Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
| dihydrolipoyllysine-residue (2-methylpropanoyl)transferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.168 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a dihydrolipoyllysine-residue (2-methylpropanoyl)transferase (EC 2.3.1.168) is an enzyme that catalyzes the chemical reaction
- 2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
Thus, the two substrates of this enzyme are 2-methylpropanoyl-CoA and enzyme N6-(dihydrolipoyl)lysine, whereas its two products are CoA and [[enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine]].
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 2-methylpropanoyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-(2-methylpropanoyl)transferase. Other names in common use include dihydrolipoyl transacylase, enzyme-dihydrolipoyllysine:2-methylpropanoyl-CoA, S-(2-methylpropanoyl)transferase, 2-methylpropanoyl-CoA:enzyme-6-N-(dihydrolipoyl)lysine, and S-(2-methylpropanoyl)transferase. This enzyme participates in valine, leucine and isoleucine degradation.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1ZWV, 2COO, 2IHW, 2II3, 2II4, and 2II5.
References
- Massey LK, Sokatch JR, Conrad RS (1976). "Branched-chain amino acid catabolism in bacteria". Bacteriol. Rev. 40 (1): 42–54. PMC 413937. PMID 773366.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Chuang DT, Hu CC, Ku LS, Niu WL, Myers DE, Cox RP (1984). "Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain alpha-keto acid dehydrogenase". J. Biol. Chem. 259 (14): 9277–84. PMID 6746648.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Wynn RM, Davie JR, Zhi W, Cox RP, Chuang DT (1994). "In vitro reconstitution of the 24-meric E2 inner core of bovine mitochondrial branched-chain alpha-keto acid dehydrogenase complex: requirement for chaperonins GroEL and GroES". Biochemistry. 33 (30): 8962–8. doi:10.1021/bi00196a014. PMID 7913832.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions". Annu. Rev. Biochem. 69: 961–1004. doi:10.1146/annurev.biochem.69.1.961. PMID 10966480.