KEGG   ENZYME: 4.1.1.88Help
Entry
EC 4.1.1.88                 Enzyme                                 

Name
biotin-independent malonate decarboxylase;
malonate decarboxylase (without biotin);
malonate decarboxylase (ambiguous);
MDC
Class
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
BRITE hierarchy
Sysname
malonate carboxy-lyase (biotin-independent)
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. 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 4.1.1.89, biotin-dependent malonate decarboxylase). 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 (acetyl-S-ACP:malonate ACP transferase), EC 2.3.1.39 ([acyl-carrier-protein] S-malonyltransferase) and EC 4.1.1.87 (malonyl-S-ACP decarboxylase). The carboxy group is lost with retention of configuration [6].
History
EC 4.1.1.88 created 2008
Reference
1  [PMID:8620876]
  Authors
Schmid M, Berg M, Hilbi H, Dimroth P
  Title
Malonate decarboxylase of Klebsiella pneumoniae catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A-like prosthetic group.
  Journal
Eur. J. Biochem. 237 (1996) 221-8.
Reference
2
  Authors
Byun, H.S. and Kim, Y.S.
  Title
Subunit organization of bacterial malonate decarboxylases: the smallest delta subunit as an acyl-carrier protein.
  Journal
J. Biochem. Mol. Biol. 30 (1997) 132-137.
Reference
3  [PMID:9208947]
  Authors
Hoenke S, Schmid M, Dimroth P
  Title
Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli.
  Journal
Eur. J. Biochem. 246 (1997) 530-8.
Reference
4  [PMID:9851033]
  Authors
Chohnan S, Fujio T, Takaki T, Yonekura M, Nishihara H, Takamura Y
  Title
Malonate decarboxylase of Pseudomonas putida is composed of five subunits.
  Journal
FEMS. Microbiol. Lett. 169 (1998) 37-43.
Reference
5  [PMID:11052676]
  Authors
Hoenke S, Schmid M, Dimroth P.
  Title
Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ancient class of nucleotidyltransferases.
  Journal
Biochemistry. 39 (2000) 13233-40.
Reference
6  [PMID:10496981]
  Authors
Handa S, Koo JH, Kim YS, Floss HG
  Title
Stereochemical course of biotin-independent malonate decarboxylase catalysis.
  Journal
Arch. Biochem. Biophys. 370 (1999) 93-6.
Reference
7  [PMID:10561613]
  Authors
Koo JH, Kim YS
  Title
Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus.
  Journal
Eur. J. Biochem. 266 (1999) 683-90.
Reference
8  [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
9  [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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