恶臭假单胞菌ML2中一种新型顺式苯二氢二醇脱氢酶的特性分析

Characterization of a novel cis-benzene dihydrodiol dehydrogenase from Pseudomonas putida ML2.

作者信息

Fong K P, Tan H M

机构信息

Department of Microbiology, National University of Singapore, Singapore.

出版信息

FEBS Lett. 1999 May 14;451(1):5-9. doi: 10.1016/s0014-5793(99)00520-7.

DOI:10.1016/s0014-5793(99)00520-7

PMID:10356973

Abstract

A second and novel cis-benzene dihydrodiol dehydrogenase which is able to dehydrogenate a range of cis-dihydrodiols and other vicinal alcohols has been purified from Pseudomonas putida ML2. The enzyme is a tetramer of a polypeptide of 39 kDa in molecular mass and has a pH optimum of 9.0. Despite having a primary structure that has significant similarity to glycerol dehydrogenases, the kcat/Km value of the enzyme for cis-benzene dihydrodiol is 4300-fold higher compared to glycerol. The apparent Km values of the enzyme for cis-benzene dihydrodiol and glycerol are 0.01 mM and 46 mM, respectively, and 0.22 mM for NAD+.

摘要

已从恶臭假单胞菌ML2中纯化出第二种新型的顺式苯二氢二醇脱氢酶，该酶能够使一系列顺式二氢二醇和其他邻位醇脱氢。该酶是一种分子量为39 kDa的多肽的四聚体，最适pH为9.0。尽管其一级结构与甘油脱氢酶有显著相似性，但该酶对顺式苯二氢二醇的kcat/Km值比甘油高4300倍。该酶对顺式苯二氢二醇和甘油的表观Km值分别为0.01 mM和46 mM，对NAD+的表观Km值为0.22 mM。