Abstract
The report is the first of purification, overproduction, and characterization of a unique -butyrobetainyl CoA synthetase from soil-isolated Agrobacterium sp. 525a. The primary structure of the enzyme shares 70-95% identity with those of ATP-dependent microbial acyl-CoA synthetases of the Rhizobiaceae family. As distinctive characteristics of the enzyme of this study, ADP was released in the catalytic reaction process, whereas many acyl CoA synthetases are annotated as an AMP-forming enzyme. The apparent K-m values for -butyrobetaine, CoA, and ATP were, respectively, 0.69, 0.02, and 0.24mM.