The molybdenum cofactor biosynthesis protein MobA from Rhodobacter capsulatus is required for the activity of molybdenum enzymes containing MGD, but not for xanthine dehydrogenase harboring the MPT cofactor

被引：16

作者：

Leimkühler, S ^{[1
]}

Klipp, W ^{[1
]}

机构：

[1] Ruhr Univ Bochum, Fak Biol, Lehrstuhl Biol Mikroorganismen, D-44780 Bochum, Germany

来源：

FEMS MICROBIOLOGY LETTERS | 1999年 / 174卷 / 02期

关键词：

molybdoenzyme; molybdenum cofactor biosynthesis; molybdopterin guanine dinucleotide synthase mob locus; Rhodobacter capsulatus;

D O I：

10.1111/j.1574-6968.1999.tb13574.x

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The requirement of MobA for molybdoenzymes with different molybdenum cofactors was analyzed in Rhodobacter capsulatus. MobA is essential for DMSO reductase and nitrate reductase activity, both enzymes containing the molybdopterin guanine dinucleotide cofactor (MGD), but not for active xanthine dehydrogenase,, harboring the molybdopterin cofactor. In contrast to the nob locus of Escherichia coli and R. sphaeroides; the mobB gene is not located downstream of mobA in R. capsulatus. The mobA gene is expressed constitutively at low levels and no increase in mobA expression could be observed even under conditions of high MGD demand. (C) 1999 Federation of European Microbiological Societies.-Published by Elsevier Science B.V. All rights reserved.

引用

页码：239 / 246

页数：8

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