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
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
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DOI:
10.1111/j.1574-6968.1999.tb13574.x
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发表时间:
1999-05-15
影响因子:
2.1
通讯作者:
Klipp, W
中科院分区:
文献类型:
--
作者:
Leimkühler, S;Klipp, W
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.