KEGG   ENZYME: 4.1.1.89Help
Entry
EC 4.1.1.89                 Enzyme                                 

Name
biotin-dependent malonate decarboxylase;
malonate decarboxylase (with biotin);
malonate decarboxylase (ambiguous)
Class
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
BRITE hierarchy
Sysname
malonate carboxy-lyase (biotin-dependent)
Reaction(IUBMB)
malonate + H+ = acetate + CO2 [RN:R09483]
Reaction(KEGG)
Substrate
malonate [CPD:C00383];
H+ [CPD:C00080]
Product
acetate [CPD:C00033];
CO2 [CPD:C00011]
Comment
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 [6]. The other type is a biotin-independent cytosolic protein (cf. EC 4.1.1.88, biotin-independent malonate decarboxylase). 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, acetyl-S-ACP:malonate ACP transferase), MadB (EC 4.3.99.2, carboxybiotin decarboxylase), MadC/MadD (EC 2.1.3.10, malonyl-S-ACP:biotin-protein carboxyltransferase) and MadH (EC 6.2.1.35, ACP-SH:acetate ligase). 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 [5].
History
EC 4.1.1.89 created 2008
Reference
1  [PMID:1628643]
  Authors
Hilbi H, Dehning I, Schink B, Dimroth P
  Title
Malonate decarboxylase of Malonomonas rubra, a novel type of biotin-containing acetyl enzyme.
  Journal
Eur. J. Biochem. 207 (1992) 117-23.
Reference
2  [PMID:18251085]
  Authors
Hilbi H, Dimroth P
  Title
Purification and characterization of a cytoplasmic enzyme component of the Na+-activated malonate decarboxylase system of Malonomonas rubra: acetyl-S-acyl carrier protein: malonate acyl carrier protein-SH transferase.
  Journal
Arch. Microbiol. 162 (1994) 48-56.
Reference
3  [PMID:8664258]
  Authors
Berg M, Hilbi H, Dimroth P
  Title
The acyl carrier protein of malonate decarboxylase of Malonomonas rubra contains 2'-(5"-phosphoribosyl)-3'-dephosphocoenzyme A as a prosthetic group.
  Journal
Biochemistry. 35 (1996) 4689-96.
Reference
4  [PMID:9128730]
  Authors
Berg M, Hilbi H, Dimroth P
  Title
Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function.
  Journal
Eur. J. Biochem. 245 (1997) 103-15.
  Sequence
[up:O06930]
Reference
5
  Authors
Micklefield, J., Harris, K.J., Groger, S., Mocek, U., Hilbi, H., Dimroth, P. and Floss, H.G.
  Title
Stereochemical course of malonate decarboxylase in Malonomonas rubra has biotin decarboxylation with retention.
  Journal
J. Am. Chem. Soc. 117 (1995) 1153-1154.
Reference
6  [PMID:12359084]
  Authors
Kim YS
  Title
Malonate metabolism: biochemistry, molecular biology, physiology, and industrial application.
  Journal
J. Biochem. Mol. Biol. 35 (2002) 443-51.
Reference
7  [PMID:11902724]
  Authors
Dimroth P, Hilbi H
  Title
Enzymic and genetic basis for bacterial growth on malonate.
  Journal
Mol. Microbiol. 25 (1997) 3-10.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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