The substrate specificity of maleate hydratase from Arthrobacter sp. strain MCI2612 |
| |
| Authors: | M. Ueda H. Yamada Y. Asano |
| |
| Affiliation: | (1) Research Center, Mitsubishi Kasei Corporation, 1000, Kamoshida-cho, Midori-ku, 227 Yokohama, Japan;(2) Faculty of Engineering, Kansai University, Suita, 564 Osaka, Japan;(3) Biotechnology Research Center, Faculty of Engineering, Toyama Prefectural University, Kosugi, 939-03 Toyama, Japan |
| |
| Abstract: | The substrate specificity of maleate hydratase from Arthrobacter sp. strain MCI2612 was examined with maleate and its derivatives. Maleate hydratase was shown to catalyze the hydration of maleate, chloromaleate, bromomaleate, and citraconate. Water was added trans to chloromaleate and bromomaleate to synthesize the (–)-erythro- -substituted derivatives of d-malate. (R)-(–)-Citramalate was synthesized from citraconate by using maleate hydratase. Many organic acids such as acetylenedicarboxylate, l(+)-, d(–)-, and meso-tartarate, and cis-, trans-epoxysuccinate inhibited competitively the formation of d-malate from maleate. |
| |
| Keywords: | |
| 本文献已被 SpringerLink 等数据库收录！ |
|
