Home  |  Contact
Due to scheduled maintenance work, this service will not be available from Tuesday August 23rd 06:00 pm until Wednesday August 24th 08:00 am CEST. Apologies for the inconvenience.

ENZYME entry: EC 2.3.1.111

Accepted Name
mycocerosate synthase.
Reaction catalysed
  • 3 (R)-methylmalonyl-CoA + 9 H(+) + long-chain fatty acyl-[mycocerosate synthase] + 6 NADPH <=> 3 CO2 + 3 CoA + 3 H2O + 6 NADP(+) + trimethylated-mycocerosoyl-[mycocerosate synthase]
  • 4 (R)-methylmalonyl-CoA + 12 H(+) + long-chain fatty acyl-[mycocerosate synthase] + 8 NADPH <=> 4 CO2 + 4 CoA + 4 H2O + 8 NADP(+) + tetramethylated-mycocerosoyl-[mycocerosate synthase]
Comment(s)
  • The enzyme, characterized from mycobacteria, is loaded with a long- chain acyl moiety by EC 6.2.1.49 and elongates it by incorporation of three or four methylmalonyl (but not malonyl) residues, to form tri- or tetramethyl-branched fatty-acids, respectively, such as 2,4,6,8- tetramethyloctacosanoate (C32-mycocerosate).
  • Since the enzyme lacks a thioesterase domain, the product remains bound and requires additional enzyme(s) for removal.
  • Even though the enzyme can accept C6 to C20 substrates in vitro, it prefers to act on C14-C20 substrates in vivo.
Cross-references
BRENDA2.3.1.111
EC2PDB2.3.1.111
ExplorEnz2.3.1.111
PRIAM enzyme-specific profiles2.3.1.111
KEGG Ligand Database for Enzyme Nomenclature2.3.1.111
IUBMB Enzyme Nomenclature2.3.1.111
IntEnz2.3.1.111
MEDLINEFind literature relating to 2.3.1.111
MetaCyc2.3.1.111
Rhea expert-curated reactions2.3.1.111
UniProtKB/Swiss-Prot
Q02251, MCAS_MYCBO

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.3.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.3.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-