| Accepted Name |
|---|
| biotin-independent malonate decarboxylase
|
| Alternative Name(s) |
|---|
| malonate carboxy-lyase (biotin-independent) |
| malonate decarboxylase |
| MDC |
| Reaction catalysed |
|---|
| malonate + H(+) = acetate + CO2 |
| Comment(s) |
|---|
- 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 7.2.4.4).
- 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 acetyl-ACP.
- 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.
- The individual enzymes involved in carrying out the reaction of this
enzyme complex are EC 2.3.1.187, EC 2.3.1.39 and EC 4.1.1.87.
- The carboxy group is lost with retention of configuration.
|
| Cross-references |
|---|
| BRENDA | 4.1.1.88 |
| EC2PDB | 4.1.1.88 |
| ExplorEnz | 4.1.1.88 |
| KEGG Ligand Database for Enzyme Nomenclature | 4.1.1.88 |
| IUBMB Enzyme Nomenclature | 4.1.1.88 |
| MEDLINE | Find literature relating to 4.1.1.88 |
| MetaCyc | 4.1.1.88 |
| Rhea expert-curated reactions | 4.1.1.88 |
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