Regulation of the mdh-sucCDAB operon in Rhizobium leguminosarum
Oxford University Press, 1999
academicJournal
Zugriff:
The malate dehydrogenase gene, mdh , from Rhizobium leguminosarum encodes a protein with a molecular weight of 33 590 that associates as a homotetramer. It is a lactate dehydrogenase-like malate dehydrogenase that most closely resembles the protein from the colonial green alga Botryococcus braunii . Malate dehydrogenase from R. leguminosarum has a K m of 74 µM and a V max of 822 µmol min−1 mg−1 protein for oxaloacetate, while the K m for malate is 3.6 mM and the V max 62 µmol min−1 mg−1 protein. Downstream of mdh are sucCDAB , which encode succinyl-CoA synthetase ( sucCD ) and the E1 and E2 components of the α-ketoglutarate dehydrogenase complex ( sucAB ). Complementation and LacZ fusion analysis indicates that there is a common promoter for the mdh-suc genes. Mutation of downstream genes in the mdh-suc operon increases transcription 7-fold from the mdh promoter. The transcriptional coupling of mdh and sucCDAB is likely to be important in the regulation of carbon and nitrogen metabolism in bacteroids.
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Regulation of the mdh-sucCDAB operon in Rhizobium leguminosarum
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Autor/in / Beteiligte Person: | Poole, Philip ; Reid, Colm ; East, Alison K. ; Allaway, David ; Day, Michael ; Leonard, Mary |
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Veröffentlichung: | Oxford University Press, 1999 |
Medientyp: | academicJournal |
DOI: | 10.1111/j.1574-6968.1999.tb13669.x |
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