ENZYME entry: EC 188.8.131.52
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|Biotin-dependent malonate decarboxylase.
|Malonate carboxy-lyase (biotin-dependent).|
|Malonate + H(+) + Na(+)(Side 1) <=> acetate + CO(2) + Na(+)(Side 2)|
- Two types of malonate decarboxylase are currently known, both of
which form multienzyme complexes.
- The enzyme described here is a membrane-bound biotin-dependent,
- 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 184.108.40.206), MadB (EC 220.127.116.11),
MadC/MadD (EC 18.104.22.168) and MadH (EC 22.214.171.124).
- 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.
- Formerly EC 126.96.36.199.
|PRIAM enzyme-specific profiles||188.8.131.52|
|KEGG Ligand Database for Enzyme Nomenclature||184.108.40.206|
|IUBMB Enzyme Nomenclature||220.127.116.11|
|MEDLINE||Find literature relating to 18.104.22.168|
entries corresponding to 7.2.4.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 7.2.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 7.-.-.-