A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 2.3.1.111

Accepted Name
Mycocerosate synthase.
Reaction catalysed
  • A long-chain acyl-[mycocerosic acid synthase] + 3 methylmalonyl-CoA + 6 NADPH <=> a trimethylated-mycocerosoyl-[mycocerosate synthase] + 3 CoA + 3 CO(2) + 6 NADP(+) + 3 H(2)O
  • A long-chain acyl-[mycocerosate synthase] + 4 methylmalonyl-CoA + 8 NADPH <=> a tetramethylated-mycocerosoyl-[mycocerosate synthase] + 4 CoA + 4 CO(2) + 8 NADP(+) + 4 H(2)O
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 (C(32)-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 C(6) to C(20) substrates in vitro, it prefers to act on C(14)-C(20) substrates in vivo.
Cross-references
PROSITEPDOC00529
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
UniProtKB/Swiss-Prot
Q02251, MCAS_MYCBO

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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.-.-.-