| Abstract: | Malonate decarboxylase from Pseudomonas putida is composed of five subunits, α, β, γ, δ, and ε. Two subunits, δ and ε, have been identified as an acyl-carrier protein (ACP) and malonyl-CoA:ACP transacylase, respectively. Functions of the other three subunits have not been identified, because recombinant subunits expressed in Escherichia coli formed inclusion bodies. To resolve this problem, we used a coexpression system with GroEL/ES from E. coli, and obtained active recombinant subunits. Enzymatic analysis of the purified recombinant subunits showed that the α subunit was an acetyl-S-ACP:malonate ACP transferase and that the βγ-subunit complex was a malonyl-S-ACP decarboxylase. |
