Kaschabek S R, Reineke W
Chemische Mikrobiologie der Bergischen Universität-Gesamthochschule Wuppertal, Federal Republic of Germany.
Arch Microbiol. 1992;158(6):412-7. doi: 10.1007/BF00276301.
The maleylacetate reductase of 3-chlorobenzoate-grown cells of Pseudomonas sp. strain B13 has been purified 50-fold. The enzyme converted 2-chloromaleylacetate to 3-oxoadipate with temporary occurrence of maleylacetate; 1 mol of chloride was eliminated during the conversion of 1 mol of 2-chloro- and 2,3-dichloromaleylacetate; 2 mol of NADH were consumed per mol of 2-chloro- and 2,3-dichloromaleylacetate while only 1 mol was necessary to catalyze the conversion of maleylacetate or 2-methylmaleylacetate. The maleylacetate reductase failed to use fumarylacetate as a substrate. The role of the enzyme in the chloroaromatics degradation is discussed.
在以3-氯苯甲酸为生长底物的假单胞菌属B13菌株细胞中，马来酰乙酸还原酶已被纯化了50倍。该酶将2-氯马来酰乙酸转化为3-氧代己二酸，过程中会短暂出现马来酰乙酸；在1摩尔2-氯和2,3-二氯马来酰乙酸的转化过程中会消除1摩尔氯离子；每摩尔2-氯和2,3-二氯马来酰乙酸消耗2摩尔NADH，而催化马来酰乙酸或2-甲基马来酰乙酸的转化仅需1摩尔NADH。马来酰乙酸还原酶不能利用富马酰乙酸作为底物。文中讨论了该酶在氯代芳烃降解中的作用。
