PURIFICATION AND CHARACTERIZATION OF AN NAD+-DEPENDENT SECONDARY ALCOHOL-DEHYDROGENASE FROM PSEUDOMONAS-MALTOPHILIA MB11L

被引：5

作者：

BRITT, AJ

BRUCE, NC

LOWE, CR

机构：

[1] Institute of Biotechnology, University of Cambridge, Cambridge

来源：

FEMS MICROBIOLOGY LETTERS | 1992年 / 93卷 / 01期

关键词：

SECONDARY ALCOHOL DEHYDROGENASE; PSEUDOMONAS-MALTOPHILIA; NAD+-DEPENDENT OXIDOREDUCTASE;

D O I：

10.1016/0378-1097(92)90488-A

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A constitutive NAD+-linked alcohol dehydrogenase was purified 338-fold from cells of Pseudomonas maltophilia MB11L grown on glucose. Maximum activity was observed with cyclic and linear secondary alcohols, with little activity seen against primary or aromatic alcohols. Substrate oxidation activity was maximal at pH 10.0, while substrate reduction was optimal at pH 4.5. The K(m) values for propan-2-ol, NAD+ and acetone were 87, 413 and 143-mu-M respectively. The enzyme is a tetramer with subunit M(r) of approximately 44 000. It has an isoelectric point of 4.75, and was inhibited by chelating agents, thiol reagents and certain metal ions.

引用

页码：49 / 55

页数：7

共 31 条

[1] ESTIMATION OF MOLECULAR WEIGHTS OF PROTEINS BY SEPHADEX GEL-FILTRATION [J].