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 4.1.1.89

Accepted Name
Biotin-dependent malonate decarboxylase.
Alternative Name(s)
Malonate carboxy-lyase (biotin-dependent).
Malonate decarboxylase.
Reaction catalysed
Malonate + H(+) <=> acetate + CO(2)
Comment(s)
  • Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes.
  • The enzyme described here is a biotin-dependent, Na(+)-translocating enzyme that includes both soluble and membrane-bound components.
  • The other type is a biotin-independent cytosolic protein (cf. EC 4.1.1.88).
  • As free malonate is chemically rather inert, it has to be activated prior to decarboxylation.
  • Both enzymes achieve this 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- bound form of the enzyme.
  • 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.
  • In the anaerobic bacterium Malonomonas rubra, the components of the multienzyme complex/enzymes involved in carrying out the reactions of this enzyme are as follows: MadA (EC 2.3.1.187), MadB (EC 4.3.99.2), MadC/MadD (EC 2.1.3.10) and MadH (EC 6.2.1.35).
  • Two other components that are involved are MadE, the acyl-carrier protein and MadF, the biotin protein.
  • The carboxy group is lost with retention of configuration.
Cross-references
PROSITEPDOC50980
BRENDA4.1.1.89
EC2PDB4.1.1.89
ExplorEnz4.1.1.89
PRIAM enzyme-specific profiles4.1.1.89
KEGG Ligand Database for Enzyme Nomenclature4.1.1.89
IUBMB Enzyme Nomenclature4.1.1.89
IntEnz4.1.1.89
MEDLINEFind literature relating to 4.1.1.89
MetaCyc4.1.1.89

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