利用改良邻位途径的氯代芳烃降解细菌中的马来酰乙酸还原酶：催化特性比较
Maleylacetate reductases in chloroaromatic-degrading bacteria using the modified ortho pathway: comparison of catalytic properties.
作者信息
Müller D, Schlömann M, Reineke W
机构信息
Bergische Universität-Gesamthochschule Wuppertal, Germany.
出版信息
J Bacteriol. 1996 Jan;178(1):298-300. doi: 10.1128/jb.178.1.298-300.1996.
Abstract
The maleylacetate reductases from Pseudomonas aeruginosa RHO1 and Alcaligenes eutrophus JMP134 were tested for activity and affinity to various maleylacetates as well as dechlorinating properties. The dechlorinating activity and the kcat/Km values revealed high-level similarity of these reductases to that of Pseudomonas sp. strain B13.
摘要
对铜绿假单胞菌RHO1和食碱假单胞菌JMP134中的马来酸乙酸还原酶进行了测试，以考察其对各种马来酸乙酸的活性、亲和力以及脱氯特性。脱氯活性和催化常数与米氏常数的比值显示，这些还原酶与假单胞菌属菌株B13的还原酶具有高度相似性。
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