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ENZYME entry: EC 4.1.1.88

Accepted Name
Biotin-independent malonate decarboxylase.
Alternative Name(s)
Malonate carboxy-lyase (biotin-independent).
Malonate decarboxylase.
MDC.
Reaction catalysed
Malonate + H(+) <=> acetate + CO(2)
Comment(s)
  • Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes.
  • This enzyme is a cytosolic protein that is biotin-independent.
  • The other type is a biotin-dependent, Na(+)-translocating enzyme that includes both soluble and membrane-bound components (cf. EC 4.1.1.89).
  • As free malonate is chemically rather inert, it has to be activated prior to decarboxylation.
  • In both enzymes, this is achieved by exchanging malonate with an acetyl group bound to an acyl-carrier protiein (ACP), to form malonyl-ACP and acetate, with subsequent decarboxylation regenerating the acetyl-ACP.
  • The ACP subunit of both enzymes differs from that found in fatty-acid biosynthesis by having phosphopantethine attached to a serine side- chain as 2'-(5-triphosphoribosyl)-3'-dephospho-CoA rather than as phosphopantetheine 4'-phosphate.
  • The individual enzymes involved in carrying out the reaction of this enzyme complex are EC 2.3.1.187, EC 2.3.1.39 and EC 4.1.1.87.
  • The carboxy group is lost with retention of configuration.
Cross-references
PROSITEPDOC50980
BRENDA4.1.1.88
EC2PDB4.1.1.88
ExplorEnz4.1.1.88
PRIAM enzyme-specific profiles4.1.1.88
KEGG Ligand Database for Enzyme Nomenclature4.1.1.88
IUBMB Enzyme Nomenclature4.1.1.88
IntEnz4.1.1.88
MEDLINEFind literature relating to 4.1.1.88
MetaCyc4.1.1.88

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.1.1.-
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