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carboxyl transferase domain-containing protein
All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognised types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilise acyl-CoA as the acceptor molecule. [1]. 8366018. Primary structure of the monomer of the 12S subunit of transcarboxylase as deduced from DNA and characterization of the product expressed in Escherichia coli. Thornton CG, Kumar GK, Haase FC, Phillips NF, Woo SB, Park VM, Magner WJ, Shenoy BC, Wood HG, Samols D;. J Bacteriol 1993;175:5301-5308. [2]. 8102604. Molecular evolution of biotin-dependent carboxylases. Toh H, Kondo H, Tanabe T;. Eur J Biochem 1993;215:687-696. [3]. 12663926. Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase. Zhang H, Yang Z, Shen Y, Tong L;. Science 2003;299:2064-2067. (from Pfam)
malonate decarboxylase subunit beta
malonate decarboxylase subunit beta catalyzes the carboxylation of acetyl-CoA to malonyl-CoA
biotin-independent malonate decarboxylase subunit beta
Members of this protein family are the beta subunit of malonate decarboxylase. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. In the malonate decarboxylase complex, the beta subunit appears to act as a malonyl-CoA decarboxylase.
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