1Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
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
Article first published online: 17 JAN 2006
FEMS Microbiology Letters
Volume 174, Issue 2, pages 239–246, May 1999
How to Cite
Leimkühler, S. and Klipp, W. (1999), 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. FEMS Microbiology Letters, 174: 239–246. doi: 10.1111/j.1574-6968.1999.tb13574.x
- Issue published online: 17 JAN 2006
- Article first published online: 17 JAN 2006
- Received 4 January 1999, Accepted 24 March 1999
- Molybdenum cofactor biosynthesis;
- Molybdopterin guanine dinucleotide synthase;
- mob locus;
- Rhodobacter capsulatus
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 mob 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.