Enzymatic Deamination ofd-Coronamic Acid: Stereoselectivity of 1-Aminocyclopropane-1-carboxylate Deaminase
- 1 August 1979
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 43 (8) , 1677-1679
- https://doi.org/10.1080/00021369.1979.10863687
Abstract
d-Coronamic acid was deaminated by 1-aminocyclopropane-1-carboxylate (ACPC) deaminase to produce α-keto-n-caproic acid. This deaminase which was purified from Pseudomonas sp. ACP was active to only d-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 d-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.This publication has 3 references indexed in Scilit:
- Metabolism of 1-Aminocyclopropane-1-carboxylic AcidAgricultural and Biological Chemistry, 1978
- Facile Stereoselective Synthesis of (+)- and (−)-Allocoronamic AcidsAgricultural and Biological Chemistry, 1977
- l-Alanine—α-Keto Acid Aminotransferase ofPseudomonassp.Agricultural and Biological Chemistry, 1977