PMID: 8955404Dec 1, 1996Paper

The NAD(P)H-utilizing glutamate dehydrogenase of Bacteroides thetaiotaomicron belongs to enzyme family I, and its activity is affected by trans-acting gene(s) positioned downstream of gdhA

Journal of Bacteriology
L Baggio, Mark Morrison

Abstract

Previous studies have suggested that regulation of the enzymes of ammonia assimilation in human colonic Bacteroides species is coordinated differently than in other eubacteria. The gene encoding an NAD(P)H-dependent glutamate dehydrogenase (gdhA) in Bacteroides thetaiotaomicron was cloned and expressed in Escherichia coli by mutant complementation from the recombinant plasmid pANS100. Examination of the predicted GdhA amino acid sequence revealed that this enzyme possesses motifs typical of the family I-type hexameric GDH proteins. Northern blot analysis with a gdhA-specific probe indicated that a single transcript with an electrophoretic mobility of approximately 1.6 kb was produced in both B. thetaiotaomicron and E. coli gdhA+ transformants. Although gdhA transcription was unaffected, no GdhA enzyme activity could be detected in E. coli transformants when smaller DNA fragments from pANS100, which contained the entire gdhA gene, were analyzed. Enzyme activity was restored if these E. coli strains were cotransformed with a second plasmid, which contained a 3-kb segment of DNA located downstream of the gdhA coding region. Frameshift mutagenesis within the DNA downstream of gdhA in pANS100 also resulted in the loss of GdhA enzyme...Continue Reading

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Citations

Sep 9, 2015·Frontiers in Microbiology·David Rios-CovianClara G de Los Reyes-Gavilán
Aug 30, 2008·Science in China. Series C, Life Sciences·B ZhuS Shen
Sep 11, 2010·Microbiology·Takeo TomitaMakoto Nishiyama
Aug 1, 1997·Applied and Environmental Microbiology·Z Wen, M Morrison
May 28, 2011·Biochimica Et Biophysica Acta·André O HudsonThomas Leustek

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