The pimelyl-CoA synthetase responsible for the first step in biotin biosynthesis by microorganisms.

Abstract
Cell-free extracts of various bacteria were active in catalyzing the synthesis of pimelylCoA from pimelic acid and CoA. The pimelyl-CoA formed was determined in a reaction coupled with the 7-keto-8-aminopelargonic acid (KAPA) synthetase system, which is required to convert pimely-CoA to KAPA, and by microbiologically assaying the amount of KAPA formed. The enzyme synthesizing pimelyl-CoA was named pimely-CoA synthetase and should belong to EC 6. 2. 1. The pimelyl-CoA synthetase reaction required pimelic acid, CoA, ATP and Mg2+ The enzyme was partially purified from a cell-free extract of Bacillus megaterium. Using purified enzyme, characterization of the enzyme was performed. The enzyme reaction was remarkably inhibited by typical metal-chelating agents. Mn2+ and ADP could replace Mg2+ and ATP, respectively. No feedback repression was observed even with the addition of 1.0μg per ml of biotin to the culture medium.

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