ENZYME entry: EC 220.127.116.11
View entry in original ENZYME format
View entry in raw text format (no links)
|Biotin-independent malonate decarboxylase.
|Malonate carboxy-lyase (biotin-independent).|
|Malonate + H(+) <=> acetate + CO(2)|
- 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 18.104.22.168).
- 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 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
- The individual enzymes involved in carrying out the reaction of this
enzyme complex are EC 22.214.171.124, EC 126.96.36.199 and EC 188.8.131.52.
- 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|
entries corresponding to 4.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-