Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Rattus norvegicus | 5739 | - |
peroxisome | - |
Rattus norvegicus | 5777 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
crotonyl-CoA + H2O | Rattus norvegicus | - |
(3S)-hydroxybutyryl-CoA | - |
r | |
crotonyl-CoA + H2O | Streptomyces sp. V-1 | - |
(3S)-hydroxybutyryl-CoA | - |
r | |
feruloyl-CoA + H2O | Streptomyces sp. V-1 | formation of the precursor of vanillin | 3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA | - |
r | |
methacrylyl-CoA + H2O | Rattus norvegicus | - |
3-hydroxy-2-methylpropanoyl-CoA | - |
r | |
methacrylyl-CoA + H2O | Streptomyces sp. V-1 | - |
3-hydroxy-2-methylpropanoyl-CoA | - |
r | |
methacrylyl-CoA + H2O | Rattus norvegicus | - |
? | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | P07896 | - |
- |
Rattus norvegicus | P14604 | - |
- |
Streptomyces sp. V-1 | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O | the CoA moiety of the substrate adopts the typical horseshoe conformation in a binding pocket formed from two adjacent monomers, while the active site catalytic residues are provided by a single monomer. The active site of rat liver mitochondrial ECH contains an oxyanion hole formed from the backbone amides of Gly141 and Ala98, which serves to polarize the carbonyl group of the alpha,beta-unsaturated enoyl-CoA substrate and stabilize the enolate intermediate. Two active site glutamate residues (Glu144 and Glu164) are proposed to act as a general base(s) for the conjugate addition of water onto the substrate enone and to protonate the resultant enolate | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
crotonyl-CoA + H2O | - |
Rattus norvegicus | (3S)-hydroxybutyryl-CoA | - |
r | |
crotonyl-CoA + H2O | - |
Streptomyces sp. V-1 | (3S)-hydroxybutyryl-CoA | - |
r | |
feruloyl-CoA + H2O | formation of the precursor of vanillin | Streptomyces sp. V-1 | 3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA | - |
r | |
methacrylyl-CoA + H2O | - |
Rattus norvegicus | 3-hydroxy-2-methylpropanoyl-CoA | - |
r | |
methacrylyl-CoA + H2O | - |
Streptomyces sp. V-1 | 3-hydroxy-2-methylpropanoyl-CoA | - |
r | |
methacrylyl-CoA + H2O | - |
Rattus norvegicus | ? | - |
r | |
additional information | enzyme ECH displays activity toward unsaturated CoA thioesters with different chain lengths, although the turnover rate decreases for longer substrates | Rattus norvegicus | ? | - |
? | |
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 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homohexamer | the ECH structure adopts a functional hexamer comprising two stacked trimers | Rattus norvegicus |
homohexamer | the ECH structure adopts a functional hexamer comprising two stacked trimers | Streptomyces sp. V-1 |
Synonyms | Comment | Organism |
---|---|---|
crotonase | - |
Rattus norvegicus |
crotonase | - |
Streptomyces sp. V-1 |
ECH | - |
Rattus norvegicus |
ECH | - |
Streptomyces sp. V-1 |
ECH-1 | - |
Rattus norvegicus |
enoyl-CoA hydratase 1 | UniProt | Rattus norvegicus |
PBE | - |
Rattus norvegicus |
PBFE | - |
Rattus norvegicus |
peroxisomal bifunctional enzyme | UniProt | Rattus norvegicus |
peroxisomal multifunctional enzyme, type 1 | - |
Rattus norvegicus |
SCEH | - |
Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
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 |