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

被引：29

作者：

HONMA, M

SHIMOMURA, T

SHIRAISHI, K

ICHIHARA, A

SAKAMURA, S

机构：

[1] Department of Agricultural Chemistry, Hokkaido University, Sapporo

来源：

AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1979年 / 43卷 / 08期

关键词：

D O I：

10.1080/00021369.1979.10863687

中图分类号：

S3 [农学（农艺学）];

学科分类号：

0901 ;

摘要：

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.

引用

页码：1677 / 1679

页数：3

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