synthase has been stud |
https://en.wikipedia.org/wiki/Isobutyryl-CoA%20mutase | In enzymology, an isobutyryl-CoA mutase () is an enzyme that catalyzes the chemical reaction
2-methylpropanoyl-CoA butanoyl-CoA
Hence, this enzyme has one substrate, 2-methylpropanoyl-CoA, and one product, butanoyl-CoA.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 2-methylpropanoyl-CoA CoA-carbonylmutase. Other names in common use include isobutyryl coenzyme A mutase, and butyryl-CoA:isobutyryl-CoA mutase. It uses adenosylcobalamin as a cofactor, which is bound at the enzyme's vitamin B12-binding domain. The mechanism of action of the enzyme is to generate a 5′-deoxyadenosyl radical by homolytic cleavage of the cobalt-carbon bond of the cofactor. This radical abstracts a hydrogen atom from the substrate to initiate the rearrangement reaction.
References
EC 5.4.99
Cobalt enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isochorismate%20synthase | Isochorismate synthase ( ) is an isomerase enzyme that catalyzes the first step in the biosynthesis of vitamin K2 (menaquinone) in Escherichia coli.
Reaction
Isochorismate synthase, belongs to the isomerase enzyme family. More specifically it is classified as an intramolecular transferase because it transfers the hydroxy group of chorismate between carbons.
Isochorismate synthase catalyzes the irreversible conversion of chorismate to isochorismate:
Isochorismate synthase is most active at 37 °C and at a pH between 7.5 and 8. It requires Mg2+ as a cofactor, in a concentration between 100 μM and 1 mM. Inhibitors of isochorismate synthase include:
(4R,5R)-4-hydroxy-5-(1-carboxyvinyloxy)-cyclohex-1-ene carboxylate
(4R,5R)-4-hydroxy-5-carboxymethoxy-cyclohex-1-enecarboxylate
(4R,5R)-5-(2-carboxy-allyloxy)-4-hydroxy-cyclohex-1-enecarboxylate
(4R,5R,6S)-6-ammonio-5-[(1-carboxylatoethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylate
(4R,5R,7R)-5-(1-carboxy-ethoxy)-4-hydroxy-cyclohex-1-enecarboxylate
(4R,5R,7S)-5-(1-carboxy-ethoxy)-4-hydroxy-cyclohex-1-enecarboxylate
(4R,5S,6S)-4-ammonio-5-[(1-carboxylatoethenyl)oxy]-6-hydroxycyclohex-1-ene-1-carboxylate
(4R,5S,6S)-5-[(1-carboxylatoethenyl)oxy]-4,6-dihydroxycyclohex-1-ene-1-carboxylate
Cu2+
Hg2+
K+
Mg2+ at concentrations above 1 mM
N-ethylmaleimide
Nomenclature
The systematic name of this enzyme is isochorismate hydroxymutase, and the common name is isochorismate synthase. Other names for this enzyme include:
Iso |
https://en.wikipedia.org/wiki/Isocitrate%20epimerase | In enzymology, an isocitrate epimerase is classified as follows: . This number indicates that it is an isomerase, specifically a racemase or epimerase that acts on hydroxy acids and their derivatives, namely isocitrate. Isocitrate epimerase specifically catalyzes the reversible reaction:
(1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate ↔ (1S,2S)-1-hydroxypropane-1,2,3-tricarboxylate
which can also be described as
D-threo-isocitrate ↔ D-erythro-isocitrate
History
Isocitrate epimerase was originally isolated from the fungal cell-free extract of Penicillium purpurogenum , where it was discovered due to the excess accumulation of L-alloisocitric acid (D-erythro-isocitrate)—a diastereomer of isocitrate previously not seen in nature. In order to accumulate L-alloisocitric acid as a fermentation product, P. purpurogenum needed to be grown on citrate supplemented nutrient agar. During this fermentation it was found that the fermentation yield of L-alloisocitric acid was capable of “exceeding 70% without producing any other stereoisomers of isocitiric acid or other metabolites”.
This enzyme has not been heavily studied since first being identified in 1982, as a result of this there is presently not a crystal structure or active site description for isocitrate epimerase. Other isocitrate enzymes, such as isocitrate lyase and isocitrate dehydrogenase have been studied more closely due to their key roles in glycolysis and the TCA cycle.
References
EC 5.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isomaltulose%20synthase | In enzymology, an isomaltulose synthase () is an enzyme that catalyzes the chemical reaction
sucrose 6-O-Alpha-D-Glucopyranosyl-D-Fructofuranose
Hence, this enzyme has one substrate, sucrose (table sugar), and one product, 6-O-Alpha-D-Glucopyranosyl-D-Fructofuranose (also known as isomaltulose or Palatinose). It converts the α-1,2 glycosidic linkage between glucose and fructose in sucrose into the α-1,6 glycosidic linkage between glucose and fructose in isomaltulose.
This enzyme belongs to the family of isomerases. The systematic name of this enzyme class is sucrose glucosylmutase. Other names in common use include sucrose isomerase, sucrose alpha-glucosyltransferase, and trehalulose synthase.
The isomaltulose synthase of the bacterium Protaminobacter rubrum is commonly used in the industrial production of isomaltulose.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 5.4.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/Isopenicillin%20N%20epimerase | In enzymology, an isopenicillin N epimerase () is an enzyme that catalyzes the chemical reaction
isopenicillin N penicillin N
Hence, this enzyme has one substrate, isopenicillin N, and one product, penicillin N.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is penicillin N 5-amino-5-carboxypentanoyl-epimerase. This enzyme participates in penicillin and cephalosporin biosynthesis.
References
EC 5.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Isopiperitenone%20Delta-isomerase | In enzymology, an isopiperitenone Delta-isomerase () is an enzyme that catalyzes the chemical reaction
isopiperitenone piperitenone
Hence, this enzyme has one substrate, isopiperitenone, and one product, piperitenone.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is isopiperitenone Delta8-Delta4-isomerase.
References
EC 5.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-arabinose%20isomerase | In enzymology, a L-arabinose isomerase () is an enzyme that catalyzes the chemical reaction
L-arabinose L-ribulose
Hence, this enzyme has one substrate, L-arabinose, and one product, L-ribulose.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-arabinose aldose-ketose-isomerase. This enzyme participates in pentose and glucuronate interconversions.
This enzyme catalyses the conversion of L-arabinose to L-ribulose as the first step in the pathway of L-arabinose utilization as a carbon source.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
Further reading
Protein families
EC 5.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/L-dopachrome%20isomerase | In enzymology, a L-dopachrome isomerase () is an enzyme that catalyzes the chemical reaction
L-dopachrome 5,6-dihydroxyindole-2-carboxylate
Hence, this enzyme has one substrate, L-dopachrome, and one product, 5,6-dihydroxyindole-2-carboxylate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is L-dopachrome keto-enol isomerase. Other names in common use include dopachrome tautomerase, tyrosinase-related protein 2, TRP-1, TRP2, TRP-2, tyrosinase-related protein-2, dopachrome Delta7,Delta2-isomerase, dopachrome Delta-isomerase, dopachrome conversion factor, dopachrome isomerase, dopachrome oxidoreductase, dopachrome-rearranging enzyme, DCF, DCT, dopachrome keto-enol isomerase, and L-dopachrome-methyl ester tautomerase. This enzyme participates in tyrosine metabolism and melanogenesis.
References
EC 5.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Leucine%202%2C3-aminomutase | In enzymology, a leucine 2,3-aminomutase () is an enzyme that catalyzes the chemical reaction
(2S)-alpha-leucine (3R)-beta-leucine
Hence, this enzyme is responsible for the conversion of -leucine to β-leucine.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is (2S)-alpha-leucine 2,3-aminomutase. This enzyme participates in valine, leucine and isoleucine degradation. It employs one cofactor, cobamide.
References
EC 5.4.3
Cobamide enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-fucose%20isomerase | In enzymology, a L-fucose isomerase () is an enzyme that catalyzes the chemical reaction
L-fucose L-fuculose
Hence, this enzyme has one substrate, L-fucose, and one product, L-fuculose.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-fucose aldose-ketose-isomerase. This enzyme participates in fructose and mannose metabolism.
The enzyme is a hexamer, forming the largest structurally known ketol isomerase, and has no sequence or structural similarity with other ketol isomerases. The structure was determined by X-ray crystallography at 2.5 Angstrom resolution. Each subunit of the hexameric enzyme is wedge-shaped and composed of three domains. Both domains 1 and 2 contain central parallel beta- sheets with surrounding alpha helices. The active centre is shared between pairs of subunits related along the molecular three-fold axis, with domains 2 and 3 from one subunit providing most of the substrate-contacting residues.
References
Further reading
Protein domains
EC 5.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Linoleate%20isomerase | In enzymology, a linoleate isomerase () is an enzyme that catalyzes the chemical reaction
9-cis,12-cis-octadecadienoate 9-cis,11-trans-octadecadienoate
Hence, this enzyme has one substrate, 9-cis,12-cis-octadecadienoate, and one product, 9-cis,11-trans-octadecadienoate.
This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is linoleate Delta12-cis-Delta11-trans-isomerase. This enzyme is also called linoleic acid isomerase. This enzyme participates in linoleic acid metabolism.
References
EC 5.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-rhamnose%20isomerase | In enzymology, a L-rhamnose isomerase () is an enzyme that catalyzes the chemical reaction
L-rhamnose L-rhamnulose
Hence, this enzyme has one substrate, L-rhamnose, and one product, L-rhamnulose.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-rhamnose aldose-ketose-isomerase. Other names in common use include rhamnose isomerase, and L-rhamnose ketol-isomerase. This enzyme participates in fructose and mannose metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 5.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/L-ribulose-5-phosphate%203-epimerase | In enzymology, a L-ribulose-5-phosphate 3-epimerase () is an enzyme that catalyzes the chemical reaction
L-ribulose 5-phosphate L-xylulose 5-phosphate
Hence, this enzyme has one substrate, L-ribulose 5-phosphate, and one product, L-xylulose 5-phosphate.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is L-ribulose-5-phosphate 3-epimerase. Other names in common use include L-xylulose 5-phosphate 3-epimerase, UlaE, and SgaU. This enzyme participates in ascorbate and aldarate metabolism.
References
EC 5.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-ribulose-5-phosphate%204-epimerase | In enzymology, a L-ribulose-5-phosphate 4-epimerase () is an enzyme that catalyzes the interconversion of ribulose 5-phosphate and xylulose 5-phosphate in the oxidative phase of the Pentose phosphate pathway.
L-ribulose 5-phosphate D-xylulose 5-phosphate
This enzyme has a molecular mass of 102 kDa and is believed to be composed of four identical 25.5 kDa subunits. It belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is L-ribulose-5-phosphate 4-epimerase. Other names in common use include phosphoribulose isomerase, ribulose phosphate 4-epimerase, L-ribulose-phosphate 4-epimerase, L-ribulose 5-phosphate 4-epimerase, AraD, and L-Ru5P. This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.
Enzyme Mechanism
L-Ribulose 5-phosphate 4-epimerase catalyzes the epimerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate by retro-aldol cleavage and subsequent aldol reaction. The proposed mechanism involves the abstraction of the proton from the hydroxyl group on C-4, followed by cleavage of the bond between C-3 and C-4 to give a metal-stabilized acetone enediolate and a glycolaldehyde phosphate fragment. The C–C bond of glycolaldehyde phosphate is then rotated 180°, and the C–C bond between C-3 and C-4 is regenerated to give inversion of stereochemistry at C-4.
This mechanism is contested by a possible alternat |
https://en.wikipedia.org/wiki/Lysine%20racemase | In enzymology, a lysine racemase () is an enzyme that catalyzes the chemical reaction
L-lysine ⇌ D-lysine
Hence, this enzyme has one substrate, L-lysine, and one product, D-lysine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is lysine racemase. This enzyme participates in lysine degradation.
References
EC 5.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lysolecithin%20acylmutase | In enzymology, a lysolecithin acylmutase () is an enzyme that catalyzes the chemical reaction
2-lysolecithin 3-lysolecithin
Hence, this enzyme has one substrate, 2-lysolecithin, and one product, 3-lysolecithin.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring acyl groups. The systematic name of this enzyme class is lysolecithin 2,3-acylmutase. This enzyme is also called lysolecithin migratase.
References
EC 5.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Maleylacetoacetate%20isomerase | In enzymology, maleylacetoacetate isomerase () is an enzyme that catalyzes the chemical reaction
4-maleylacetoacetate 4-fumarylacetoacetate
This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is 4-maleylacetoacetate cis-trans-isomerase.
4-Maleylacetoacetate isomerase is an enzyme involved in the degradation of L-phenylalanine. It is encoded by the gene glutathione S-transferase zeta 1, or GSTZ1. This enzyme catalyzes the conversion of 4-maleylacetoacetate to 4-fumarylacetoacetate. 4-Maleylacetoacetate isomerase belongs to the zeta class of the glutathione S-transferase (GST) superfamily.
Mechanism
In the phenylalanine degradation pathway, 4-maleylacetoacetate isomerase catalyzes a cis-trans isomerization of 4-maleylacetoacetate to fumarylacetoacetate. 4-maleylacetoacetate isomerase requires the cofactor glutathione to function. Ser 15, Cys 16, Gln 111, and the helix dipole of alpha 1 of the enzyme stabilize the thiolate form of glutathione which activates it to attack the alpha carbon of 4-maleylacetoacetate, thus breaking the double bond and allowing rotation around the single bond.
4-maleylacetoacetate is converted to 4-fumarylacetoacetate, this compound can be broken down into fumarate and acetoacetate by the enzyme fumarylacetoacetate hydrolase.
The conversion of 4-maleylacetoacetate to fumarylacetoacetate is a step in the catabolism of phenylalanine and tyrosine, amino acids acquired thro |
https://en.wikipedia.org/wiki/Maleylpyruvate%20isomerase | In enzymology, a maleylpyruvate isomerase () is an enzyme that catalyzes the chemical reaction
3-maleylpyruvate 3-fumarylpyruvate
Hence, this enzyme has one substrate, 3-maleylpyruvate, and one product, 3-fumarylpyruvate.
This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is 3-maleylpyruvate cis-trans-isomerase. This enzyme participates in tyrosine metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 5.2.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Maltose%20alpha-D-glucosyltransferase | In enzymology, a maltose α-D-glucosyltransferase () is an enzyme that catalyzes the chemical reaction
maltose alpha,alpha-trehalose
Hence, this enzyme has one substrate, maltose, and one product, alpha,alpha-trehalose.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is maltose alpha-D-glucosylmutase. Other names in common use include trehalose synthase, and maltose glucosylmutase. This enzyme participates in starch and sucrose metabolism.
References
EC 5.4.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Maltose%20epimerase | In enzymology, a maltose epimerase () is an enzyme that catalyzes the chemical reaction
alpha-maltose beta-maltose
Hence, this enzyme has one substrate, alpha-maltose, and one product, beta-maltose.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is maltose 1-epimerase.
References
EC 5.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mannose%20isomerase | In enzymology, a mannose isomerase () is an enzyme that catalyzes the chemical reaction
D-mannose D-fructose
Hence, this enzyme has one substrate, D-mannose, and one product, D-fructose.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is D-mannose aldose-ketose-isomerase. Other names in common use include D-mannose isomerase, and D-mannose ketol-isomerase. This enzyme participates in fructose and mannose metabolism.
References
EC 5.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methionine%20racemase | In enzymology, a methionine racemase () is an enzyme that catalyzes the chemical reaction
L-methionine D-methionine
Hence, this enzyme has one substrate, L-methionine, and one product, D-methionine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is methionine racemase. It employs one cofactor, pyridoxal phosphate.
References
EC 5.1.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methylaspartate%20mutase | In enzymology, a methylaspartate mutase () is an enzyme that catalyzes the chemical reaction
L-threo-3-methylaspartate L-glutamate
Hence, this enzyme has one substrate, L-threo-3-methylaspartate, and one product, L-glutamate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is L-threo-3-methylaspartate carboxy-aminomethylmutase. Other names in common use include glutamate mutase, glutamic mutase, glutamic isomerase, glutamic acid mutase, glutamic acid isomerase, methylaspartic acid mutase, beta-methylaspartate-glutamate mutase, and glutamate isomerase. This enzyme participates in c5-branched dibasic acid metabolism. It employs one cofactor, cobamide.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
References
EC 5.4.99
Cobamide enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Methylitaconate%20Delta-isomerase | In enzymology, a methylitaconate Δ-isomerase () is an enzyme that catalyzes the chemical reaction
methylitaconate 2,3-dimethylmaleate
Hence, this enzyme has one substrate, methylitaconate, and one product, 2,3-dimethylmaleate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is methylitaconate Delta2-Delta3-isomerase. This enzyme is also called methylitaconate isomerase. This enzyme participates in c5-branched dibasic acid metabolism.
References
EC 5.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Muconolactone%20%CE%94-isomerase | In enzymology, a muconolactone Δ-isomerase () is an enzyme that catalyzes the chemical reaction
(S)-5-oxo-2,5-dihydrofuran-2-acetate 5-oxo-4,5-dihydrofuran-2-acetate
Hence, this enzyme has one substrate, (S)-5-oxo-2,5-dihydrofuran-2-acetate, and one product, 5-oxo-4,5-dihydrofuran-2-acetate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is 5-oxo-4,5-dihydrofuran-2-acetate Delta3-Delta2-isomerase. This enzyme is also called muconolactone isomerase. This enzyme participates in benzoate degradation via hydroxylation.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 5.3.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acylglucosamine%202-epimerase | In enzymology, a N-acylglucosamine 2-epimerase () is an enzyme that catalyzes the chemical reaction
N-acyl-D-glucosamine N-acyl-D-mannosamine
Hence, this enzyme has one substrate, N-acyl-D-glucosamine, and one product, N-acyl-D-mannosamine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is N-acyl-D-glucosamine 2-epimerase. Other names in common use include acylglucosamine 2-epimerase, and N-acetylglucosamine 2-epimerase. This enzyme participates in aminosugars metabolism. It employs one cofactor, ATP.
Structural studies
As of late 2019, three structures have been solved for this class of enzymes, with the PDB accession codes , , and . They show that the N-acylglucosamine 2-epimerase monomer folds as a barrel composed of α-helices, in a manner known as (α/α)6-barrel. The structures are presented as dimers, with the structures from Sus scrofa and Anabaena sp. CH1 having a different organization than the structure from Nostoc sp. KJV10.
References
EC 5.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acylglucosamine-6-phosphate%202-epimerase | In enzymology, a N-acylglucosamine-6-phosphate 2-epimerase () is an enzyme that catalyzes the chemical reaction
N-acyl-D-glucosamine 6-phosphate N-acyl-D-mannosamine 6-phosphate
Hence, this enzyme has one substrate, N-acyl-D-glucosamine 6-phosphate, and one product, N-acyl-D-mannosamine 6-phosphate.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is N-acyl-D-glucosamine-6-phosphate 2-epimerase. Other names in common use include acylglucosamine-6-phosphate 2-epimerase, and acylglucosamine phosphate 2-epimerase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 5.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Neoxanthin%20synthase | In enzymology, a neoxanthin synthase () is an enzyme that catalyzes the chemical reaction:
violaxanthin neoxanthin
Hence, this enzyme has one substrate, violaxanthin, and one product, neoxanthin.
This enzyme belongs to the family of isomerases, specifically a class of other intramolecular oxidoreductases. The systematic name of this enzyme class is violaxanthin---neoxanthin isomerase (epoxide-opening). This enzyme is also called NSY. This enzyme participates in carotenoid biosynthesis - general.
References
EC 5.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nocardicin-A%20epimerase | In enzymology, a nocardicin-A epimerase () is an enzyme that catalyzes the chemical reaction
isonocardicin A nocardicin A
Hence, this enzyme has one substrate, isonocardicin A, and one product, nocardicin A.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is nocardicin-A epimerase. This enzyme is also called isonocardicin A epimerase.
References
EC 5.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ornithine%20racemase | In enzymology, an ornithine racemase () is an enzyme that catalyzes the chemical reaction:
L-ornithine D-ornithine
Hence, this enzyme has one substrate, L-ornithine, and one product, D-ornithine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is ornithine racemase. This enzyme participates in d-arginine and d-ornithine metabolism.
References
EC 5.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Oxaloacetate%20tautomerase | In enzymology, an oxaloacetate tautomerase () is an enzyme that catalyzes the chemical reaction
keto-oxaloacetate enol-oxaloacetate
Hence, this enzyme has one substrate, keto-oxaloacetate, and one product, enol-oxaloacetate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting keto- and enol-groups. The systematic name of this enzyme class is oxaloacetate keto---enol-isomerase. This enzyme is also called oxaloacetic keto-enol isomerase.
While oxaloacetate tautomerase was characterized in several papers in the 1960s and 1970s, this activity has not been correlated with any gene identified in the genome of higher organisms.
References
EC 5.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phenylpyruvate%20tautomerase | In enzymology, phenylpyruvate tautomerase or Macrophage migration inhibitory factor () is an enzyme that catalyzes the chemical reaction
keto-phenylpyruvate enol-phenylpyruvate
Phenylpyruvate tautomerase has also been found to exhibit the same keto-enol tautomerism for 4-Hydroxyphenylpyruvic acid, which is structurally similar to phenylpyruvate but contains an additional hydroxyl moiety in the para position of the aromatic ring.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting keto- and enol-groups. The systematic name of this enzyme class is phenylpyruvate keto---enol-isomerase. This enzyme is also called phenylpyruvic keto-enol isomerase. This enzyme participates in tyrosine metabolism and phenylalanine metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 5.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phosphoacetylglucosamine%20mutase | In enzymology, a phosphoacetylglucosamine mutase () is an enzyme that catalyzes the chemical reaction
N-acetyl-alpha-D-glucosamine 1-phosphate N-acetyl-D-glucosamine 6-phosphate
Hence, this enzyme has one substrate, N-acetyl-alpha-D-glucosamine 1-phosphate, and one product, N-acetyl-D-glucosamine 6-phosphate.
This enzyme belongs to the family of isomerases, specifically the phosphotransferases (phosphomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is N-acetyl-alpha-D-glucosamine 1,6-phosphomutase. Other names in common use include acetylglucosamine phosphomutase, acetylglucosamine phosphomutase, acetylaminodeoxyglucose phosphomutase, phospho-N-acetylglucosamine mutase, and N-acetyl-D-glucosamine 1,6-phosphomutase. This enzyme participates in aminosugars metabolism. This enzyme has at least one effector, N-Acetyl-D-glucosamine 1,6-bisphosphate.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p. 407-477.
EC 5.4.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phosphoenolpyruvate%20mutase | In enzymology, a phosphoenolpyruvate mutase () is an enzyme that catalyzes the chemical reaction
phosphoenolpyruvate 3-phosphonopyruvate
Hence, this enzyme has one substrate, phosphoenolpyruvate (PEP), and one product, 3-phosphonopyruvate (PPR), which are structural isomers.
This enzyme belongs to the family of isomerases, specifically the phosphotransferases (phosphomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is phosphoenolpyruvate 2,3-phosphonomutase. Other names in common use include phosphoenolpyruvate-phosphonopyruvate phosphomutase, PEP phosphomutase, phosphoenolpyruvate phosphomutase, PEPPM, and PEP phosphomutase. This enzyme participates in aminophosphonate metabolism.
Phosphoenolpyruvate mutase was discovered in 1988.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, all by the Herzberg group at the University of Maryland using PEPPM from the blue mussel, Mytilus edulis. The first structure (PDB accession code ) was solved in 1999 and featured a magnesium oxalate inhibitor. This structure identified the enzyme as consisting of identical beta barrel subunits (exhibiting the TIM barrel fold, which consists of eight parallel beta strands). Dimerization was observed in which a helix from each subunit interacts with the other subunit's barrel; the authors called this feature "helix swapping." The dimers can dimerize as well to form a homotetrameric enzyme. A |
https://en.wikipedia.org/wiki/Phosphoglucomutase%20%28glucose-cofactor%29 | In enzymology, a phosphoglucomutase (glucose-cofactor) () is an enzyme that catalyzes the chemical reaction
alpha-D-glucose 1-phosphate D-glucose 6-phosphate
Hence, this enzyme has one substrate, alpha-D-glucose 1-phosphate, and one product, D-glucose 6-phosphate.
This enzyme belongs to the family of isomerases, specifically the phosphotransferases (phosphomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is alpha-D-glucose 1,6-phosphomutase (glucose-cofactor). Other names in common use include glucose phosphomutase, and glucose-1-phosphate phosphotransferase. This enzyme has at least one effector, D-Glucose.
References
Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p. 407-477.
EC 5.4.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoglucosamine%20mutase | In enzymology, a phosphoglucosamine mutase () is an enzyme that catalyzes the chemical reaction
alpha-D-glucosamine 1-phosphate D-glucosamine 6-phosphate
Hence, this enzyme has one substrate, alpha-D-glucosamine 1-phosphate, and one product, D-glucosamine 6-phosphate.
This enzyme belongs to the family of isomerases, specifically the phosphotransferases (α-D-phosphohexomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is alpha-D-glucosamine 1,6-phosphomutase. This enzyme participates in aminosugars metabolism.
Crystal structures of two bacterial phosphoglucosamine mutases are known (PDB entries 3I3W and 3PDK), from Francisella tularensis and Bacillus anthracis. Both share a similar dimeric quaternary structure, as well as conserved features of the active site, as found their enzyme superfamily, the α-D-phosphohexomutases.
References
EC 5.4.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphomannomutase | In enzymology, a phosphomannomutase () is an enzyme that catalyzes the chemical reaction
alpha-D-mannose 1-phosphate D-mannose 6-phosphate
Hence, this enzyme has one substrate, alpha-D-mannose 1-phosphate, and one product, D-mannose 6-phosphate.
This enzyme belongs to the family of isomerases, specifically the phosphotransferases (phosphomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is alpha-D-mannose 1,6-phosphomutase. Other names in common use include mannose phosphomutase, phosphomannose mutase, and D-mannose 1,6-phosphomutase. This enzyme participates in fructose and mannose metabolism. It has 2 cofactors: D-glucose 1,6-bisphosphate, and D-Mannose 1,6-bisphosphate.
Structural studies
As of late 2007, 18 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , and .
References
EC 5.4.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phosphopentomutase | In enzymology, a phosphopentomutase () is an enzyme that catalyzes the chemical reaction
alpha-D-ribose 1-phosphate D-ribose 5-phosphate
Hence, this enzyme has one substrate, alpha-D-ribose 1-phosphate, and one product, D-ribose 5-phosphate.
This enzyme belongs to the family of isomerases, specifically the phosphotransferases (phosphomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is alpha-D-ribose 1,5-phosphomutase. Other names in common use include phosphodeoxyribomutase, deoxyribose phosphomutase, deoxyribomutase, phosphoribomutase, alpha-D-glucose-1,6-bisphosphate:deoxy-D-ribose-1-phosphate, phosphotransferase, and D-ribose 1,5-phosphomutase. This enzyme participates in pentose phosphate pathway and purine metabolism. It has 3 cofactors: D-ribose 1,5-bisphosphate, alpha-D-Glucose 1,6-bisphosphate, and 2-Deoxy-D-ribose 1,5-bisphosphate.
Structural studies
The first published description of a structure of a prokaryotic phosphopentomutase was in 2011. Structures of Bacillus cereus phosphopentomutase as it was purified, after activation, bound to ribose 5-phosphate and bound to glucose 1,6-bisphosphate are deposited in the PDB with accession codes , , and , respectively.
References
Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p. 407-477.
EC 5.4.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phosphoribosylanthranilate%20isomerase | In enzymology, a phosphoribosylanthranilate isomerase (PRAI) () is an enzyme that catalyzes the third step of the synthesis of the amino acid tryptophan.
This enzyme participates in the phenylalanine, tyrosine and tryptophan biosynthesis pathway, also known as the aromatic amino acid biosynthesis pathway
In yeast, it is encoded by the TRP1 gene.
Nomenclature
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is N-(5-phospho-beta-D-ribosyl)anthranilate aldose-ketose-isomerase. Other names in common use include:
PRA isomerase,
PRAI,
IGPS:PRAI (indole-3-glycerol-phosphate,
synthetase/N-5'-phosphoribosylanthranilate isomerase complex), and
N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase.
xPRAI (monomeric variant in Saccharmyces cerevisiae)
PRAI[ML256-452] (engineered variant of 1-(2-carboxy-phenylamino)-1-deoxy-D-ribulose 5-phosphate carboxylase: PRAI)
Reaction
Phosphoribosylanthranilate isomerase is one of the many enzymes within the biosynthesis pathway of tryptophan (an essential amino acid). The upstream* pathway substrates and intermediates are shown below (Fig. 2).
As seen in Fig. 3, N-(5'-phosphoribosyl)-anthranilate via this enzyme is converted into 1-(o-carboxyphenylamino)-1-deoxribulose 5-phosphate. As the name phosphoribosylanthranilate isomerase suggests, it functions as an isomerase, rearranging the parts of the molecule |
https://en.wikipedia.org/wiki/Polyenoic%20fatty%20acid%20isomerase | In enzymology, a polyenoic fatty acid isomerase () is an enzyme that catalyzes the chemical reaction
(5Z,8Z,11Z,14Z,17Z)-icosapentaenoate (5Z,7E,9E,14Z,17Z)-icosapentaenoate
Hence, this enzyme has one substrate, (5Z,8Z,11Z,14Z,17Z)-icosapentaenoate, and one product, (5Z,7E,9E,14Z,17Z)-icosapentaenoate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is (5Z,8Z,11Z,14Z,17Z)-icosapentaenoate Delta8,11-Delta7,9-isomerase (trans-double-bond-forming). Other names in common use include PFI, eicosapentaenoate cis-Delta5,8,11,14,17-eicosapentaenoate, cis-Delta5-trans-Delta7,9-cis-Delta14,17 isomerase, (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Delta8,11-Delta7,8-isomerase, (incorrect), (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Delta8,11-Delta7,9-isomerase, and (trans-double-bond-forming).
References
EC 5.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Precorrin-8X%20methylmutase | In enzymology, a precorrin-8X methylmutase () is an enzyme that catalyzes the chemical reaction
precorrin-8X hydrogenobyrinate
Hence, this enzyme has one substrate, precorrin 8X, and one product, hydrogenobyrinate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is precorrin-8X 11,12-methylmutase. Other names in common use include precorrin isomerase, hydrogenobyrinic acid-binding protein and CobH. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also
Cobalamin biosynthesis
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 5.4.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/Proline%20racemase | In enzymology, a proline racemase () is an enzyme that catalyzes the chemical reaction
L-proline D-proline
Hence, this enzyme has two substrates, L- and D-proline, and two products, D- and L- proline.
This enzyme belongs to the family of proline racemases acting on free amino acids. The systematic name of this enzyme class is proline racemase. This enzyme participates in arginine and proline metabolism. These enzymes catalyse the interconversion of L- and D-proline in bacteria.
Species distribution
This first eukaryotic proline racemase was identified in Trypanosoma cruzi and fully characterized . The parasite enzyme, TcPRAC, is as a co-factor-independent proline racemase and displays B-cell mitogenic properties when released by T. cruzi upon infection, contributing to parasite escape.
Novel proline racemases of medical and veterinary importance were described respectively in Clostridium difficile () and Trypanosoma vivax (). These studies showed that a peptide motif used as a minimal pattern signature to identify putative proline racemases (motif III*) is insufficient stringent per se to discriminate proline racemases from 4-hydroxyproline epimerases (HyPRE). Also, additional, non-dissociated elements that account for the discrimination of these enzymes were identified, based for instance on polarity constraints imposed by specific residues of the catalytic pockets. Based on those elements, enzymes incorrectly described as proline racemases were biochemically proved |
https://en.wikipedia.org/wiki/Prostaglandin-A1%20Delta-isomerase | In enzymology, a Prostaglandin-A1 Δ-isomerase () is an enzyme that catalyzes the chemical reaction
(13E)-(15S)-15-hydroxy-9-oxoprosta-10,13-dienoate (13E)-(15S)-15-hydroxy-9-oxoprosta-11,13-dienoate
Hence, this enzyme has one substrate, (13E)-(15S)-15-hydroxy-9-oxoprosta-10,13-dienoate (Prostaglandin A1 or PGA1), and one product, (13E)-(15S)-15-hydroxy-9-oxoprosta-11,13-dienoate (Prostaglandin C1).
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is (13E)-(15S)-15-hydroxy-9-oxoprosta-10,13-dienoate Delta10-Delta11-isomerase. This enzyme is also called prostaglandin A isomerase.
References
EC 5.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Prostaglandin-D%20synthase | In enzymology, a prostaglandin-D synthase () is an enzyme that catalyzes the chemical reaction
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
Thus, the substrate of this enzyme is (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate, whereas its product is (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate.
This enzyme belongs to the family of isomerases, specifically a class of other intramolecular oxidoreductases. The systematic name of this enzyme class is (5,13)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate Delta-isomerase. Other names in common use include prostaglandin-H2 Delta-isomerase, prostaglandin-R-prostaglandin D isomerase, and PGH-PGD isomerase. This enzyme participates in arachidonic acid metabolism.
In March 2012 American scientists reported a discovery that shows this enzyme triggers male baldness According to the discovery, levels of this enzyme are elevated in the cells of hair follicles located in bald patches on the scalp, but not in hairy areas. The research could lead to a cream to treat baldness.
Structural studies
As of late 2001, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
See also
Prostaglandin D2 synthase
Hematopoietic prostaglandin D synthase
References
EC 5.3.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/Protein-serine%20epimerase | In enzymology, a protein-serine epimerase () is an enzyme that catalyzes the chemical reaction
[protein]-L-serine [protein]-D-serine
Hence, this enzyme has one substrate, [protein]-L-serine, and one product, [protein]-D-serine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is [protein]-serine epimerase. This enzyme is also called protein-serine racemase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 5.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Retinal%20isomerase | Retinal isomerase () is an enzyme that catalyzes the isomerisation of all-trans-retinal in the eye into 11-cis-retinal which is the form that most opsins bind.
all-trans-retinal 11-cis-retinal
Hence, this enzyme has one substrate, all-trans-retinal, and one product, 11-cis-retinal.
This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. Its systematic name is all-trans-retinal 11-cis-trans-isomerase. Other names are retinene isomerase, and retinoid isomerase. This enzyme participates in the retinol metabolism.
References
EC 5.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Retinol%20isomerase | In enzymology, a retinol isomerase () is an enzyme that catalyzes the chemical reaction
all-trans-retinol 11-cis-retinol
Hence, this enzyme has one substrate, all-trans-retinol, and one product, 11-cis-retinol. These enzymes are alternatively referred to as retinoid isomerases.
This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is all-trans-retinol 11-cis-trans-isomerase. This enzyme is also called all-trans-retinol isomerase. This enzyme participates in retinol metabolism.
In vertebrates, RPE65 is the active retinol isomerase in the visual cycle. A lack of RPE65 function results in congenital blindness in children (specifically Leber congenital amaurosis). Emixustat, a partial inhibitor of RPE65, is currently in FDA clinical trials for the treatment of age-related macular degeneration.
References
EC 5.2.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ribose-5-phosphate%20isomerase | Ribose-5-phosphate isomerase (Rpi) encoded by the RPIA gene is an enzyme () that catalyzes the conversion between ribose-5-phosphate (R5P) and ribulose-5-phosphate (Ru5P). It is a member of a larger class of isomerases which catalyze the interconversion of chemical isomers (in this case structural isomers of pentose). It plays a vital role in biochemical metabolism in both the pentose phosphate pathway and the Calvin cycle. The systematic name of this enzyme class is D-ribose-5-phosphate aldose-ketose-isomerase.
Structure
Gene
RpiA in human beings is encoded on the second chromosome on the short arm (p arm) at position 11.2. Its encoding sequence is nearly 60,000 base pairs long. The only known naturally occurring genetic mutation results in ribose-5-phosphate isomerase deficiency, discussed below. The enzyme is thought to have been present for most of evolutionary history. Knock-out experiments conducted on the genes of various species meant to encode RpiA have indicated similar conserved residues and structural motifs, indicating ancient origins of the gene.
Protein
Rpi exists as two distinct proteins, termed RpiA and RpiB. Although RpiA and RpiB catalyze the same reaction, they show no sequence or overall structural homology. According to Jung et al., an assessment of RpiA using SDS-PAGE shows that the enzyme is a homodimer of 25 kDa subunits. The molecular mass of the RpiA dimer was found to be 49 kDa by gel filtration. Recently, the crystal structure of RpiA was de |
https://en.wikipedia.org/wiki/Ribose%20isomerase | In enzymology, a ribose isomerase () is an enzyme that catalyzes the chemical reaction
D-ribose D-ribulose
Hence, this enzyme has one substrate, D-ribose, and one product, D-ribulose.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is D-ribose aldose-ketose-isomerase. Other names in common use include D-ribose isomerase, and D-ribose ketol-isomerase.
References
EC 5.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/S-methyl-5-thioribose-1-phosphate%20isomerase | In enzymology, a S-methyl-5-thioribose-1-phosphate isomerase () is an enzyme that catalyzes the chemical reaction
S-methyl-5-thio-alpha-D-ribose 1-phosphate S-methyl-5-thio-D-ribulose 1-phosphate
Hence, this enzyme has one substrate, S-methyl-5-thio-alpha-D-ribose 1-phosphate, and one product, S-methyl-5-thio-D-ribulose 1-phosphate.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is S-methyl-5-thio-alpha-D-ribose-1-phosphate aldose-ketose-isomerase. Other names in common use include methylthioribose 1-phosphate isomerase, 1-PMTR isomerase, 5-methylthio-5-deoxy-D-ribose-1-phosphate ketol-isomerase, S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate ketol-isomerase, S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate, aldose-ketose-isomerase, 1-phospho-5'-S-methylthioribose isomerase, and S-methyl-5-thio-D-ribose-1-phosphate aldose-ketose-isomerase. This enzyme participates in methionine metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 5.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Steroid%20Delta-isomerase | In enzymology, a steroid Δ5-isomerase () is an enzyme that catalyzes the chemical reaction
a 3-oxo-Δ5-steroid a 3-oxo-Δ4-steroid
Hence, this enzyme has one substrate, a 3-oxo-Δ5-steroid, and one product, a 3-oxo-Δ4-steroid.
Introduction
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is 3-oxosteroid Δ5-Δ4-isomerase. Other names in common use include ketosteroid isomerase (KSI), hydroxysteroid isomerase, steroid isomerase, Δ5-ketosteroid isomerase, Δ5(or Δ4)-3-keto steroid isomerase, Δ5-steroid isomerase, 3-oxosteroid isomerase, Δ5-3-keto steroid isomerase, and Δ5-3-oxosteroid isomerase.
KSI has been studied extensively from the bacteria Comamonas testosteroni (TI), formerly referred to as Pseudomonas testosteroni, and Pseudomonas putida (PI). The enzymes from these two sources are 34% homologous, and structural studies have shown that the placement of the catalytic groups in the active sites is virtually identical. Mammalian KSI has been studied from bovine adrenal cortex and rat liver. This enzyme participates in c21-steroid hormone metabolism and androgen and estrogen metabolism. An example substrate is Δ5-androstene-3,17-dione, which KSI converts to Δ4-androstene-3,17-dione. The above reaction in the absence of enzyme takes 7 weeks to complete in aqueous solution. KSI performs this reaction on an order of 1011 times faster, ranking it among the most pro |
https://en.wikipedia.org/wiki/Styrene-oxide%20isomerase | In enzymology, a styrene-oxide isomerase () is an enzyme that catalyzes the chemical reaction
styrene oxide phenylacetaldehyde
Hence, this enzyme has one substrate, styrene oxide, and one product, phenylacetaldehyde.
This enzyme belongs to the family of isomerases, specifically a class of other intramolecular oxidoreductases. The systematic name of this enzyme class is styrene-oxide isomerase (epoxide-cleaving). This enzyme is also called SOI. This enzyme participates in styrene degradation, and is the second step of the pathway after the epoxidation of styrene by styrene monooxygenase.
References
EC 5.3.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tartrate%20epimerase | In enzymology, a tartrate epimerase () is an enzyme that catalyzes the chemical reaction
(R,R)-tartrate meso-tartrate
Hence, this enzyme has one substrate, (R,R)-tartrate, and one product, meso-tartrate.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on hydroxy acids and derivatives. The systematic name of this enzyme class is tartrate epimerase. This enzyme is also called tartaric racemase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 5.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tetrahydroxypteridine%20cycloisomerase | In enzymology, a tetrahydroxypteridine cycloisomerase () is an enzyme that catalyzes the chemical reaction
tetrahydroxypteridine xanthine-8-carboxylate
Hence, this enzyme has one substrate, tetrahydroxypteridine, and one product, xanthine-8-carboxylate.
This enzyme belongs to the family of isomerases, specifically the class of intramolecular lyases. The systematic name of this enzyme class is tetrahydroxypteridine lyase (isomerizing). It employs one cofactor, NAD+.
References
EC 5.5.1
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiocyanate%20isomerase | In enzymology, a thiocyanate isomerase () is an enzyme that catalyzes the chemical reaction
benzyl isothiocyanate benzyl thiocyanate
Hence, this enzyme has one substrate, benzyl isothiocyanate, and one product, benzyl thiocyanate.
This enzyme belongs to the family of isomerases, specifically those other isomerases sole sub-subclass for isomerases that do not belong in the other subclasses. The systematic name of this enzyme class is benzyl-thiocyanate isomerase. This enzyme is also called isothiocyanate isomerase.
References
EC 5.99.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Threonine%20racemase | In enzymology, a threonine racemase () is an enzyme that catalyzes the chemical reaction
L-threonine D-threonine
Hence, this enzyme has one substrate, L-threonine, and one product, D-threonine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is threonine racemase.
References
EC 5.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trans-2-decenoyl-%28acyl-carrier%20protein%29%20isomerase | In enzymology, a trans-2-decenoyl-[acyl-carrier protein] isomerase () is an enzyme that catalyzes the chemical reaction
trans-dec-2-enoyl-[acyl-carrier-protein] cis-dec-3-enoyl-[acyl-carrier-protein]
Hence, this enzyme has one substrate, [[trans-dec-2-enoyl-[acyl-carrier-protein]]], and one product, [[cis-dec-3-enoyl-[acyl-carrier-protein]]].
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is decenoyl-[acyl-carrier-protein] Delta2-trans-Delta3-cis-isomerase. Other names in common use include beta-hydroxydecanoyl thioester dehydrase, trans-2-cis-3-decenoyl-ACP isomerase, trans-2,cis-3-decenoyl-ACP isomerase, trans-2-decenoyl-ACP isomerase, and FabM.
References
Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd ed., vol. 1, ASM Press, Washington, DC, 1996, p. 612-636.
EC 5.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/TRNA-pseudouridine%20synthase%20I | In enzymology, a tRNA-pseudouridine synthase I () is an enzyme that catalyzes the chemical reaction
tRNA uridine tRNA pseudouridine
Hence, this enzyme has one substrate, tRNA uridine, and one product, tRNA pseudouridine.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is tRNA-uridine uracilmutase. Other names in common use include tRNA-uridine isomerase, tRNA pseudouridylate synthase I, transfer ribonucleate pseudouridine synthetase, pseudouridine synthase, and transfer RNA pseudouridine synthetase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 5.4.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tyrosine%202%2C3-aminomutase | In enzymology, a tyrosine 2,3-aminomutase () is an enzyme that catalyzes the chemical reaction
L-tyrosine 3-amino-3-(4-hydroxyphenyl)propanoate
Hence, this enzyme has one substrate, L-tyrosine, and one product, 3-amino-3-(4-hydroxyphenyl)propanoate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is L-tyrosine 2,3-aminomutase. This enzyme is also called tyrosine alpha,beta-mutase. This enzyme participates in tyrosine metabolism. It employs one cofactor, 5-methylene-3,5-dihydroimidazol-4-one (MIO) which is formed autocatalytic rearrangement of the internal tripeptide Ala-Ser-Gly.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 5.4.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/UDP-arabinose%204-epimerase | In enzymology, an UDP-arabinose 4-epimerase () is an enzyme that catalyzes the chemical reaction
UDP-L-arabinose UDP-D-xylose
Hence, this enzyme has one substrate, UDP-L-arabinose, and one product, UDP-D-xylose.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is UDP-L-arabinose 4-epimerase. Other names in common use include uridine diphosphoarabinose epimerase, UDP arabinose epimerase, uridine 5'-diphosphate-D-xylose 4-epimerase, and UDP-D-xylose 4-epimerase. This enzyme participates in nucleotide sugars metabolism.
References
EC 5.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-galactopyranose%20mutase | In enzymology, an UDP-galactopyranose mutase () is an enzyme that catalyzes the chemical reaction
UDP-D-galactopyranose UDP-D-galacto-1,4-furanose
Hence, this enzyme has one substrate, UDP-D-galactopyranose, and one product, UDP-D-galacto-1,4-furanose.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is UDP-D-galactopyranose furanomutase.
UDP-D-galactofuranose then serves as an activated sugar donor for the biosynthesis of galactofuranose glycoconjugates. The exocyclic 1,2-diol of galactofuranose is the epitope recognized by the putative chordate immune lectin intelectin.
Structural studies
Because UGM is not present in the mammalian systems but is essential among several pathogenic microbes, the enzyme is an attractive antibiotic target. As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 5.4.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/UDP-glucosamine%204-epimerase | In enzymology, an UDP-glucosamine 4-epimerase () is an enzyme that catalyzes the chemical reaction
UDP-glucosamine UDP-galactosamine
Hence, this enzyme has one substrate, UDP-glucosamine, and one product, UDP-galactosamine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is UDP-glucosamine 4-epimerase.
References
EC 5.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-glucose%204-epimerase | The enzyme UDP-glucose 4-epimerase (), also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.
Additionally, human and some bacterial GALE isoforms reversibly catalyze the formation of UDP-N-acetylgalactosamine (UDP-GalNAc) from UDP-N-acetylglucosamine (UDP-GlcNAc) in the presence of NAD+, an initial step in glycoprotein or glycolipid synthesis.
Historical significance
Dr. Luis Leloir deduced the role of GALE in galactose metabolism during his tenure at the Instituto de Investigaciones Bioquímicas del Fundación Campomar, initially terming the enzyme waldenase. Dr. Leloir was awarded the 1970 Nobel Prize in Chemistry for his discovery of sugar nucleotides and their role in the biosynthesis of carbohydrates.
Structure
GALE belongs to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. This family is characterized by a conserved Tyr-X-X-X-Lys motif necessary for enzymatic activity; one or more Rossmann fold scaffolds; and the ability to bind NAD+.
Tertiary structure
GALE structure has been resolved for a number of species, including E. coli and humans. GALE exists as a homodimer in various species.
While subunit size vari |
https://en.wikipedia.org/wiki/UDP-glucuronate%204-epimerase | In enzymology, an UDP-glucuronate 4-epimerase () is an enzyme that catalyzes the chemical reaction
UDP-glucuronate UDP-D-galacturonate
Hence, this enzyme has one substrate, UDP-glucuronate, and one product, UDP-D-galacturonate.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is UDP-glucuronate 4-epimerase. Other names in common use include uridine diphospho-D-galacturonic acid, UDP glucuronic epimerase, uridine diphosphoglucuronic epimerase, UDP-galacturonate 4-epimerase, uridine diphosphoglucuronate epimerase, and UDP-D-galacturonic acid 4-epimerase. This enzyme participates in starch and sucrose metabolism and nucleotide sugars metabolism.
References
EC 5.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-glucuronate%205%27-epimerase | In enzymology, an UDP-glucuronate 5'-epimerase () is an enzyme that catalyzes the chemical reaction
UDP-glucuronate UDP-L-iduronate
Hence, this enzyme has one substrate, UDP-glucuronate, and one product, UDP-L-iduronate.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is UDP-glucuronate 5'-epimerase. Other names in common use include uridine diphosphoglucuronate 5'-epimerase, UDP-glucuronic acid 5'-epimerase, and C-5-uronosyl epimerase. This enzyme participates in nucleotide sugars metabolism. It employs one cofactor, NAD+.
References
EC 5.1.3
NADH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine%202-epimerase | In enzymology, an UDP-N-acetylglucosamine 2-epimerase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine UDP-N-acetyl-D-mannosamine
Hence, this enzyme has one substrate, UDP-N-acetyl-D-glucosamine, and one product, UDP-N-acetyl-D-mannosamine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine 2-epimerase. Other names in common use include UDP-N-acetylglucosamine 2'-epimerase, uridine diphosphoacetylglucosamine 2'-epimerase, uridine diphospho-N-acetylglucosamine 2'-epimerase, and uridine diphosphate-N-acetylglucosamine-2'-epimerase. This enzyme participates in aminosugars metabolism.
In microorganisms this epimerase is involved in the synthesis of the capsule precursor UDP-ManNAcA. An inhibitor of the bacterial 2-epimerase, epimerox, has been described. Some of these enzymes are bifunctional. The UDP-N-acetylglucosamine 2-epimerase from rat liver displays both epimerase and kinase activity.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
See also
UDP-N-acetylglucosamine 2-epimerase (hydrolysing)
Notes
References
Further reading
Protein families
EC 5.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine%204-epimerase | In enzymology, an UDP-N-acetylglucosamine 4-epimerase () is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-D-glucosamine UDP-N-acetyl-D-galactosamine
Hence, this enzyme has one substrate, UDP-N-acetyl-D-glucosamine, and one product, UDP-N-acetyl-D-galactosamine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine 4-epimerase. Other names in common use include UDP acetylglucosamine epimerase, uridine diphosphoacetylglucosamine epimerase, uridine diphosphate N-acetylglucosamine-4-epimerase, and uridine 5'-diphospho-N-acetylglucosamine-4-epimerase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 5.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Vinylacetyl-CoA%20Delta-isomerase | In enzymology, a vinylacetyl-CoA Delta-isomerase () is an enzyme that catalyzes the chemical reaction
vinylacetyl-CoA crotonyl-CoA
Hence, this enzyme has one substrate, vinylacetyl-CoA, and one product, crotonyl-CoA.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is vinylacetyl-CoA Delta3-Delta2-isomerase. Other names in common use include vinylacetyl coenzyme A Delta-isomerase, vinylacetyl coenzyme A isomerase, and Delta3-cis-Delta2-trans-enoyl-CoA isomerase. This enzyme participates in butanoate 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 5.3.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Clyde%20Fastlink | Clyde Fastlink is a high frequency bus rapid transit system in Glasgow, Scotland. The system was designed to provide greater connectivity and faster journey times between Glasgow City Centre and the Queen Elizabeth University Hospital in Govan, as well as to several other key developments along the north and south banks of the Clyde Waterfront.
The project's initial conception and construction was led by Strathclyde Partnership for Transport (SPT) and Glasgow City Council. Operation of the system is contracted by the transport authority to Stagecoach West Scotland as an extension to their existing X19 service. McGill's also run their 23 and 26 services along sections of the right-of-way. The 4 mile (6km) long route began construction in September 2013, and was opened to passenger service in 2015 after over £40m of investment.
Route
The system runs along segregated and regular bus lanes running parallel to main roads, as well as mixed traffic sections, and uses priority signalling to allow buses in the system to move faster than regular traffic. The current 'North Bank' right-of-way originates in the City Centre, integrating with the two major rail hubs, Glasgow Queen Street and Glasgow Central. The route then follows the River Clyde in a westerly direction along the Broomielaw and over the Clyde Arc bridge, where it travels west on Govan Road's segregated infrastructure past the BBC offices at Pacific Quay. It continues towards the Govan Interchange and bypasses the hear |
https://en.wikipedia.org/wiki/Cyclin%20A2 | Cyclin-A2 is a protein that in humans is encoded by the CCNA2 gene. It is one of the two types of cyclin A: cyclin A1 is expressed during meiosis and embryogenesis while cyclin A2 is expressed in dividing somatic cells.
Function
Cyclin A2 belongs to the cyclin family, whose members regulate cell cycle progression by interacting with CDK kinases. Cyclin A2 is unique in that it can activate two different CDK kinases; it binds CDK2 during S phase, and CDK1 during the transition from G2 to M phase.
Cyclin A2 is synthesized at the onset of S phase and localizes to the nucleus, where the cyclin A2-CDK2 complex is implicated in the initiation and progression of DNA synthesis. Phosphorylation of CDC6 and MCM4 by the cyclin A2-CDK2 complex prevents re-replication of DNA during the cell cycle.
Cyclin A2 is involved in the G2/M transition but it cannot independently form a maturation promoting factor (MPF). Recent studies have shown that the cyclin A2-CDK1 complex triggers cyclin B1-CDK1 activation which results in chromatin condensation and the breakdown of the nuclear envelope.
Regulation
The levels of cyclin A2 are tightly synchronized with the progression of the cell cycle. Transcription initiates in late G1, peaks and plateaus in mid-S, and declines in G2.
Cyclin A2 transcription is mostly regulated by the transcription factor E2F and begins in G1, after the R point. Absence of cyclin A2 before the R point is due to the E2F inhibition by hypophosphorylated retinoblastoma p |
https://en.wikipedia.org/wiki/CCN1 | CCN1 may refer to:
Cyclin A2 - a protein in the cyclin family
CYR61 - a protein in the CCN family |
https://en.wikipedia.org/wiki/Potentiometric%20surface | A potentiometric surface is the imaginary plane where a given reservoir of fluid will "equalize out to" if allowed to flow. A potentiometric surface is based on hydraulic principles. For example, two connected storage tanks with one full and one empty will gradually fill/drain to the same level. This is because of atmospheric pressure and gravity. This idea is heavily used in city water supplies - a tall water tower containing the water supply has a great enough potentiometric surface to provide flowing water at a decent pressure to the houses it supplies.
For groundwater "potentiometric surface" is a synonym of "piezometric surface" which is an imaginary surface that defines the level to which water in a confined aquifer would rise were it completely pierced with wells. If the potentiometric surface lies above the ground surface, a flowing artesian well results. Contour maps and profiles of the potentiometric surface can be prepared from the well data.
See also
Hydraulic head
References
Earth: Portrait of a Planet; Second edition; Stephen Marshak, 2005 W.W. Norton & Company, Inc (Page 604–605)
Concepts in physics
Dynamics (mechanics)
Effects of gravitation |
https://en.wikipedia.org/wiki/Heuristic%20%28computer%20science%29 | In mathematical optimization and computer science, heuristic (from Greek εὑρίσκω "I find, discover") is a technique designed for problem solving more quickly when classic methods are too slow for finding an exact or approximate solution, or when classic methods fail to find any exact solution in a search space. This is achieved by trading optimality, completeness, accuracy, or precision for speed. In a way, it can be considered a shortcut.
A heuristic function, also simply called a heuristic, is a function that ranks alternatives in search algorithms at each branching step based on available information to decide which branch to follow. For example, it may approximate the exact solution.
Definition and motivation
The objective of a heuristic is to produce a solution in a reasonable time frame that is good enough for solving the problem at hand. This solution may not be the best of all the solutions to this problem, or it may simply approximate the exact solution. But it is still valuable because finding it does not require a prohibitively long time.
Heuristics may produce results by themselves, or they may be used in conjunction with optimization algorithms to improve their efficiency (e.g., they may be used to generate good seed values).
Results about NP-hardness in theoretical computer science make heuristics the only viable option for a variety of complex optimization problems that need to be routinely solved in real-world applications.
Heuristics underlie the wh |
https://en.wikipedia.org/wiki/Adenosylmethionine%20hydrolase | In enzymology, an adenosylmethionine hydrolase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-methionine + H2O L-homoserine + methylthioadenosine
Thus, the two substrates of this enzyme are S-adenosyl-L-methionine and H2O, whereas its two products are L-homoserine and methylthioadenosine.
This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds involving sulfur (thioether and trialkylsulfonium hydrolases). The systematic name of this enzyme class is S-adenosyl-L-methionine hydrolase. Other names in common use include S-adenosylmethionine cleaving enzyme, methylmethionine-sulfonium-salt hydrolase, and adenosylmethionine lyase.
References
EC 3.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alkenylglycerophosphocholine%20hydrolase | In enzymology, an alkenylglycerophosphocholine hydrolase () is an enzyme that catalyzes the chemical reaction
1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O an aldehyde + sn-glycero-3-phosphocholine
Thus, the two substrates of this enzyme are 1-(1-alkenyl)-sn-glycero-3-phosphocholine and H2O, whereas its two products are aldehyde and sn-glycero-3-phosphocholine.
This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is 1-(1-alkenyl)-sn-glycero-3-phosphocholine aldehydohydrolase. This enzyme is also called lysoplasmalogenase. This enzyme participates in ether lipid metabolism.
References
EC 3.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alkenylglycerophosphoethanolamine%20hydrolase | In enzymology, an alkenylglycerophosphoethanolamine hydrolase () is an enzyme that catalyzes the chemical reaction
1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O an aldehyde + sn-glycero-3-phosphoethanolamine
Thus, the two substrates of this enzyme are 1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine and H2O, whereas its two products are aldehyde and sn-glycero-3-phosphoethanolamine.
This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is 1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine aldehydohydrolase. This enzyme participates in ether lipid metabolism.
References
EC 3.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hepoxilin-epoxide%20hydrolase | In enzymology, a hepoxilin-epoxide hydrolase () is an enzyme that catalyzes the conversion of the epoxyalcohol metabolites arachidonic acid, hepoxilin A3 and hepoxilin B3 to their tri-hydroxyl products, trioxolin A3 and trioxilin B3, respectively. These reactions in general inactivate the two biologically active hepoxilins.
Enzyme activity
Hepoxilin-epoxide hydrolase converts the epoxide residue in hepoxilins A3 and B3 to Vicinal (chemistry) diols as exemplified in the following enzyme reaction for the metabolism of hepoxilin A3 to trioxilin A3:
The substrates of this enzyme are 8-hydroxy-11S,12Sepoxy-(5Z,8Z,14Z)-eicosatrienoic acid, i.e. hepoxilin A3 and H2O, whereas its product is 8,11,12-trihydroxy-(5Z,9E,14Z)-eicosatrienoic acid, i.e. the triol, trioxilin A3.
Epoxide hydrolases
Epoxide hydrolases represent a group of enzymes that convert various types of epoxides to vicinal diols. Several members of this group have this metabolic activity on fatty acid epoxides including microsomal epoxide hydrolase (i.e. epoxide hydrolase 1 or EH1), soluble epoxide hydrolase (i.e. epoxide hydrolase 2 or EH2), epoxide hydrolase 3 (EH3), epoxide hydrolase 4 (EH4), and leukotriene A4 hydrolase (see epoxide hydrolase). The systematic name of this enzyme class is (5Z,9E,14Z)-(8xi,11R,12S)-11,12-epoxy-8-hydroxyicosa-5,9,14-trienoat e hydrolase. Other names in common use include hepoxilin epoxide hydrolase, hepoxylin hydrolase, and hepoxilin A3 hydrolase. Since the hepoxilins are metabolit |
https://en.wikipedia.org/wiki/Isochorismatase | In enzymology, an isochorismatase () is an enzyme that catalyzes the chemical reaction
isochorismate + H2O 2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate
Thus, the two substrates of this enzyme are isochorismate and H2O, whereas its two products are 2,3-dihydroxy-2,3-dihydrobenzoate and pyruvate.
This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is isochorismate pyruvate-hydrolase. Other names in common use include 2,3-dihydro-2,3-dihydroxybenzoate synthase, 2,3-dihydroxy-2,3-dihydrobenzoate synthase, and 2,3-dihydroxy-2,3-dihydrobenzoic synthase. This enzyme participates in the biosynthesis of siderophore group (nonribosomal).
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 3.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Leukotriene-A4%20hydrolase | Leukotriene A4 hydrolase, also known as LTA4H is a human gene. The protein encoded by this gene is a bifunctional enzyme () which converts leukotriene A4 to leukotriene B4 and acts as an aminopeptidase.
Function
This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate hydrolase. Other names in common use include LTA4 hydrolase, LTA4H, and leukotriene A4 hydrolase. This enzyme participates in arachidonic acid metabolism.
Catalyzed reaction
Structure
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
Further reading
External links
EC 3.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Limonene-1%2C2-epoxide%20hydrolase | In enzymology, a limonene-1,2-epoxide hydrolase () is an enzyme that catalyzes the chemical reaction
limonene-1,2-epoxide + H2O limonene-1,2-diol
Thus, the two substrates of this enzyme are limonene-1,2-epoxide and H2O, whereas its product is limonene-1,2-diol.
This enzyme is found in the bacterium Rhodococcus erythropolis DCL14, where it plays a role in the limonene degradation pathway that allows the bacteria to catabolize limonene as a carbon and energy source. The enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is limonene-1,2-epoxide hydrolase. This enzyme is also called limonene oxide hydrolase. This enzyme has maximal activity at pH 7 and 50°C, and participates in limonene and pinene degradation.
Epoxide hydrolases catalyze the hydrolysis of epoxides to corresponding diols, which is important in detoxification, synthesis of signal molecules, or metabolism. Limonene-1,2- epoxide hydrolase (LEH) differs from many other epoxide hydrolases (EHs) in its structure and its novel one-step catalytic mechanism. EHs typically contain conserved α/β-hydrolase folds and catalytic residues which aid with epoxide stabilization and its subsequent hydrolysis reaction. However, LEH’s low molecular mass of 16 kDa suggests that it is too small to house these α/β-hydrolase folds and catalytic triad motifs found in other EHs. Moreover, compared to other EHs, LEH accepts a smaller diversity |
https://en.wikipedia.org/wiki/Microsomal%20epoxide%20hydrolase | In enzymology, a microsomal epoxide hydrolase (mEH) () is an enzyme that catalyzes the hydrolysis reaction between an epoxide and water to form a diol.
This enzyme plays a role in the uptake of bile salts within the large intestine. It functions as a Na+ dependent transporter. This enzyme participates in metabolism of xenobiotics by cytochrome p450. mEH has been identified as playing a large role in the detoxification and bioactivation of a wide variety of substrates, such as polycyclic aromatic hydrocarbons (PAHs), which are known for their carcinogenic properties.
The human homolog of microsomal epoxide hydrolase is EPHX1 and is located on chromosome 1.
Nomenclature
This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is cis-stilbene-oxide hydrolase. Other names in common use include epoxide hydratase (ambiguous), microsomal epoxide hydratase (ambiguous), epoxide hydrase, microsomal epoxide hydrase, arene-oxide hydratase (ambiguous), benzo[a]pyrene-4,5-oxide hydratase, benzo(a)pyrene-4,5-epoxide hydratase, aryl epoxide hydrase (ambiguous), cis-epoxide hydrolase, and mEH.
Structure
Microsomal epoxide hydrolase is a single polypeptide chain composed of 455 amino acids with a molecular weight of 52.96 kilodaltons. It is known that the N-terminal region of the enzyme is responsible for anchoring the protein to the cell membrane, while the C-terminal region of the enzyme co |
https://en.wikipedia.org/wiki/Trans-epoxysuccinate%20hydrolase | In enzymology, a trans-epoxysuccinate hydrolase () is an enzyme that catalyzes the chemical reaction
trans-2,3-epoxysuccinate + H2O meso-tartrate
Thus, the two substrates of this enzyme are trans-2,3-epoxysuccinate and H2O, whereas its product is meso-tartrate.
This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is trans-2,3-epoxysuccinate hydrolase. Other names in common use include trans-epoxysuccinate hydratase, and tartrate epoxydase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 3.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1-Aminocyclopropane-1-carboxylate%20synthase | The enzyme aminocyclopropane-1-carboxylic acid synthase (ACC synthase, ACS) (EC 4.4.1.14) catalyzes the synthesis of 1-Aminocyclopropane-1-carboxylic acid (ACC), a precursor for ethylene, from S-Adenosyl methionine (AdoMet, SAM), an intermediate in the Yang cycle and activated methyl cycle and a useful molecule for methyl transfer:
S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + S-methyl-5′-thioadenosine
Like other PLP dependent enzymes, it catalyzes the reaction through a quinonoid zwitterion intermediate and uses cofactor pyridoxal phosphate (PLP, the active form of vitamin B6) for stabilization.
This enzyme belongs to the family of lyases, specifically carbon-sulfur lyases. The systematic name of this enzyme class is S-adenosyl-L-methionine S-methyl-5′-thioadenosine-lyase (1-aminocyclopropane-1-carboxylate-forming). Other names in common use include 1-aminocyclopropanecarboxylate synthase, 1-aminocyclopropane-1-carboxylic acid synthase, 1-aminocyclopropane-1-carboxylate synthetase, aminocyclopropanecarboxylic acid synthase, aminocyclopropanecarboxylate synthase, ACC synthase, and ''S''-adenosyl-L-methionine methylthioadenosine-lyase. This enzyme participates in propanoate metabolism. It employs one cofactor, pyridoxal phosphate.
Enzyme mechanism
The reaction catalyzed by 1-aminocyclopropane-1-carboxylic acid synthase (ACS) is the committed and rate-limiting step in the biosynthesis of ethylene [20], a gaseous plant hormone that is responsible for the i |
https://en.wikipedia.org/wiki/2-C-methyl-D-erythritol%202%2C4-cyclodiphosphate%20synthase | 2-C-Methyl-D-erythritol 2,4-cyclodiphosphate synthase (MEcPP synthase, IspF, EC 4.6.1.12) is a zinc-dependent enzyme and a member of the YgbB N terminal protein domain, which participates in the MEP pathway (non-mevalonate pathway) of isoprenoid precursor biosynthesis. It catalyzes the following reaction:
4-diphosphocytidyl-2-C-methyl-D)erythritol 2-phosphate 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP
The enzyme is considered a phosphorus-oxygen lyase. The systematic name of this enzyme class is 2-phospho-4-(cytidine 5′-diphospho)-2-C-methyl-D-D-erythritol CMP-lyase (cyclizing; 2-C-methyl-D-erythritol 2,4-cyclodiphosphate-forming). Other names in common use include IspF, YgbB and MEcPP synthase.
Structural studies
As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , and .
References
EC 4.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-aminobutyryl-CoA%20ammonia-lyase | The enzyme 3-aminobutyryl-CoA ammonia-lyase (EC 4.3.1.14) catalyzes the chemical reaction
L-3-aminobutyryl-CoA crotonoyl-CoA + NH3
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-3-aminobutyryl-CoA ammonia-lyase (crotonoyl-CoA-forming). Other names in common use include L-3-aminobutyryl-CoA deaminase, and L-3-aminobutyryl-CoA ammonia-lyase.
References
EC 4.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-chloro-D-alanine%20dehydrochlorinase | The enzyme 3-chloro-D-alanine dehydrochlorinase (EC 4.5.1.2) catalyzes the reaction
3-chloro-D-alanine + H2O = pyruvate + chloride + NH3 (overall reaction)
(1a) 3-chloro-D-alanine = chloride + 2-aminoprop-2-enoate
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
This enzyme belongs to the family of lyases, specifically the class of carbon-halide lyases. The systematic name of this enzyme class is 3-chloro-D-alanine chloride-lyase (deaminating; pyruvate-forming). Other names in common use include β-chloro-D-alanine dehydrochlorinase, and 3-chloro-D-alanine chloride-lyase (deaminating). It employs one cofactor, pyridoxal phosphate.
References
EC 4.5.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-ketovalidoxylamine%20C-N-lyase | The enzyme 3-ketovalidoxylamine C-N-lyase (EC 4.3.3.1) catalyzes the chemical reaction
4-nitrophenyl-3-ketovalidamine 4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
This enzyme belongs to the family of lyases, specifically amine lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase [5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one-forming]. Other names in common use include 3-ketovalidoxylamine A C-N-lyase, p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase, and 4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase. It employs one cofactor, Ca2+.
References
EC 4.3.3
Calcium enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aspartate%20ammonia-lyase | The enzyme aspartate ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction
L-aspartate fumarate + NH3
The reaction is the basis of the industrial synthesis of aspartate.
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming). Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 4.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Beta-alanyl-CoA%20ammonia-lyase | The enzyme β-Alanyl-CoA ammonia-lyase (EC 4.3.1.6) catalyzes the chemical reaction
β-alanyl-CoA acryloyl-CoA + NH3
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is β-alanyl-CoA ammonia-lyase (acryloyl-CoA-forming). This enzyme is also called β-alanyl coenzyme A ammonia-lyase. This enzyme participates in β-alanine metabolism and propanoate metabolism.
References
EC 4.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carbamoyl-serine%20ammonia-lyase | The enzyme carbamoyl-serine ammonia-lyase (EC 4.3.1.13) catalyzes the chemical reaction
O-carbamoyl-L-serine + H2O = pyruvate + 2 NH3 + CO2 (overall reaction)
(1a) O-carbamoyl-L-serine = CO2 + NH3 + 2-aminoprop-2-enoate
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is O-carbamoyl-L-serine ammonia-lyase (decarboxylating; pyruvate-forming). Other names in common use include ''O-carbamoyl-L-serine deaminase, carbamoylserine deaminase, and O''-carbamoyl-L-serine ammonia-lyase (pyruvate-forming). It employs one cofactor, pyridoxal phosphate.
References
EC 4.3.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cystathionine%20beta-lyase | Cystathionine beta-lyase (), also commonly referred to as CBL or β-cystathionase, is an enzyme that primarily catalyzes the following α,β-elimination reaction
Thus, the substrate of this enzyme is L-cystathionine, whereas its 3 products are homocysteine, pyruvate, and ammonia.
Found in plants, bacteria, and yeast, cystathionine beta-lyase is an essential part of the methionine biosynthesis pathway as homocysteine can be directly converted into methionine by methionine synthase. The enzyme belongs to the γ-family of PLP-dependent enzymes due to its use of a pyridoxal-5'-phosphate (PLP) cofactor to cleave cystathionine. The enzyme also belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-cystathionine L-homocysteine-lyase (deaminating; pyruvate-forming). This enzyme participates in 5 metabolic pathways: methionine metabolism, cysteine metabolism, selenoamino acid metabolism, nitrogen metabolism, and sulfur metabolism.
Structure
Cystathionine beta-lyase is a tetramer composed of identical subunits, and is constructed as a dimer of dimers, each associated with one molecule of PLP bound to the catalytic site by a lysine residue. The dimer is formed by two monomers associated through several electrostatic, hydrogen bonding, and hydrophobic interactions, whereas the tetramer is stabilized through interactions between the N-terminal domains and key α-helices.
Most of the enzyme's catalytic site residues |
https://en.wikipedia.org/wiki/Cysteine%20lyase | The enzyme cysteine lyase (EC 4.4.1.10) catalyzes the chemical reaction
L-cysteine + sulfite L-cysteate + hydrogen sulfide
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-cysteine hydrogen-sulfide-lyase (adding sulfite; L-cysteate-forming). Other names in common use include cysteine (sulfite) lyase, and L-cysteine hydrogen-sulfide-lyase (adding sulfite). This enzyme participates in cysteine and taurine metabolism. It employs one cofactor, pyridoxal phosphate.
Evolution
Genes encoding cysteine lyase (CL) originated around 300 million years ago by a tandem gene duplication and neofunctionalization of cystathionine β-lyase (CBS) shortly after the split of mammalian and reptilian lineages. CL genes are found only in Sauropsida where they are involved in a metabolic pathway for sulfur metabolism in the chicken egg.
References
EC 4.4.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cysteine-S-conjugate%20beta-lyase | The enzyme cysteine-S-conjugate β-lyase (EC 4.4.1.13) catalyzes the chemical reaction
an L-cysteine-S-conjugate + H2O = a thiol + NH3 + pyruvate (overall reaction)
(1a) an L-cysteine-S-conjugate = a thiol + 2-aminoprop-2-enoate
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-cysteine-S-conjugate thiol-lyase (deaminating; pyruvate-forming). Other names in common use include cysteine conjugate β-lyase, glutamine transaminase K/cysteine conjugate β-lyase, and L-cysteine-S-conjugate thiol-lyase (deaminating). It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 4.4.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Cytidylate%20cyclase | The enzyme cytidylate cyclase (EC 4.6.1.6) is an enzyme that catalyzes the reaction
CTP = 3′,5′-cyclic CMP + diphosphate
This enzyme belongs to the family of lyases, specifically the class of phosphorus-oxygen lyases. The systematic name of this enzyme class is CTP diphosphate-lyase (cyclizing; 3′,5′-cyclic-CMP-forming). Other names in common use include 3',5'-cyclic-CMP synthase, cytidylyl cyclase, cytidyl cyclase, and CTP diphosphate-lyase (cyclizing).
References
EC 4.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-cysteine%20desulfhydrase | The enzyme D-cysteine desulfhydrase (EC 4.4.1.15) catalyzes the chemical reaction
D-cysteine + H2O sulfide + NH3 + pyruvate
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is D-cysteine sulfide-lyase (deaminating; pyruvate-forming). Other names in common use include D-cysteine lyase, and D-cysteine sulfide-lyase (deaminating). This enzyme participates in cysteine metabolism.
References
EC 4.4.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DDT-dehydrochlorinase | The enzyme DDT-dehydrochlorinase (EC 4.5.1.1) catalyzes the reaction
1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride
This enzyme belongs to the family of lyases, specifically the class of carbon-halide lyases. The systematic name of this enzyme class is 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane chloride-lyase [1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene-forming]. Other names in common use include DDT-ase, 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane chloride-lyase, dehydrohalogenase, and DDTase.
References
EC 4.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deacetylipecoside%20synthase | The enzyme deacetylipecoside synthase (EC 4.3.3.4) catalyzes the chemical reaction
deacetylipecoside + H2O dopamine + secologanin
This enzyme belongs to the family of lyases, specifically amine lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is deacetylipecoside dopamine-lyase (secologanin-forming). This enzyme is also called deacetylipecoside dopamine-lyase. It participates in indole and ipecac alkaloid biosynthesis.
References
EC 4.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deacetylisoipecoside%20synthase | The enzyme deacetylisoipecoside synthase (EC 4.3.3.3) catalyzes the chemical reaction
deacetylisoipecoside + H2O dopamine + secologanin
This enzyme belongs to the family of lyases, specifically amine lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is deacetylisoipecoside dopamine-lyase (secologanin-forming). It is also called deacetylisoipecoside dopamine-lyase. It participates in indole and ipecac alkaloid biosynthesis.
References
EC 4.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diaminopropionate%20ammonia-lyase | The enzyme diaminopropionate ammonia-lyase (EC 4.3.1.15) catalyzes the chemical reaction
2,3-diaminopropanoate + H2O pyruvate + 2 NH3
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is 2,3-diaminopropanoate ammonia-lyase (adding water; pyruvate-forming). Other names in common use include diaminopropionatase, α,β-diaminopropionate ammonia-lyase, 2,3-diaminopropionate ammonia-lyase, and 2,3-diaminopropanoate ammonia-lyase. It employs one cofactor, pyridoxal phosphate.
References
EC 4.3.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
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