This enzyme comprises the beta and gamma subunits of EC 4.1.1.88, biotin-independent malonate decarboxylase but is not present in EC 7.2.4.4, biotin-dependent malonate decarboxylase. It follows on from EC 2.3.1.187, acetyl-S-ACP:malonate ACP transferase, and results in the regeneration of the acetylated form of the acyl-carrier-protein subunit of malonate decarboxylase . The carboxy group is lost with retention of configuration .
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The enzyme appears in viruses and cellular organisms
a malonyl-[acyl-carrier protein] + H+ = an acetyl-[acyl-carrier protein] + CO2
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a malonyl-[acyl-carrier protein] + H+ = an acetyl-[acyl-carrier protein] + CO2
malonate decarboxylation proceeds in two steps: the acetyl residue on the acyl carrier protein is first replaced by a malonyl residue which subsequently undergoes decarboxylation thereby regenerating the acetyl-S-acyl carrier protein
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SYSTEMATIC NAME
IUBMB Comments
malonyl-[acyl-carrier-protein] carboxy-lyase
This enzyme comprises the beta and gamma subunits of EC 4.1.1.88, biotin-independent malonate decarboxylase but is not present in EC 7.2.4.4, biotin-dependent malonate decarboxylase. It follows on from EC 2.3.1.187, acetyl-S-ACP:malonate ACP transferase, and results in the regeneration of the acetylated form of the acyl-carrier-protein subunit of malonate decarboxylase [5]. The carboxy group is lost with retention of configuration [3].
presence of two forms of the enzyme: a catalytically inactive SH-enzyme and the catalytically active acetyl-S-enzyme which is formed by post-translational acetylation of the SH-enzyme with ATP, acetate and a specific ligase. the delta subunit is the acyl carrier protein of the enzyme complex
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reacylation of the catalytically inactive SH-enzyme to form the catalytically active acetyl-S-enzyme can be achieved with acetic anhydride or more efficiently with malonyl-CoA
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4.1.1.87 malonyl-S-ACP decarboxylase
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