ALKENE MONOOXYGENASE FROM MYCOBACTERIUM - A MULTICOMPONENT ENZYME

被引：39

作者：

HARTMANS, S

WEBER, FJ

SOMHORST, DPM

DEBONT, JAM

机构：

[1] Div of Industrial Microbiology, Department of Food Science, Agricultural University, 6700 EV Wageningen

来源：

JOURNAL OF GENERAL MICROBIOLOGY | 1991年 / 137卷

关键词：

D O I：

10.1099/00221287-137-11-2555

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A NADH-or NADPH-dependent alkene monooxygenase (AMO) activity has been detected in cell-free extracts of the ethene-utilizing Mycobacterium E3 and Mycobacterium aurum L1. The activity was not linear with protein concentration in the assay suggesting AMO is a multicomponent enzyme. The inhibition pattern of AMO activity was very similar to the inhibition patterns published for the three-component soluble methane monooxygenases. Fractionation of crude extracts revealed that combination of two fractions was required to restore alkene monooxygenase activity. The first fraction was inhibited by acetylene, indicating it contained an oxygenase component. The second fraction contained reductase activity which was absent from non-induced cells. This reductase activity is probably the NADH-acceptor reductase of AMO.

引用

页码：2555 / 2560

页数：6

共 27 条

[1] BACTERIAL OXIDATION OF METHANE AND METHANOL [J].