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EC 4.1.1.88 is Orphan !
Common name :Biotin-independent malonate decarboxylase

Systematic name :Malonate carboxy-lyase (biotin-independent)

Other names :Malonate decarboxylase (without biotin)
MDC
Comments :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). 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). 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.

Created :EC 4.1.1.88 created 2008

BRENDA organisms :Acinetobacter calcoaceticus
Acinetobacter calcoaceticus
Klebsiella pneumoniae
Pseudomonas fluorescens
Prosite :PDOC50980

Swiss-ProtNo protein sequences are associated with EC 4.1.1.88 in Swiss-Prot

TrEMBLNo protein sequences are associated with EC 4.1.1.88 in TrEMBL

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Links to other databases
NC-IUBMB, INTENZ, ENZYME, PDB, BRENDA, KEGG, BIOCYC, PubMed,NCBI-Entrez

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