Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase

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dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
2ii5.jpg
Identifiers
EC number2.3.1.168
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / 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[edit]

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[edit]

  • Massey LK, Sokatch JR, Conrad RS (1976). "Branched-chain amino acid catabolism in bacteria". Bacteriol. Rev. 40 (1): 42&ndash, 54. PMC 413937. PMID 773366.
  • 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&ndash, 84. PMID 6746648.
  • 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&ndash, 8. doi:10.1021/bi00196a014. PMID 7913832.
  • Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions". Annu. Rev. Biochem. 69: 961&ndash, 1004. doi:10.1146/annurev.biochem.69.1.961. PMID 10966480.