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Literature summary extracted from

  • Lohans, C.; Wang, D.; Wang, J.; Hamed, R.; Schofield, C.
    Crotonases natures exceedingly convertible catalysts (2017), ACS Catal., 7, 6587-6599 .
No PubMed abstract available

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.1.17 mitochondrion
-
Rattus norvegicus
-
-
4.2.1.17 peroxisome
-
Rattus norvegicus
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.17 crotonyl-CoA + H2O Rattus norvegicus
-
(3S)-hydroxybutyryl-CoA
-
r
4.2.1.17 crotonyl-CoA + H2O Streptomyces sp. V-1
-
(3S)-hydroxybutyryl-CoA
-
r
4.2.1.17 feruloyl-CoA + H2O Streptomyces sp. V-1 formation of the precursor of vanillin 3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
-
r
4.2.1.17 methacrylyl-CoA + H2O Rattus norvegicus
-
3-hydroxy-2-methylpropanoyl-CoA
-
r
4.2.1.17 methacrylyl-CoA + H2O Streptomyces sp. V-1
-
3-hydroxy-2-methylpropanoyl-CoA
-
r
4.2.1.17 methacrylyl-CoA + H2O Rattus norvegicus
-
?
-
r

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.17 Streptomyces sp. V-1
-
-
-
4.2.1.17 Rattus norvegicus P07896
-
-
4.2.1.17 Rattus norvegicus P14604
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.1.17 liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.17 additional information enzyme ECH displays activity toward unsaturated CoA thioesters with different chain lengths, although the turnover rate decreases for longer substrates Rattus norvegicus ?
-
?
4.2.1.17 additional information enzyme ECH displays activity toward unsaturated CoA thioesters with different chain lengths, although the turnover rate decreases for longer substrates Streptomyces sp. V-1 ?
-
?
4.2.1.17 crotonyl-CoA + H2O
-
Rattus norvegicus (3S)-hydroxybutyryl-CoA
-
r
4.2.1.17 crotonyl-CoA + H2O
-
Streptomyces sp. V-1 (3S)-hydroxybutyryl-CoA
-
r
4.2.1.17 feruloyl-CoA + H2O formation of the precursor of vanillin Streptomyces sp. V-1 3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
-
r
4.2.1.17 methacrylyl-CoA + H2O
-
Rattus norvegicus 3-hydroxy-2-methylpropanoyl-CoA
-
r
4.2.1.17 methacrylyl-CoA + H2O
-
Streptomyces sp. V-1 3-hydroxy-2-methylpropanoyl-CoA
-
r
4.2.1.17 methacrylyl-CoA + H2O
-
Rattus norvegicus ?
-
r

Subunits

EC Number Subunits Comment Organism
4.2.1.17 homohexamer the ECH structure adopts a functional hexamer comprising two stacked trimers Rattus norvegicus
4.2.1.17 homohexamer the ECH structure adopts a functional hexamer comprising two stacked trimers Streptomyces sp. V-1

Synonyms

EC Number Synonyms Comment Organism
4.2.1.17 crotonase
-
Rattus norvegicus
4.2.1.17 crotonase
-
Streptomyces sp. V-1
4.2.1.17 ECH
-
Rattus norvegicus
4.2.1.17 ECH
-
Streptomyces sp. V-1
4.2.1.17 SCEH
-
Rattus norvegicus
4.2.1.17 enoyl-CoA hydratase 1 UniProt Rattus norvegicus
4.2.1.17 ECH-1
-
Rattus norvegicus
4.2.1.17 peroxisomal multifunctional enzyme, type 1
-
Rattus norvegicus
4.2.1.17 peroxisomal bifunctional enzyme UniProt Rattus norvegicus
4.2.1.17 PBE
-
Rattus norvegicus
4.2.1.17 PBFE
-
Rattus norvegicus

General Information

EC Number General Information Comment Organism
4.2.1.17 physiological function prototypical crotonase enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are crucially involved in the beta-oxidation pathway of fatty acid metabolism. Enzyme ECH catalyzes the second step of the beta-oxidation pathway: i.e. the syn addition of a water molecule across the double bond of an alpha,beta-unsaturated enoyl-CoA thioester substrate, e.g. crotonyl or methacrylyl-CoA Rattus norvegicus
4.2.1.17 physiological function prototypical crotonase enoyl-CoA hydratase (ECH) is crucially involved in the beta-oxidation pathway of fatty acid metabolism. Enzyme ECH catalyzes the second step of the beta-oxidation pathway: i.e. the syn addition of a water molecule across the double bond of an alpha,beta-unsaturated enoyl-CoA thioester substrate, e.g. crotonyl or methacrylyl-CoA. Rat mitochondrial ECH-1 (which has the two glutamate residues typical of ECH) has isomerase activity, albeit much lower than its hydratase activity Rattus norvegicus
4.2.1.17 physiological function prototypical crotonase enoyl-CoA hydratase (ECH) is crucially involved in the beta-oxidation pathway of fatty acid metabolism. Enzyme ECH catalyzes the second step of the beta-oxidation pathway: i.e. the syn addition of a water molecule across the double bond of an alpha,beta-unsaturated enoyl-CoA thioester substrate, e.g. crotonyl or methacrylyl-CoA. The enzyme is also involved in the formation of vanillin, combined with aldolase activity Streptomyces sp. V-1
4.2.1.17 malfunction while mutation of Glu144 to alanine in this enzyme diminishes the isomerase activity by 10fold, mutation of Glu164 to alanine decreases the isomerase activity 1000fold, the hydratase activity is decreased 2000fold for both mutants Rattus norvegicus
4.2.1.17 metabolism the prototypical crotonases enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are crucially involved in the beta-oxidation pathway of fatty acid metabolism Rattus norvegicus
4.2.1.17 metabolism the prototypical crotonases enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are crucially involved in the beta-oxidation pathway of fatty acid metabolism Streptomyces sp. V-1
4.2.1.17 evolution the crotonases comprise a widely distributed enzyme superfamily that has multiple roles in both primary and secondary metabolism. Enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are prototypical crotonases. The term crotonase has been used to refer specifically to ECH, but it is also used to refer to the entirety of the superfamily of enzymes bearing the crotonase-type fold Streptomyces sp. V-1
4.2.1.17 evolution the crotonases comprise a widely distributed enzyme superfamily that has multiple roles in both primary and secondary metabolism. Enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are prototypical crotonases. The term crotonase has been used to refer specifically to ECH, but it is also used to refer to the entirety of the superfamily of enzymes bearing the crotonase-type fold. Some enzymes (e.g. rat peroxisomal multifunctional enzyme, type 1) have both ECH and ECI activities. These enzymes employ an active site with two glutamate residues. Rat mitochondrial ECH-1 (which has the two glutamate residues typical of ECH) has isomerase activity, albeit much lower than its hydratase activity. While the hydratase activity depends on both glutamate residues, the isomerase activity (as with dedicated ECI enzymes) relies mostly on a single glutamate Rattus norvegicus
4.2.1.17 evolution the crotonases comprise a widely distributed enzyme superfamily that has multiple roles in both primary and secondary metabolism. Enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are prototypical crotonases. The term crotonase has been used to refer specifically to ECH, but it is also used to refer to the entirety of the superfamily of enzymes bearing the crotonase-type fold. Some enzymes, e.g. rat peroxisomal multifunctional enzyme, type 1, have both ECH and ECI activities. These enzymes employ an active site with two glutamate residues. Through the use of an additional domain, some multifunctional crotonase enzymes can also catalyze a further step in fatty acid catabolism, i.e. the oxidation of the enoyl-CoA hydratase product. While the hydratase activity depends on both glutamate residues, the isomerase activity (as with dedicated ECI enzymes) relies mostly on a single glutamate Rattus norvegicus