| Accepted Name |
|---|
| biotin-dependent malonate decarboxylase
|
| Alternative Name(s) |
|---|
| malonate carboxy-lyase (biotin-dependent) |
| malonate decarboxylase |
| Reaction catalysed |
|---|
| H(+) + malonate + Na(+)(in) = acetate + CO2 + Na(+)(out) |
| Comment(s) |
|---|
- Two types of malonate decarboxylase are currently known, both of
which form multienzyme complexes.
- The enzyme described here is a membrane-bound biotin-dependent,
Na(+)-translocating enzyme.
- 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 7.2.4.1),
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.
- Formerly EC 4.1.1.89.
|
| Cross-references |
|---|
| BRENDA | 7.2.4.4 |
| EC2PDB | 7.2.4.4 |
| ExplorEnz | 7.2.4.4 |
| PRIAM enzyme-specific profiles | 7.2.4.4 |
| KEGG Ligand Database for Enzyme Nomenclature | 7.2.4.4 |
| IUBMB Enzyme Nomenclature | 7.2.4.4 |
| IntEnz | 7.2.4.4 |
| MEDLINE | Find literature relating to 7.2.4.4 |
| MetaCyc | 7.2.4.4 |
| Rhea expert-curated reactions | 7.2.4.4 |
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