In enzymology, a vinylacetyl-CoA Delta-isomerase (EC 5.3.3.3) is an enzyme that catalyzes the chemical reaction
| Vinylacetyl-CoA Δ-isomerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.3.3.3 | ||||||||
| CAS no. | 9023-73-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- vinylacetyl-CoA crotonyl-CoA
Hence, this enzyme has one substrate, vinylacetyl-CoA, and one product, crotonyl-CoA.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases transposing C=C bonds. The systematic name of this enzyme class is vinylacetyl-CoA Delta3-Delta2-isomerase. Other names in common use include vinylacetyl coenzyme A Delta-isomerase, vinylacetyl coenzyme A isomerase, and Delta3-cis-Delta2-trans-enoyl-CoA isomerase. This enzyme participates in butanoate metabolism.
Structural studies
editAs of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1U8V.
References
edit- Lynen F, Knappe J, Lorch E, Jutting G, Ringelmann E (1959). "Die biochemische Funktion des Biotins". Angew. Chem. 71 (15–16): 481–486. doi:10.1002/ange.19590711503.
- Rilling HC; Coon MJ (1960). "The enzymatic isomerization of beta-methylvinylacetyl coenzyme A and the specificity of a bacterial beta-methylcrotonyl coenzyme A carboxylase". J. Biol. Chem. 235 (11): 3087–3092. doi:10.1016/S0021-9258(20)81314-3.
