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https://en.wikipedia.org/wiki/Alpha-ribazole%20phosphatase | The primary biochemical reaction catalyzed by the enzyme adenosylcobalamin/α-ribazole phosphatase (formerly α-ribazole phosphatase) (EC 3.1.3.73) is
adenosylcobalamin 5′-phosphate + H2O = coenzyme B12 + phosphate
This enzyme can also catalyze the following reaction in vitro, however it is not the biologically relevant reaction
α-ribazole 5′-phosphate + H2O α-ribazole + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is adenosylcobalamin/α-ribazole-5′-phosphate phosphohydrolase. This enzyme is also called CobC. It is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
See also
Cobalamin biosynthesis
Structural studies
As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , and .
References
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Aminoacyl-tRNA%20hydrolase | The enzyme aminoacyl-tRNA hydrolase (EC 3.1.1.29) catalyzes the reaction
N-substituted aminoacyl-tRNA + H2O N-substituted amino acid + tRNA
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is aminoacyl-tRNA aminoacylhydrolase. Other names in common use include aminoacyl-transfer ribonucleate hydrolase, N-substituted aminoacyl transfer RNA hydrolase, and peptidyl-tRNA hydrolase.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , and .
References
EC 3.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Arylesterase | The enzyme arylesterase (EC 3.1.1.2) catalyzes the reaction
a phenyl acetate + H2O a phenol + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is aryl-ester hydrolase. Other names in common use include A-esterase, paraoxonase, and aromatic esterase. This enzyme participates in bisphenol a degradation.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Bile-acid-CoA%20hydrolase | In enzymology, a bile-acid-CoA hydrolase () is an enzyme that catalyzes the chemical reaction
deoxycholoyl-CoA + H2O CoA + deoxycholate
Thus, the two substrates of this enzyme are deoxycholoyl-CoA and H2O, whereas its two products are CoA and deoxycholate.
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is deoxycholoyl-CoA hydrolase.
References
EC 3.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Bis%282-ethylhexyl%29phthalate%20esterase | The enzyme bis(2-ethylhexyl)phthalate esterase (EC 3.1.1.60) catalyzes the reaction
bis(2-ethylhexyl)phthalate + H2O 2-ethylhexyl phthalate + 2-ethylhexan-1-ol
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is bis(2-ethylhexyl)phthalate acylhydrolase. This enzyme is also called DEHP esterase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Bisphosphoglycerate%20phosphatase | In enzymology, a bisphosphoglycerate phosphatase () is an enzyme that catalyzes the chemical reaction
2,3-bisphospho-D-glycerate + H2O 3-phospho-D-glycerate + phosphate
Thus, the two substrates of this enzyme are 2,3-bisphospho-D-glycerate and H2O, whereas its two products are 3-phospho-D-glycerate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is 2,3-bisphospho-D-glycerate 2-phosphohydrolase. Other names in common use include 2,3-diphosphoglycerate phosphatase, diphosphoglycerate phosphatase, 2,3-diphosphoglyceric acid phosphatase, 2,3-bisphosphoglycerate phosphatase, and glycerate-2,3-diphosphate phosphatase. This enzyme participates in glycolysis/gluconeogenesis.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Caldesmon-phosphatase | The enzyme caldesmon-phosphatase (EC 3.1.3.55) catalyzes the reaction
caldesmon phosphate + H2O caldesmon + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is caldesmon-phosphate phosphohydrolase. Other names in common use include SMP-I, and smooth muscle caldesmon phosphatase.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Carboxylesterase | The enzyme carboxylesterase (or carboxylic-ester hydrolase, EC 3.1.1.1; systematic name carboxylic-ester hydrolase) catalyzes reactions of the following form:
a carboxylic ester + H2O an alcohol + a carboxylate
Most enzymes from this group are serine hydrolases belonging to the superfamily of proteins with α/β hydrolase fold. Some exceptions include an esterase with β-lactamase-like structure ().
Carboxylesterases are widely distributed in nature, and are common in mammalian liver. Many participate in phase I metabolism of xenobiotics such as toxins or drugs; the resulting carboxylates are then conjugated by other enzymes to increase solubility and eventually excreted. The essential polyunsaturated fatty acid arachidonic acid (AA C20H32O2; 20:4, n-6), formed by the synthesis from dietary linoleic acid (LA: C18H32O2 18:2, n-6), has a role as a human carboxylesterase inhibitor.
The carboxylesterase family of evolutionarily related proteins (those with clear sequence homology to each other) includes a number of proteins with different substrate specificities, such as acetylcholinesterases.
Examples
acetylcholinesterase
ali-esterase,
B-esterase,
butyrate esterase,
butyryl esterase,
carboxylesterase 1
carboxylesterase 2
carboxylesterase 3
esterase A,
esterase B,
esterase D,
methylbutyrase,
methylbutyrate esterase,
monobutyrase,
procaine esterase,
propionyl esterase,
triacetin esterase,
vitamin A esterase, and
cocaine esterase
The last enzyme also participa |
https://en.wikipedia.org/wiki/Carboxymethylenebutenolidase | In enzymology, a carboxymethylenebutenolidase (, also known as CMBL and dienelactone hydrolase) is an enzyme that catalyzes the chemical reaction
4-carboxymethylenebut-2-en-4-olide + H2O 4-oxohex-2-enedioate
Thus, the two substrates of this enzyme are 4-carboxymethylenebut-2-en-4-olide and H2O, whereas its product is 4-oxohex-2-enedioate.
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 4-carboxymethylenebut-2-en-4-olide lactonohydrolase. Other names in common use include maleylacetate enol-lactonase, dienelactone hydrolase, and carboxymethylene butenolide hydrolase. This enzyme participates in gamma-hexachlorocyclohexane degradation and 1,4-dichlorobenzene degradation.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , and .
References
EC 3.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Cephalosporin-C%20deacetylase | The enzyme cephalosporin-C deacetylase (EC 3.1.1.41) catalyzes the reaction
cephalosporin C + H2O deacetylcephalosporin C + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is cephalosporin-C acetylhydrolase. Other names in common use include cephalosporin C acetyl-hydrolase, cephalosporin C acetylase, cephalosporin acetylesterase, cephalosporin C acetylesterase, cephalosporin C acetyl-esterase, and cephalosporin C deacetylase. This enzyme participates in penicillin and cephalosporin biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 3.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/GPR179 | Probable G-protein coupled receptor 179 is a protein that in humans is encoded by the GPR179 gene.
Clinical relevance
Mutations in this gene have been associated to cases of congenital stationary Night Blindness.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Cetraxate%20benzylesterase | The enzyme cetraxate benzylesterase (EC 3.1.1.70) catalyzes the reaction
cetraxate benzyl ester + H2O cetraxate + benzyl alcohol
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is cetraxate-benzyl-ester benzylhydrolase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chlorogenate%20hydrolase | The enzyme chlorogenate hydrolase (EC 3.1.1.42) catalyzes the reaction
chlorogenate + H2O caffeate + quinate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is chlorogenate hydrolase. Other names in common use include chlorogenase, and chlorogenic acid esterase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Choline-sulfatase | The enzyme choline-sulfatase (EC 3.1.6.6) catalyzes the reaction
choline sulfate + H2O choline + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name is choline-sulfate sulfohydrolase.
References
EC 3.1.6
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Choloyl-CoA%20hydrolase | The enzyme choloyl-CoA hydrolase (EC 3.1.2.27) catalyzes the reaction
choloyl-CoA + H2O cholate + CoA
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is choloyl-CoA hydrolase. Other names in common use include PTE-2 (ambiguous), choloyl-coenzyme A thioesterase, chenodeoxycholoyl-coenzyme A thioesterase, and peroxisomal acyl-CoA thioesterase 2.
References
EC 3.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chondro-4-sulfatase | The enzyme chondro-4-sulfatase (EC 3.1.6.9) catalyzes the reaction
4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine 4-sulfate + H2O 4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name is 4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase. This enzyme is also called chondroitin-4-sulfatase.
References
EC 3.1.6
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chondro-6-sulfatase | The enzyme chondro-6-sulfatase (EC 3.1.6.10) catalyzes the reaction
4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine 6-sulfate + H2O 4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name is 4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine-6-sulfate 6-sulfohydrolase.
References
EC 3.1.6
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Citrate%20lyase%20deacetylase | The enzyme citrate lyase deacetylase (EC 3.1.2.16) catalyzes the reaction
acetyl-[citrate (pro-3S)-lyase] + H2O = holo-[citrate (pro-3S)-lyase] + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is acetyl-[citrate-(pro-3S)-lyase] hydrolase. This enzyme is also called [citrate-(pro-3S)-lyase] thiolesterase.
References
EC 3.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CMP-N-acylneuraminate%20phosphodiesterase | The enzyme CMP-N-acylneuraminate phosphodiesterase (EC 3.1.4.40) catalyzes the reaction
CMP-N-acylneuraminate + H2O CMP + N-acylneuraminate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is CMP-N-acylneuraminate N-acylneuraminohydrolase. Other names in common use include CMP-sialate hydrolase, CMP-sialic acid hydrolase, CMP-N-acylneuraminic acid hydrolase, cytidine monophosphosialic hydrolase, cytidine monophosphosialate hydrolase, cytidine monophosphate-N-acetylneuraminic acid hydrolase, and CMP-N-acetylneuraminate hydrolase.
References
EC 3.1.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cutinase | The enzyme cutinase (systematic name: cutin hydrolase, EC 3.1.1.74) is a member of the hydrolase family. It catalyzes the following reaction:
R1COOR2 + H2O -> R1COOH + R2OH
In biological systems, the reactant carboxylic ester is a constituent of the cutin polymer, and the hydrolysis of cutin results in the formation of alcohol and carboxylic acid monomer products.
Nomenclature
Cutinase has an assigned enzyme commission number of EC 3.1.1.74. Cutinase is in the third class of enzymes, meaning that its primary function is to hydrolyze its substrate (in this case, cutin). Within the third class, cutinase is further categorized into the first subclass, which indicates that it specifically hydrolyzes ester bonds. It is then placed in the first sub-subclass, meaning that it targets carboxylic esters, which are those that join together cutin polymers.
Function
Most plants have a layer composed of cutin, called the cuticle, on their aboveground surfaces such as stems, leaves, and fruits. This layer of cutin is formed by a matrix-like structure that contains waxy components embedded in the carbohydrate layers. The molecule, cutin, which composes most of the cuticle matrix (40-80%), is composed primarily of fatty acid chains that are polymerized via carboxylic ester bonds.
Research suggests that cutin plays a critical role in preventing pathogenic infections in plant systems. For instance, experiments conducted on tomato plants that had a substantial inability to synthesize cutin |
https://en.wikipedia.org/wiki/D-arabinonolactonase | The enzyme D-arabinonolactonase (EC 3.1.1.30) the reaction
D-arabinono-1,4-lactone + H2O D-arabinonate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is D-arabinono-1,4-lactone lactonohydrolase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deoxylimonate%20A-ring-lactonase | The enzyme deoxylimonate A-ring-lactonase (EC 3.1.1.46) catalyzes the reaction
deoxylimonate + H2O deoxylimononic acid D-ring-lactone
The reaction opens the A-ring-lactone of the triterpenoid deoxylimonic acid, leaving the D-ring-lactone intact.
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is deoxylimonate A-ring-lactonohydrolase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deoxynucleotide%203%27-phosphatase | The enzyme deoxynucleotide 3′-phosphatase (EC 3.1.3.34) catalyzes the reaction
a 2′-deoxyribonucleoside 3′-phosphate + H2O = a 2′-deoxyribonucleoside + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 2′-deoxyribonucleotide 3′-phosphohydrolase. Other names in common use include 3′-deoxynucleotidase, and 3′-deoxyribonucleotidase.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DGTPase | The enzyme dGTPase (EC 3.1.5.1) catalyzes the reaction
dGTP + H2O deoxyguanosine + triphosphate
This enzyme belongs to the family of hydrolases, specifically those acting on triphosphoric monoester bonds. The systematic name is dGTP triphosphohydrolase. Other names in common use include deoxy-GTPase, deoxyguanosine 5-triphosphate triphosphohydrolase, deoxyguanosine triphosphatase, and deoxyguanosine triphosphate triphosphohydrolase. This enzyme participates in purine metabolism.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 3.1.5
Enzymes of known structure |
https://en.wikipedia.org/wiki/Dihydrocoumarin%20hydrolase | The enzyme dihydrocoumarin hydrolase (EC 3.1.1.35) catalyzes the reaction
dihydrocoumarin + H2O melilotate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is dihydrocoumarin lactonohydrolase. This enzyme participates in fluorene degradation.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diisopropyl-fluorophosphatase | The enzyme diisopropyl-fluorophosphatase (EC 3.1.8.2) catalyzes the reaction
diisopropyl fluorophosphate + H2O diisopropyl phosphate + fluoride
This enzyme belongs to the family of hydrolases, specifically those acting on ester bonds phosphoric-triester hydrolases. The systematic name is diisopropyl-fluorophosphate fluorohydrolase. Other names in common use include DFPase, tabunase, somanase, organophosphorus acid anhydrolase, organophosphate acid anhydrase, OPA anhydrase, diisopropylphosphofluoridase, dialkylfluorophosphatase, diisopropyl phosphorofluoridate hydrolase, isopropylphosphorofluoridase, and diisopropylfluorophosphonate dehalogenase. It employs one cofactor, divalent cation. At least one compound, chelating agent is known to inhibit this enzyme.
Structural studies
As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , and .
References
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 4, Academic Press, New York, 1960, p. 541-550.
EC 3.1.8
Enzymes of known structure |
https://en.wikipedia.org/wiki/Disulfoglucosamine-6-sulfatase | The enzyme disulfoglucosamine-6-sulfatase (EC 3.1.6.1) catalyzes the reaction
2-N,6-O-disulfo-D-glucosamine + H2O 2-N-sulfo-D-glucosamine + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name is 2-N,6-O-disulfo-D-glucosamine 6-sulfohydrolase. Other names in common use include N-sulfoglucosamine-6-sulfatase, and 6,N-disulfoglucosamine 6-O-sulfohydrolase.
References
EC 3.1.6
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-lactate-2-sulfatase | The enzyme D-lactate-2-sulfatase (EC 3.1.6.17) catalyzes the reaction
(R)-2-O-sulfolactate + H2O (R)-lactate + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name is (R)-2-O-sulfolactate 2-sulfohydrolase.
The other name (S)-2-O-sulfolactate 2-sulfohydrolase specifies the stereochemistry incorrectly.
References
EC 3.1.6
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dodecanoyl-%28acyl-carrier-protein%29%20hydrolase | The enzyme dodecanoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.21) catalyzes the reaction
a dodecanoyl-[acyl-carrier-protein] + H2O an [acyl-carrier-protein] + dodecanoate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is dodecanoyl-[acyl-carrier-protein] hydrolase. Other names in common use include lauryl-acyl-carrier-protein hydrolase, dodecanoyl-acyl-carrier-protein hydrolase, dodecyl-acyl-carrier protein hydrolase, and dodecanoyl-[acyl-carrier protein] hydrolase.
References
EC 3.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dolichyl-phosphatase | The enzyme dolichyl-phosphatase (EC 3.1.3.51) catalyzes the reaction
dolichyl phosphate + H2O dolichol + phosphate
This enzyme belongs to the family of hydrolases, to be specific, those acting on phosphoric monoester bonds. The systematic name is dolichyl-phosphate phosphohydrolase. Other names in common use include dolichol phosphate phosphatase, dolichol phosphatase, dolichol monophosphatase, dolichyl monophosphate phosphatase, dolichyl phosphate phosphatase, polyisoprenyl phosphate phosphatase, polyprenylphosphate phosphatase, and Dol-P phosphatase. This enzyme participates in N-linked-glycan biosynthesis.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dolichylphosphate-glucose%20phosphodiesterase | The enzyme dolichylphosphate-glucose phosphodiesterase (EC 3.1.4.48) catalyzes the reaction
dolichyl β-D-glucosyl phosphate + H2O dolichyl phosphate + D-glucose
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is dolichyl-β-D-glucosyl-phosphate dolichylphosphohydrolase. Other names in common use include dolichol phosphoglucose phosphodiesterase, and Dol-P-Glc phosphodiesterase. This enzyme participates in n-glycan biosynthesis.
References
EC 3.1.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dolichylphosphate-mannose%20phosphodiesterase | The enzyme dolichylphosphate-mannose phosphodiesterase (EC 3.1.4.49) catalyzes the reaction
dolichyl β-D-mannosyl phosphate + H2O dolichyl phosphate + D-mannose
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is dolichyl-β-D-mannosyl-phosphate dolichylphosphohydrolase. This enzyme is also called mannosylphosphodolichol phosphodiesterase.
References
EC 3.1.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Fatty-acyl-ethyl-ester%20synthase | The enzyme fatty-acyl-ethyl-ester synthase (EC 3.1.1.67) catalyzes the reaction
a long-chain-fatty-acyl ethyl ester + H2O a long-chain-fatty acid + ethanol
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is long-chain-fatty-acyl-ethyl-ester acylhydrolase. This enzyme is also called FAEES.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Feruloyl%20esterase | The enzyme feruloyl esterase (EC 3.1.1.73) catalyzes the reaction
feruloyl-polysaccharide + H2O ferulate + polysaccharide
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 4-hydroxy-3-methoxycinnamoyl-sugar hydrolase. Other names in common use include ferulic acid esterase (FAE), hydroxycinnamoyl esterase, hemicellulase accessory enzyme, cinnamoyl ester hydrolase (cinnAE).
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 3.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Formyl-CoA%20hydrolase | The enzyme formyl-CoA hydrolase (EC 3.1.2.10) catalyzes the reaction
formyl-CoA + H2O CoA + formate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is formyl-CoA hydrolase. This enzyme is also called formyl coenzyme A hydrolase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 3.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Fructose-2%2C6-bisphosphate%202-phosphatase | The enzyme fructose-2,6-bisphosphate 2-phosphatase ({EC 3.1.3.46) catalyzes the reaction
β-D-fructose 2,6-bisphosphate + H2O D-fructose 6-phosphate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is β-D-fructose-2,6-bisphosphate 2-phosphohydrolase. Other names in common use include fructose-2,6-bisphosphatase, and D-fructose-2,6-bisphosphate 2-phosphohydrolase. This enzyme participates in fructose and mannose metabolism.
Structural studies
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , and .
References
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Fructose-2%2C6-bisphosphate%206-phosphatase | The enzyme fructose-2,6-bisphosphate 6-phosphatase (EC 3.1.3.54) catalyzes the reaction
β-D-fructose 2,6-bisphosphate + H2O β-D-fructofuranose 2-phosphate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is β-D-fructose-2,6-bisphosphate 6-phosphohydrolase. Other names in common use include fructose 2,6-bisphosphate-6-phosphohydrolase, fructose-2,6-bisphosphate 6-phosphohydrolase, and D-fructose-2,6-bisphosphate 6-phosphohydrolase. This enzyme participates in fructose and mannose metabolism.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Fusarinine-C%20ornithinesterase | The enzyme fusarinine-C ornithinesterase (EC 3.1.1.48) catalyzes the reaction
N 5-acyl-L-ornithine ester + H2O N 5-acyl-L-ornithine + an alcohol
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is N 5-L-ornithine-ester hydrolase. Other names in common use include ornithine esterase, and 5-N 5-L-ornithine-ester hydrolase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Galactolipase | The enzyme galactolipase (EC 3.1.1.26) catalyzes the reaction
1,2-diacyl-3-β-D-galactosyl-sn-glycerol + 2 H2O 3-β-D-galactosyl-sn-glycerol + 2 carboxylates
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 1,2-diacyl-3-β-D-galactosyl-sn-glycerol acylhydrolase. Other names in common use include galactolipid lipase, polygalactolipase, and galactolipid acylhydrolase. This enzyme participates in glycerolipid metabolism.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Gluconolactonase | The enzyme gluconolactonase (EC 3.1.1.17) catalyzes the reaction
D-glucono-1,5-lactone + H2O D-gluconate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is D-glucono-1,5-lactone lactonohydrolase. Other names in common use include lactonase, aldonolactonase, glucono-δ-lactonase, and gulonolactonase. This enzyme participates in three metabolic pathways: pentose phosphate pathway, ascorbate and aldarate metabolism, and caprolactam degradation.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucose-1-phosphatase | The enzyme glucose-1-phosphatase (EC 3.1.3.10) catalyzes the reaction
α-D-glucose 1-phosphate + H2O D-glucose + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is α-D-glucose-1-phosphate phosphohydrolase. This enzyme participates in glycolysis and gluconeogenesis.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glucose-1-phospho-D-mannosylglycoprotein%20phosphodiesterase | The enzyme glucose-1-phospho-D-mannosylglycoprotein phosphodiesterase (EC 3.1.4.51) catalyzes the reaction
6-(D-glucose-1-phospho)-D-mannosylglycoprotein + H2O α-D-glucose 1-phosphate + D-mannosylglycoprotein
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is 6-(D-glucose-1-phospho)-D-mannosylglycoprotein glucose-1-phosphohydrolase. This enzyme is also called α-glucose-1-phosphate phosphodiesterase.
References
EC 3.1.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucosylglycerol%203-phosphatase | The enzyme glucosylglycerol 3-phosphatase (EC 3.1.3.69) catalyzes the reaction
2-O-(α-Dglucosyl)-sn-glycerol-3-phosphate + H2O = 2-O-(α-D-glucopyranosyl)glycerol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 2-O-(α-D-glucopyranosyl)-sn-glycerol-3-phosphate phosphohydrolase. This enzyme is also called salt tolerance protein A, StpA.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutathione%20thiolesterase | The enzyme glutathione thiolesterase (EC 3.1.2.7) catalyzes the reaction
S-acylglutathione + H2O glutathione + a carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is S-acylglutathione hydrolase. It is also called citryl-glutathione thioesterhydrolase.
References
EC 3.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol-1%2C2-cyclic-phosphate%202-phosphodiesterase | The enzyme glycerol-1,2-cyclic-phosphate 2-phosphodiesterase (EC 3.1.4.42) catalyzes the reaction
glycerol 1,2-cyclic phosphate + H2O glycerol 1-phosphate
This enzyme belongs to the family of hydrolases, specifically, those acting on phosphoric diester bonds. The systematic name is rac-glycerol-1,2-cyclic-phosphate 2-glycerophosphohydrolase. This enzyme is also called rac-glycerol 1:2-cyclic phosphate 2-phosphodiesterase.
References
EC 3.1.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol-1-phosphatase | The enzyme glycerol-1-phosphatase (EC 3.1.3.21) catalyzes the reaction
glycerol 1-phosphate + H2O glycerol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is glycerol-1-phosphate phosphohydrolase. Other names in common use include α-glycerophosphatase, α-glycerol phosphatase, glycerol 3-phosphatase, glycerol-3-phosphate phosphatase, and glycerol 3-phosphate phosphohydrolase. This enzyme participates in glycerolipid metabolism.
Among the organisms that have been shown to express this enzymatic activity are A. thaliana (plant) via the AtSgpp and AtGpp gene products; D. salina (alga); S. cerevisiae (fungus) via the GPP1/RHR2/YIL053W and GPP2/HOR2/YER062C gene products; C. albicans (fungus) via the GPP1 gene product; M. tuberculosis (bacteria) via the rv1692 gene product; and C57BL/6N mice and Wistar rats (mammals) via the PGP gene product.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol-2-phosphatase | The enzyme glycerol-2-phosphatase (EC 3.1.3.19) catalyzes the reaction
glycerol 2-phosphate + H2O glycerol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is glycerol-2-phosphate phosphohydrolase. Other names in common use include β-glycerophosphatase, β-glycerophosphate phosphatase, and 2-glycerophosphatase.
References
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 37-47.
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerophosphocholine%20cholinephosphodiesterase | The enzyme glycerophosphocholine cholinephosphodiesterase (EC 3.1.4.38) is an enzyme that catalyzes the reaction
sn-glycero-3-phosphocholine + H2O = glycerol + phosphocholine
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is sn-glycero-3-phosphocholine cholinephosphohydrolase. This enzyme is also called L-3-glycerylphosphinicocholine cholinephosphohydrolase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 3.1.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glycerophosphocholine%20phosphodiesterase | The enzyme glycerophosphocholine phosphodiesterase (EC 3.1.4.2) catalyzes the reaction
sn-glycero-3-phosphocholine + H2O choline + sn-glycerol 3-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is sn-glycero-3-phosphocholine glycerophosphohydrolase. Other names in common use include glycerophosphinicocholine diesterase, glycerylphosphorylcholinediesterase, ''sn''-glycero-3-phosphorylcholine diesterase, glycerolphosphorylcholine phosphodiesterase, and glycerophosphohydrolase. This enzyme participates in glycerophospholipid metabolism.
References
EC 3.1.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerophosphodiester%20phosphodiesterase | The enzyme glycerophosphodiester phosphodiesterase ({EC 3.1.4.46) catalyzes the reaction
a glycerophosphodiester + H2O an alcohol + sn-glycerol 3-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is glycerophosphodiester glycerophosphohydrolase. Other names in common use include gene hpd protein, glycerophosphoryl diester phosphodiesterase, and IgD-binding protein D. This enzyme participates in glycerophospholipid metabolism.
References
EC 3.1.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glycerophosphoinositol%20glycerophosphodiesterase | The enzyme glycerophosphoinositol glycerophosphodiesterase (EC 3.1.4.44) catalyzes the reaction
1-(sn-glycero-3-phospho)-1D-myoinositol + H2O myo-inositol + sn-glycerol 3-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is 1-(sn-glycero-3-phospho)-1D-myo-inositol glycerophosphohydrolase. Other names in common use include sn-glycero(3)phosphoinositol glycerophosphohydrolase, and ''sn''-glycero-3-phospho-1-inositol glycerophosphohydrolase.
References
EC 3.1.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerophosphoinositol%20inositolphosphodiesterase | The enzyme glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) is an enzyme that catalyzes the chemical reaction
1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O glycerol + 1D-myo-inositol 1-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is 1-(sn-glycero-3-phospho)-1D-myo-inositol inositolphosphohydrolase. Other names in common use include 1,2-cyclic-inositol-phosphate phosphodiesterase, D-myo-inositol 1:2-cyclic phosphate 2-phosphohydrolase, D-inositol 1,2-cyclic phosphate 2-phosphohydrolase, D-myo-inositol 1,2-cyclic phosphate 2-phosphohydrolase, 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase, and inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase.
This enzyme 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase, was reported to be identical to annexin III. Sekar and co-workers clearly demonstrated the dissociation of 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase activity from annexin III. Perron and co-workers confirmed on the basis of structural studies that annexin III did not possess an enzymatic activity. While the physiological significance of this enzymatic activity is still not clear, Sekar et al. [Biochem. Mol. Med. 61:95-100, 1007] reported over 10-fold increased release of this enzymatic activity in several patients admitted to the hospital's intensive care unit.
References
EC 3.1.4
Enzymes of unknown str |
https://en.wikipedia.org/wiki/%28glycogen-synthase-D%29%20phosphatase | The enzyme [glycogen-synthase-D] phosphatase ({EC 3.1.3.42) catalyzes the reaction
[glycogen-synthase D] + HO [glycogen-synthase I] + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is [UDP-glucose:glycogen 4-α-D-glucosyltransferase-D] phosphohydrolase. Other names in common use include uridine diphosphoglucose-glycogen glucosyltransferase phosphatase, UDP-glycogen glucosyltransferase phosphatase, UDPglucose-glycogen glucosyltransferase phosphatase, glycogen glucosyltransferase phosphatase, glycogen synthetase phosphatase, glycogen synthase phosphatase, glycogen synthase D phosphatase, Mg dependent glycogen synthase phosphatase, and phosphatase type 2 °C.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycosulfatase | The enzyme glycosulfatase (EC 3.1.6.3) catalyzes the reaction
D-glucose 6-sulfate + H2O D-glucose + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is sugar-sulfate sulfohydrolase. This enzyme is also called glucosulfatase. This enzyme participates in glycolysis and gluconeogenesis.
References
EC 3.1.6
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Guanidinodeoxy-scyllo-inositol-4-phosphatase | The enzyme guanidinodeoxy-scyllo-inositol-4-phosphatase (EC 3.1.3.40) catalyzes the reaction
1-guanidino-1-deoxy-scyllo-inositol 4-phosphate + H2O 1-guanidino-1-deoxy-scyllo-inositol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 1-guanidino-1-deoxy-scyllo-inositol-4-phosphate 4-phosphohydrolase. Other names in common use include 1-guanidino-scyllo-inositol 4-phosphatase, and 1-guanidino-1-deoxy-scyllo-inositol-4-P phosphohydrolase.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Guanosine-3%27%2C5%27-bis%28diphosphate%29%203%27-diphosphatase | The enzyme guanosine-3′,5′-bis(diphosphate) 3′-diphosphatase (EC 3.1.7.2) catalyzes the reaction
guanosine 3′,5′-bis(diphosphate) + H2O GDP + diphosphate
This enzyme belongs to the family of hydrolases, specifically those acting on diphosphoric monoester bonds. The systematic name is guanosine-3′,5′-bis(diphosphate) 3′-diphosphohydrolase. Other names in common use include guanosine-3′,5′-bis(diphosphate) 3′-pyrophosphatase, PpGpp-3'-pyrophosphohydrolase, and PpGpp phosphohydrolase. This enzyme participates in purine metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 3.1.7
Enzymes of known structure |
https://en.wikipedia.org/wiki/Histidinol-phosphatase | The enzyme histidinol-phosphatase (EC 3.1.3.15) catalyzes the reaction
L-histidinol phosphate + H2O L-histidinol + phosphate
This enzyme participates in histidine metabolism.
Nomenclature
This enzyme belongs to the family of hydrolases, to be specific, those acting on phosphoric monoester bonds. The systematic name is L-histidinol-phosphate phosphohydrolase. Other names in common use include histidinol phosphate phosphatase, L-histidinol phosphate phosphatase, histidinolphosphate phosphatase, HPpase, and histidinolphosphatase.
E. coli
In E. coli the enzyme encoded by the gene hisB is a fused imidazoleglycerol-phosphate dehydratase and histidinol-phosphatase.
References
Further reading
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Hydroxybutyrate-dimer%20hydrolase | The enzyme hydroxybutyrate-dimer hydrolase (EC 3.1.1.22) catalyzes the reaction
(R)-3-((R)-3-hydroxybutanoyloxy)butanoate + H2O 2 (R)-3-hydroxybutanoate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is (R)-3-((R)-3-hydroxybutanoyloxy)butanoate hydroxybutanoylhydrolase. The enzyme is also called D-(–)-3-hydroxybutyrate-dimer hydrolase. It participates in butanoate metabolism.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroxymethylglutaryl-CoA%20hydrolase | The enzyme hydroxymethylglutaryl-CoA hydrolase (EC 3.1.2.5) catalyzes the reaction
S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is S-(2-hydroxyacyl)glutathione hydrolase. Other names in common use include β-hydroxy-beta-methylglutaryl coenzyme A hydrolase, β-hydroxy-β-methylglutaryl coenzyme A deacylase, hydroxymethylglutaryl coenzyme A hydrolase, hydroxymethylglutaryl coenzyme A deacylase, and 3-hydroxy-3-methylglutaryl-CoA hydrolase.
References
EC 3.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28hydroxymethylglutaryl-CoA%20reductase%20%28NADPH%29%29-phosphatase | The enzyme [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase (EC 3.1.3.47) catalyzes the reaction
[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + HO [hydroxymethylglutaryl-CoA reductase (NADPH)] + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphate phosphohydrolase. This enzyme is also called reductase phosphatase.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Inositol-1%2C4-bisphosphate%201-phosphatase | The enzyme inositol-1,4-bisphosphate 1-phosphatase (EC 3.1.3.57) catalyzes the reaction
1D-myo-inositol 1,4-bisphosphate + H2O 1D-myo-inositol 4-phosphate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is D-myo-inositol-1,4-bisphosphate 1-phosphohydrolase. This enzyme is also called inositol-polyphosphate 1-phosphatase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Inositol-phosphate%20phosphatase | The enzyme Inositol phosphate-phosphatase (EC 3.1.3.25) is of the phosphodiesterase family of enzymes. It is involved in the phosphophatidylinositol signaling pathway, which affects a wide array of cell functions, including but not limited to, cell growth, apoptosis, secretion, and information processing. Inhibition of inositol monophosphatase may be key in the action of lithium in treating bipolar disorder, specifically manic depression.
The catalyzed reaction:
myo-inositol phosphate + H2O myo-inositol + phosphate
Nomenclature
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is myo-inositol-phosphate phosphohydrolase. Other names in common use include:
myo-inositol-1(or 4)-monophosphatase,
inositol 1-phosphatase,
L-myo-inositol-1-phosphate phosphatase,
myo-inositol 1-phosphatase,
inositol phosphatase,
inositol monophosphate phosphatase,
inositol-1(or 4)-monophosphatase,
myo-inositol-1(or 4)-phosphate phosphohydrolase,
myo-inositol monophosphatase, and
myo-inositol-1-phosphatase.
Structure
The enzyme is a dimer comprising 277 amino acid residues per subunit. Each dimer exists in 5 layers of alternating α-helices and β-sheets, totaling to 9 α-helices and β-sheets per subunit. IMPase has three hydrophilic hollow active sites, each of which bind water and magnesium molecules. These binding sites appear to be conserved in other phosphodiesterases such as fructose 1,6-bisphosphatase (F |
https://en.wikipedia.org/wiki/Juvenile-hormone%20esterase | The enzyme juvenile hormone esterase (EC 3.1.1.59, systematic name methyl-(2E,6E,10R)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate acylhydrolase, JH esterase) catalyzes the hydrolysis of juvenile hormone:
(1) juvenile hormone I + H2O = juvenile hormone I acid + methanol
(2) juvenile hormone III + H2O = juvenile hormone III acid + methanol
Nomenclature and function
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is methyl-(2E,6E)-(10R,11S)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate acylhydrolase. Other names in common use include JH esterase, juvenile hormone esterase, and juvenile hormone carboxyesterase.
Juvenile hormone (JH) controls insect metamorphosis. High JH titers maintain the larval state while a decrease in the JH titer initiates the pupation sequence as well as a change in tissue commitment away from synthesis of larval tissues to pupal tissues at the pupal stage. The drop in JH titer at the beginning of the last larval instar in the Lepidoptera appears to be due to a combination of increased metabolism and decreased synthesis. In the Lepidoptera, JH is initially metabolized by ester hydrolysis; esterases capable of hydrolyzing JH are detectable in the hemolymph at times during the last larval instar that appear to coincide with reported drops in the JH titre. The JHE's are also selective for the 2E methyl ester of the naturally occurring JH's. These s |
https://en.wikipedia.org/wiki/L-arabinonolactonase | The enzyme L-arabinonolactonase (EC 3.1.1.15) catalyzes the reaction
L-arabinono-1,4-lactone + H2O L-arabinonate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is L-arabinono-1,4-lactone lactonohydrolase. This enzyme participates in ascorbate and aldarate metabolism.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Limonin-D-ring-lactonase | The enzyme limonin-D-ring-lactonase (EC 3.1.1.36) catalyzes the reaction
limonoate D-ring-lactone + H2O limonoate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is limonoate-D-ring-lactone lactonohydrolase. Other names in common use include limonin-D-ring-lactone hydrolase, and limonin lactone hydrolase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lipid-phosphate%20phosphatase | The enzyme lipid-phosphate phosphatase (EC 3.1.3.76) catalyzes the reaction
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H2O (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate phosphohydrolase. Other names in common use include hydroxy fatty acid phosphatase, dihydroxy fatty acid phosphatase, hydroxy lipid phosphatase, sEH (ambiguous), and soluble epoxide hydrolase (ambiguous).
See also
Epoxide hydrolase 2
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/L-rhamnono-1%2C4-lactonase | The enzyme L-rhamnono-1,4-lactonase (EC 3.1.1.65) catalyzes the reaction
L-rhamnono-1,4-lactone + H2O Lrhamnonate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is L-rhamnono-1,4-lactone lactonohydrolase. Other names in common use include Lrhamno-γ-lactonase, L-rhamnono-γ-lactonase, and L-rhamnonate dehydratase. This enzyme participates in fructose and mannose metabolism.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lysophospholipase | The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction
2-lysophosphatidylcholine + H2O glycerophosphocholine + a carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This family consists of lysophospholipase / phospholipase B (EC 3.1.1.5) and cytosolic phospholipase A2 which also has a C2 domain . Phospholipase B enzymes catalyse the release of fatty acids from lysophospholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids, the aligned region corresponds the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.
The systematic name of this enzyme class is 2-lysophosphatidylcholine acylhydrolase. Other names in common use include lecithinase B, lysolecithinase, phospholipase B, lysophosphatidase, lecitholipase, phosphatidase B, lysophosphatidylcholine hydrolase, lysophospholipase A1, lysophopholipase L2, lysophospholipase transacylase, neuropathy target esterase, NTE, NTE-LysoPLA, and NTE-lysophospholipase. This enzyme participates in glycerophospholipid metabolism.
Examples
Human genes encoding proteins that contain this domain include:
PLA2G4A, PLA2G4B, PLA2G4C, PLA2G4D, PLA2G4E, PLA2G4F
See also
Charcot-Leyden crystals
References
Further reading
|
https://en.wikipedia.org/wiki/Mannitol-1-phosphatase | The enzyme mannitol-1-phosphatase (EC 3.1.3.22) catalyzes the reaction
D-mannitol 1-phosphate + H2O D-mannitol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is D-mannitol-1-phosphate phosphohydrolase. This enzyme is also called mannitol-1-phosphate phosphatase. This enzyme participates in fructose and mannose metabolism.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mannosyl-3-phosphoglycerate%20phosphatase | The enzyme mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70) catalyzes the reaction
2-O-(α-D-mannosyl)-3-phosphoglycerate + H2O = 2-O-(α-D-mannosyl)-D-glycerate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 2-O-(α-D-mannosyl)-3-phosphoglycerate phosphohydrolase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Methylphosphothioglycerate%20phosphatase | The enzyme methylphosphothioglycerate phosphatase (EC 3.1.3.14) catalyzes the reaction
S-methyl-3-phospho-1-thio-D-glycerate + H2O S-methyl-1-thio-D-glycerate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is S-methyl-3-phospho-1-thio-D-glycerate phosphohydrolase. This enzyme is also called methylthiophosphoglycerate phosphatase.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methylumbelliferyl-acetate%20deacetylase | The enzyme methylumbelliferyl-acetate deacetylase (EC 3.1.1.56, esterase D) catalyzes the reaction
4-methylumbelliferyl acetate + H2O 4-methylumbelliferone + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 4-methylumbelliferyl-acetate acylhydrolase. This enzyme is also called esterase D.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Monomethyl-sulfatase | The enzyme monomethyl-sulfatase (EC 3.1.6.16) catalyzes the reaction
monomethyl sulfate + H2O methanol + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name is monomethyl-sulfate sulfohydrolase.
References
EC 3.1.6
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Monoterpenyl-diphosphatase | The enzyme monoterpenyl-diphosphatase (EC 3.1.7.3) catalyzes the reaction
a monoterpenyl diphosphate + H2O a monoterpenol + diphosphate
This enzyme belongs to the family of hydrolases, specifically those acting on diphosphoric monoester bonds. The systematic name is monoterpenyl-diphosphate diphosphohydrolase. Other names in common use include bornyl pyrophosphate hydrolase and monoterpenyl-pyrophosphatase.
References
EC 3.1.7
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Multiple%20inositol-polyphosphate%20phosphatase | The enzyme multiple inositol-polyphosphate phosphatase (EC 3.1.3.62) catalyzes the reaction
myo-inositol hexakisphosphate + H2O myo-inositol pentakisphosphate (mixed isomers) + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 1D-myo-inositol-hexakisphosphate 5-phosphohydrolase. Other names in common use include inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase, inositol 1,3,4,5-tetrakisphosphate 3-phosphomonoesterase, inositol 1,3,4,5-tetrakisphosphate-5-phosphomonoesterase, inositol tetrakisphosphate phosphomonoesterase, inositol-1,3,4,5-tetrakisphosphate 3-phosphatase, and MIPP. This enzyme participates in inositol phosphate metabolism.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Myosin-light-chain%20phosphatase | Myosin light-chain phosphatase, also called myosin phosphatase (EC 3.1.3.53; systematic name [myosin-light-chain]-phosphate phosphohydrolase), is an enzyme (specifically a serine/threonine-specific protein phosphatase) that dephosphorylates the regulatory light chain of myosin II:
[myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate
This dephosphorylation reaction occurs in smooth muscle tissue and initiates the relaxation process of the muscle cells. Thus, myosin phosphatase undoes the muscle contraction process initiated by myosin light-chain kinase. The enzyme is composed of three subunits: the catalytic region (protein phosphatase 1, or PP1), the myosin binding subunit (MYPT1), and a third subunit (M20) of unknown function. The catalytic region uses two manganese ions as catalysts to dephosphorylate the light-chains on myosin, which causes a conformational change in the myosin and relaxes the muscle. The enzyme is highly conserved and is found in all organisms’ smooth muscle tissue. While it is known that myosin phosphatase is regulated by rho-associated protein kinases, there is current debate about whether other molecules, such as arachidonic acid and cAMP, also regulate the enzyme.
Function
Smooth muscle tissue is mostly made of actin and myosin, two proteins that interact together to produce muscle contraction and relaxation. Myosin II, also known as conventional myosin, has two heavy chains that consist of the head and tail domains and f |
https://en.wikipedia.org/wiki/N-acetylgalactosaminoglycan%20deacetylase | The enzyme N-acetylgalactosaminoglycan deacetylase (EC 3.1.1.58) catalyzes the reaction
N-acetyl-D-galactosaminoglycan + H2O D-galactosaminoglycan + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is ''N-acetyl-D-galactosaminoglycan acetylhydrolase. Other names in common use include polysaccharide deacetylase, Vi-polysaccharide deacetylase, and N''-acetyl galactosaminoglycan deacetylase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetylglucosamine-1-phosphodiester%20alpha-N-acetylglucosaminidase | The enzyme N-acetylglucosamine-1-phosphodiester α-N-acetylglucosaminidase (EC 3.1.4.45) catalyzes the reaction
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is glycoprotein-N-acetyl-D-glucosaminyl-phospho-D-mannose N-acetyl-D-glucosaminylphosphohydrolase. Other names in common use include α-N-acetylglucosaminyl phosphodiesterase, lysosomal α-N-acetylglucosaminidase, phosphodiester glycosidase, α-N-acetyl-D-glucosamine-1-phosphodiester, ''N''-acetylglucosaminidase, 2-acetamido-2-deoxy-α-D-glucose 1-phosphodiester, and acetamidodeoxyglucohydrolase.
References
EC 3.1.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acylneuraminate-9-phosphatase | The enzyme N-acylneuraminate-9-phosphatase (EC 3.1.3.29) catalyzes the reaction
N-acylneuraminate 9-phosphate + H2O N-acylneuraminate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is ''N-acylneuraminate-9-phosphate phosphohydrolase. Other names in common use include acylneuraminate 9-phosphatase, N-acylneuraminic acid 9-phosphate phosphatase, and N''-acylneuraminic (sialic) acid 9-phosphatase. This enzyme participates in aminosugars metabolism.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dynactin | Dynactin is a 23 subunit protein complex that acts as a co-factor for the microtubule motor cytoplasmic dynein-1. It is built around a short filament of actin related protein-1 (Arp1).
Discovery
Dynactin was identified as an activity that allowed purified cytoplasmic dynein to move membrane vesicles along microtubules in vitro. It was shown to be a multiprotein complex and named "dynactin" because of its role in dynein activation.
The main features of dynactin were visualized by quick-freeze, deep-etch, rotary shadow electron microscopy. It appears as a short filament, 37-nm in length, which resembles F-actin, plus a thinner, laterally oriented arm. Antibody labelling was used to map the location of the dynactin subunits.
Structure
Dynactin consists of three major structural domains: (1) sidearm-shoulder: DCTN1/p150Glued, DCTN2/p50/dynamitin, DCTN3/p24/p22;(2)the Arp1 filament: ACTR1A/Arp1/centractin, actin, CapZ; and (3) the pointed end complex: Actr10/Arp11, DCTN4/p62, DCTN5/p25, and DCTN6/p27.
A 4Å cryo-EM structure of dynactin revealed that its filament contains eight Arp1 molecules, one β-actin and one Arp11. In the pointed end complex p62/DCTN4 binds to Arp11 and β-actin and p25 and p27 bind both p62 and Arp11. At the barbed end the capping protein (CapZαβ) binds the Arp1 filament in the same way that it binds actin, although with more charge complementarity, explaining why it binds dynactin more tightly than actin.
The shoulder contains two copies of p150Glu |
https://en.wikipedia.org/wiki/Oleoyl-%28acyl-carrier-protein%29%20hydrolase | The enzyme oleoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14) catalyzes the reaction
an oleoyl-[acyl-carrier-protein] + H2O an [acyl-carrier-protein] + oleate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is oleoyl-[acyl-carrier-protein] hydrolase. Other names in common use include acyl-[acyl-carrier-protein] hydrolase, acyl-ACP-hydrolase, acyl-acyl carrier protein hydrolase, oleoyl-ACP thioesterase, and oleoyl-acyl carrier protein thioesterase. This enzyme participates in fatty acid biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.1.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Palmitoyl-CoA%20hydrolase | Palmitoyl-CoA hydrolase (EC 3.1.2.2) is an enzyme in the family of hydrolases that specifically acts on thioester bonds. It catalyzes the hydrolysis of long chain fatty acyl thioesters of acyl carrier protein or coenzyme A to form free fatty acid and the corresponding thiol:
palmitoyl-CoA + H2O = CoA + palmitate
It has a strict specificity for thioesters with a chain link greater than C10.
These enzymes are localized in almost all cellular compartments, such as endoplasmic reticulum, cytosol, mitochondria, and peroxisomes. They are highly regulated by peroxisome proliferator activated receptors, which led to their involvement in lipid metabolism. The enzyme is up-regulated during times of increased fatty acid oxidation, which suggests that this enzyme has a potential role the peroxisomal beta-oxidation.
The systematic name is palmitoyl-CoA hydrolase. Other names in common use include long-chain fatty-acyl-CoA hydrolase, palmitoyl coenzyme A hydrolase, palmitoyl thioesterase, palmitoyl coenzyme A hydrolase, palmitoyl-CoA deacylase, palmityl thioesterase, palmityl-CoA deacylase, fatty acyl thioesterase I, and palmityl thioesterase I.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
Mechanism
At a subcellular level, palmitoyl-CoA hydrolase is localized in the endoplasmic reticulum, cytosol, mitochondria, and peroxisomes. Studies have shown that in rats that are fed high fat diets, palmitoyl- |
https://en.wikipedia.org/wiki/Palmitoyl%28protein%29%20hydrolase | Palmitoyl protein hydrolase/thioesterases is an enzyme (EC 3.1.2.22) that removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. It catalyzes the reaction
palmitoyl[protein] + H2O palmitate + protein
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is palmitoyl[protein] hydrolase. Other names in common use include palmitoyl-protein thioesterase, and palmitoyl-(protein) hydrolase. This enzyme participates in fatty acid elongation in mitochondria.
Neuronal ceroid lipofuscinoses (NCL) represent a group of encephalopathies that occur in 1 in 12,500 children. Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis. The most common mutation results in intracellular accumulation of the polypeptide and undetectable enzyme activity in the brain. Direct sequencing of cDNAs derived from brain RNA of INCL patients has shown a mis-sense transversion of A to T at nucleotide position 364, which results in substitution of Trp for Arg at position 122 in the protein - Arg 122 is immediately adjacent to a lipase consensus sequence that contains the putative active site Ser of PPT. The occurrence of this and two other independent mutations in the PPT gene strongly suggests that defects in this gene cause INCL.
Examples
Human proteins containing this domain include:
Structural studies
|
https://en.wikipedia.org/wiki/Orsellinate-depside%20hydrolase | The enzyme orsellinate-depside hydrolase (EC 3.1.1.40) catalyzes the reaction
orsellinate depside + H2O 2 orsellinate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is orsellinate-depside hydrolase. This enzyme is also called lecanorate hydrolase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phenylacetyl-CoA%20hydrolase | The enzyme phenylacetyl-CoA hydrolase (EC 3.1.2.25) catalyzes the reaction
phenylglyoxylyl-CoA + H2O phenylglyoxylate + CoA
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is phenylglyoxylyl-CoA hydrolase.
References
EC 3.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phorbol-diester%20hydrolase | The enzyme phorbol-diester hydrolase (EC 3.1.1.51) catalyzes the reaction
phorbol 12,13-dibutanoate + H2O phorbol 13-butanoate + butanoate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 12,13-diacylphorbate 12-acylhydrolase. Other names in common use include diacylphorbate 12-hydrolase, diacylphorbate 12-hydrolase, phorbol-12,13-diester 12-ester hydrolase, and PDEH.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidate%20phosphatase | The enzyme phosphatidate phosphatase (PAP, EC 3.1.3.4) is a key regulatory enzyme in lipid metabolism, catalyzing the conversion of phosphatidate to diacylglycerol:
a 1,2-diacylglycerol 3-phosphate + H2O a 1,2-diacyl-sn-glycerol + phosphate
The reverse conversion is catalyzed by the enzyme diacylglycerol kinase, which replaces the hydroxyl group on diacylgylcerol with a phosphate from ATP, generating ADP in the process.
In yeast, the forward direction is Mg2+-dependent, while the reverse process is Ca2+-dependent. PAP1, a cytosolic phosphatidate phosphatase found in the lung, is also Mg^2+-dependent, but PAP2, a six-transmembrane-domain integral protein found in the plasma membrane, is not.
Role in the regulation of lipid flux
Phosphatidate phosphatase regulates lipid metabolism in several ways. In short, it is a key player in controlling the overall flux of triacylglycerols to phospholipids and vice versa, also exerting control through the generation and degradation of lipid-signaling molecules related to phosphatidate. When the phosphatase is active, diacylglycerols formed by it can go on to form any of several products, including phosphatidylethanolamine, phosphatidylcholine, phosphatidylserine, and triacylglycerol. Phospholipids can be formed from diacylglycerol through reaction with activated alcohols, and triacylglycerols can be formed from diacylglycerols through reaction with fatty acyl CoA molecules. When phosphatidate phosphatase is inactive, diacylglycerol k |
https://en.wikipedia.org/wiki/Glucuronate-2-sulfatase | In enzymology, a glucuronate-2-sulfatase () is an enzyme that catalyzes the chemical reaction of cleaving off the 2-sulfate groups of the 2-O-sulfo-D-glucuronate residues of chondroitin sulfate, heparin and heparitin sulfate.
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is polysaccharide-2-O-sulfo-D-glucuronate 2-sulfohydrolase. This enzyme is also called glucurono-2-sulfatase. This enzyme participates in glycosaminoglycan degradation and glycan structures - degradation.
References
EC 3.1.6
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylglycerophosphatase | The enzyme phosphatidylglycerophosphatase (EC 3.1.3.27) catalyzes the following reaction:
phosphatidylglycerophosphate + H2O phosphatidylglycerol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is phosphatidylglycerophosphate phosphohydrolase. Other names in common use include phosphatidylglycerol phosphate phosphatase, phosphatidylglycerol phosphatase, and PGP phosphatase. It participates in glycerophospholipid metabolism.
This is a family of proteins that acts as a mitochondrial phosphatase in cardiolipin biosynthesis. Cardiolipin is a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylinositol-3%2C4%2C5-trisphosphate%203-phosphatase | The enzyme phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase (EC 3.1.3.67) catalyzes the chemical reaction
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O = 1-phosphatidyl-1D-myoinositol 4,5-bisphosphate + phosphate
This enzyme class belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 1-phosphatidyl-D-myoinositol-3,4,5-trisphosphate 3-phosphohydrolase. Other names in common use include PTEN, MMAC1, and phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase. PTEN also refers to a member of the class, phosphatase and tensin homolog. This enzyme participates in 10 metabolic pathways: inositol phosphate metabolism, phosphatidylinositol signaling system, p53 signaling pathway, focal adhesion, tight junction, endometrial cancer, glioma, prostate cancer, melanoma, and small cell lung cancer. It employs one cofactor, magnesium.
References
EC 3.1.3
Magnesium enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylinositol-3%2C4-bisphosphate%204-phosphatase | The enzyme phosphatidylinositol-3,4-bisphosphate 4-phosphatase (EC 3.1.3.66) that catalyzes the reaction
1-phosphatidyl-myo-inositol 3,4-bisphosphate + H2O 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 1-phosphatidyl-1D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase. Other names in common use include inositol-3,4-bisphosphate 4-phosphatase, D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase, phosphoinositide 4-phosphatase, inositol polyphosphate 4-phosphatase, D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase, and inositol polyphosphate 4-phosphatase type II. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylinositol-3-phosphatase | The enzyme phosphatidylinositol-3-phosphatase (EC 3.1.3.64) catalyzes the reaction
1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O 1-phosphatidyl-1D-myo-inositol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 1-phosphatidyl-1D-myo-inositol-3-phosphate 3-phosphohydrolase. Other names in common use include inositol-1,3-bisphosphate 3-phosphatase, inositol 1,3-bisphosphate phosphatase, inositol-polyphosphate 3-phosphatase, D-myo-inositol-1,3-bisphosphate 3-phosphohydrolase, and phosphatidyl-3-phosphate 3-phosphohydrolase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Cellulose-polysulfatase | The enzyme cellulose-polysulfatase (EC 3.1.6.7) catalyzes hydrolysis of the 2- and 3-sulfate groups of the polysulfates of cellulose and charonin.
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is cellulose-sulfate sulfohydrolase.
References
EC 3.1.6
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphatidylinositol%20deacylase | The enzyme phosphatidylinositol deacylase (EC 3.1.1.52) catalyzes the reaction
1-phosphatidyl-D-myo-inositol + H2O 1-acylglycerophosphoinositol + a carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 1-phosphatidyl-D-myo-inositol 2-acylhydrolase. Other names in common use include phosphatidylinositol phospholipase A2, and phospholipase A2.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoenolpyruvate%20phosphatase | The enzyme phosphoenol pyruvate phosphatase (EC 3.1.3.60) catalyzes the reaction
phosphoenolpyruvate + H2O pyruvate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is phosphoenolpyruvate phosphohydrolase. This enzyme is also called PEP phosphatase.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoglycerate%20phosphatase | The enzyme phosphoglycerate phosphatase (EC 3.1.3.20) catalyzes the reaction
D-glycerate 2-phosphate + H2O D-glycerate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is D-glycerate-2-phosphate phosphohydrolase. Other names in common use include D-2-phosphoglycerate phosphatase, and glycerophosphate phosphatase.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoinositide%205-phosphatase | The enzyme phosphoinositide 5-phosphatase (EC 3.1.3.36) catalyzes the reaction
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is phosphatidyl-myo-inositol-4,5-bisphosphate 4-phosphohydrolase. Other names in common use include type II inositol polyphosphate 5-phosphatase, triphosphoinositide phosphatase, IP3 phosphatase, PtdIns(4,5)P2 phosphatase, triphosphoinositide phosphomonoesterase, diphosphoinositide phosphatase, inositol 1,4,5-triphosphate 5-phosphomonoesterase, inositol triphosphate 5-phosphomonoesterase, phosphatidylinositol-bisphosphatase, phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase, phosphatidylinositol 4,5-bisphosphate phosphatase, polyphosphoinositol lipid 5-phosphatase, and phosphatidyl-inositol-bisphosphate phosphatase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
Cockcroft, S. (Ed.), Biology of Phosphoinositides, Biology of Phosphoinositides, Oxford, 2000, p. 320-338.
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28phosphorylase%29%20phosphatase | The enzyme phosphorylase a phosphatase (EC 3.1.3.17) catalyzes the reaction
[phosphorylase a] + 4 HO 2 [phosphorylase b] + 4 phosphate
It is synonymous with Protein phosphatase 1. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is [phosphorylase a] phosphohydrolase. Other names in common use include PR-enzyme, phosphorylase a phosphatase, glycogen phosphorylase phosphatase, protein phosphatase C, and type 1 protein phosphatase.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoserine%20phosphatase | The enzyme phosphoserine phosphatase (EC 3.1.3.3) catalyzes the reaction
O-phospho-L(or D)-serine + H2O L(or D)-serine + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is O-phosphoserine phosphohydrolase. This enzyme participates in glycine, serine and threonine metabolism.
Structural studies
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , and .
References
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 73-78.
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acetylgalactosamine-6-sulfatase | The enzyme N-acetylgalactosamine-6-sulfatase (EC 3.1.6.4) catalyzes the chemical reaction of cleaving off the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of the macromolecule chondroitin sulfate and, similarly, of the D-galactose 6-sulfate units of the macromolecule keratan sulfate.
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is ''N-acetyl-D-galactosamine-6-sulfate 6-sulfohydrolase. Other names in common use include chondroitin sulfatase, chondroitinase, galactose-6-sulfate sulfatase, acetylgalactosamine 6-sulfatase, N-acetylgalactosamine-6-sulfate sulfatase, and N''-acetylgalactosamine 6-sulfatase. This enzyme participates in glycosaminoglycan degradation and degradation of glycan structures.
Deficiency
Morquio syndrome is a rare birth defect caused by a deficiency in this essential enzyme. Treatment options include enzyme replacement therapy with a synthetic version of the enzyme called elosulfase alfa.
References
EC 3.1.6
Enzymes of unknown structure |
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