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 |
PROSITE | PDOC50980 |
BRENDA | 4.1.1.89 |
EC2PDB | 4.1.1.89 |
ExplorEnz | 4.1.1.89 |
PRIAM enzyme-specific profiles | 4.1.1.89 |
KEGG Ligand Database for Enzyme Nomenclature | 4.1.1.89 |
IUBMB Enzyme Nomenclature | 4.1.1.89 |
IntEnz | 4.1.1.89 |
MEDLINE | Find literature relating to 4.1.1.89 |
MetaCyc | 4.1.1.89 |
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