ENZYMATIC DEAMINATION OF D-CORONAMIC ACID - STEREOSELECTIVITY OF 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE

D-Coronamic acid was deaminated by 1-aminocyclopropane-l-carboxylate (ACPC) deaminase to produce a-keto-1i-caproic acid. This deaminase which was purified from Pseudomonas sp. ACP was active to only rf-coronamic acid among its stereoisomers. L- Coronamic acid or dL-allocoronamic acid was inactive or negligibly poor as the substrate. In addition, both deamination of ACPC and rf-coronamic acid were inhibited by L-alanine, not by D-isomer and the inhibition of ACPC deamination by L-alanine was competitive. On the basis of these results, stereoselectivity of the enzymatic deamination was discussed. © 1979 Taylor & Francis Group, LLC.