Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Park, S.J.; Lee, S.Y.
    Identification and characterization of a new enoyl coenzyme A hydratase involved in biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli (2003), J. Bacteriol., 185, 5391-5397.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.119
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.119 additional information Escherichia coli MaoC is an enoyl-CoA hydratase which is involved in converting enoyl-CoAs to (R)-3-hydroxyacyl coenzyme A in fadB mutant Escherichia coli. Metabolic link between fatty acid metabolism and polyhydroxyalkanoate biosynthesis ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.3.2.12 Escherichia coli
-
-
-
4.2.1.119 Escherichia coli
-
 The classification is ambiguous because the stereochemistry of the reaction product is not exactly determined
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.3.2.12 additional information enzyme additionally shows enoyl-CoA hydratase activity involved in supplying (R)-3-hydroxyacyl-CoA from the beta-oxidation pathway to polyhydroxyalkanoate biosynthetic pathway in the fadB mutant Escherichia coli strain Escherichia coli ?
-
 ?
4.2.1.119 crotonyl-CoA + H2O the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined Escherichia coli ?
-
 ?
4.2.1.119 additional information MaoC is an enoyl-CoA hydratase which is involved in converting enoyl-CoAs to (R)-3-hydroxyacyl coenzyme A in fadB mutant Escherichia coli. Metabolic link between fatty acid metabolism and polyhydroxyalkanoate biosynthesis Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.3.2.12 MaoC
-
 Escherichia coli
4.2.1.119 MaoC
-
 Escherichia coli
4.2.1.119 MaoC the classification is ambiguous because the stereochemistry of the reaction product is not exactly determined Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.119 8
-
 assay at Escherichia coli

General Information

EC Number General Information Comment Organism
3.3.2.12 physiological function a fadB maoC double-mutant strain, lacking fatty acid oxidation complex protein FadB and the enzyme, accumulates 43% less amount of medium-chain-length polyhydroxyalkanoates from fatty acid compared with the fadB mutant Escherichia coli