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Literature summary extracted from

  • Zhang, Y.; Yang, X.; Yu, H.; Ma, G.
    Theoretical insight into the catalytic mechanism of enoyl-CoA hydratase (2017), Acta Chim. Sin., 75, 494-500 .
No PubMed abstract available

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.1.17 mitochondrion
-
 Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.17 4-(N,N-dimethylamino)cinnamoyl-CoA + H2O Homo sapiens
-
 ?
-
 ?
4.2.1.17 crotonyl-CoA + H2O Homo sapiens
-
 3-hydroxybutyryl-CoA
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.17 Homo sapiens P30084
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.17 (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O reaction mechansim of enoyl-CoA hydration, overview Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.17 4-(N,N-dimethylamino)cinnamoyl-CoA + H2O
-
 Homo sapiens ?
-
 ?
4.2.1.17 4-(N,N-dimethylamino)cinnamoyl-CoA + H2O
-
 Homo sapiens ?
-
 r
4.2.1.17 crotonyl-CoA + H2O
-
 Homo sapiens 3-hydroxybutyryl-CoA
-
 r
4.2.1.17 crotonyl-CoA + H2O preferred substrate Homo sapiens 3-hydroxybutyryl-CoA
-
 r

Synonyms

EC Number Synonyms Comment Organism
4.2.1.17 ECH
-
 Homo sapiens
4.2.1.17 enoyl-CoA hydratase
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
4.2.1.17 additional information molecular mechanism analysis by density functional theory methods, overview. Residue Glu164 functions as the acid/base in catalysis. And although Glu144 is not directly involved in hydration, it induces the catalytic water molecule to locate in ideal orientation to attack the double bond of substrate by hydrogen-bonding interaction. The backbone NH groups of Ala98 and Gly141 form an oxyanion whole with substrate carbonyl oxygen, playing a key role in substrate binding and stabilization of generated transition states and intermediates Homo sapiens
4.2.1.17 physiological function the enzyme is the second requisite enzyme in the beta-oxidation pathway of fatty acids that catalyzes the syn hydration of alpha,beta-unsaturated thiolester substrates Homo sapiens