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莫拉克斯氏菌属菌株C-1甲酸脱氢酶的纯化及性质

Purification and properties of formate dehydrogenase from Moraxella sp. strain C-1.

作者信息

Asano Y, Sekigawa T, Inukai H, Nakazawa A

机构信息

Sagami Chemical Research Center, Kanagawa, Japan.

出版信息

J Bacteriol. 1988 Jul;170(7):3189-93. doi: 10.1128/jb.170.7.3189-3193.1988.

Abstract

NAD+-dependent formate dehydrogenase was screened in various bacterial strains. Facultative methanol-utilizing bacteria isolated from soil samples, acclimated to a medium containing methanol and formate at pH 9.5, were classified as members of the genus Moraxella. From a crude extract of Moraxella sp. strain C-1, formate dehydrogenase was purified to homogeneity, as judged by disc gel electrophoresis. The enzyme has an isoelectric point of 3.9 and a molecular weight of approximately 98,000. The enzyme is composed of two identical subunits with molecular weights of about 48,000. The apparent Km values for sodium formate and NAD+ were calculated to be 13 mM and 0.068 mM, respectively.

摘要

在各种细菌菌株中筛选了依赖烟酰胺腺嘌呤二核苷酸(NAD+)的甲酸脱氢酶。从土壤样品中分离出的兼性利用甲醇的细菌,适应了pH为9.5的含有甲醇和甲酸的培养基,被归类为莫拉克斯氏菌属成员。通过圆盘凝胶电泳判断,从莫拉克斯氏菌属菌株C-1的粗提取物中,甲酸脱氢酶被纯化至同质。该酶的等电点为3.9,分子量约为98,000。该酶由两个分子量约为48,000的相同亚基组成。甲酸钠和NAD+的表观米氏常数(Km值)分别计算为13 mM和0.068 mM。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/956d/211267/53524f93cfb2/jbacter00185-0311-a.jpg

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