Enzymatic Deamination of d-Coronamic Acid: Stereoselectivity of 1-Aminocyclopropane-1-carboxylate Deaminase
Enzymatic Deamination of d-Coronamic Acid: Stereoselectivity of 1-Aminocyclopropane-1-carboxylate Deaminase
复制标题
d-冠状酸的酶促脱氨：1-氨基环丙烷-1-羧酸脱氨酶的立体选择性
DOI：
10.1271/bbb1961.43.1677
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发表时间：
1979
期刊：
影响因子：
--
通讯作者：
S. Sakamura
中科院分区：
文献类型：
--
作者：
M. Honma;T. Shimomura;Kunio Shiraishi;A. Ichihara;S. Sakamura
d-冠酸通过 1-氨基环丙烷-1-羧酸酯 (ACPC) 脱氨酶脱氨，生成 α-酮基-正己酸。这种脱氨酶是从假单胞菌中纯化的。 ACP 仅对其立体异构体中的 d-冠酸有活性。 L-冠酸或dl-别冠酸作为底物没有活性或可以忽略不计。此外，ACPC和d-冠酸的脱氨基作用均受到L-丙氨酸的抑制，而不受d-异构体的抑制，并且L-丙氨酸对ACPC脱氨基作用的抑制是竞争性的。在这些结果的基础上，讨论了酶促脱氨基的立体选择性。
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.