ENZYME entry: EC 220.127.116.11
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|Biotin-dependent malonate decarboxylase.
|Malonate carboxy-lyase (biotin-dependent).|
|Malonate + H(+) <=> acetate + CO(2)|
- 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.
- 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
- 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 18.104.22.168), MadB (EC 22.214.171.124),
MadC/MadD (EC 126.96.36.199) and MadH (EC 188.8.131.52).
- 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.
|PRIAM enzyme-specific profiles||184.108.40.206|
|KEGG Ligand Database for Enzyme Nomenclature||220.127.116.11|
|IUBMB Enzyme Nomenclature||18.104.22.168|
|MEDLINE||Find literature relating to 22.214.171.124|
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entries corresponding to 4.1.-.-
entries corresponding to 4.-.-.-