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Microbiology 154 (2008), 3329-3337; DOI  10.1099/mic.0.2008/022087-0
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Microbiology 154 (2008), 3329-3337; DOI  10.1099/mic.0.2008/022087-0
© 2008 Society for General Microbiology

Carbon source-dependent modulation of NADP-glutamate dehydrogenases in isophthalate-degrading Pseudomonas aeruginosa strain PP4, Pseudomonas strain PPD and Acinetobacter lwoffii strain ISP4

C. Vamsee-Krishna and Prashant S. Phale

Biotechnology Group, School of Biosciences and Bioengineering, Indian Institute of Technology – Bombay, Powai, Mumbai 400 076, India

Correspondence
Prashant S. Phale
pphale{at}iitb.ac.in

Acinetobacter lwoffii strain ISP4 metabolizes isophthalate rapidly compared with Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Isophthalate has been reported to be a potent competitive inhibitor of glutamate dehydrogenase (GDH). Exogenous supplementation of isophthalate with glutamate or {alpha}-ketoglutarate at 1 mM concentration caused strains PP4 and PPD to grow faster than in the presence of isophthalate alone; however, no such effect was observed in strain ISP4. When grown on isophthalate, all strains showed activity of NADP-dependent GDH (NADP-GDH), while cells grown on glucose, 2x yeast extract-tryptone broth (2YT) or glutamate showed activities of both NAD-dependent GDH (NAD-GDH) and NADP-GDH. Activity staining, inhibition and thermal stability studies indicated the carbon source-dependent presence of two (GDHI and GDHII), three (GDHA, GDHB and GDHC) and one (GDHP) forms of NADP-GDH in strains PP4, PPD and ISP4, respectively. The results demonstrate the carbon source-dependent modulation of different forms of NADP-GDH in these bacterial strains. This modulation may help the efficient utilization of isophthalate as a carbon source by overcoming the inhibitory effect on GDH.


Abbreviations: GDH, glutamate dehydrogenase; mHB, m-hydroxybenzoate; pHB, p-hydroxybenzoate; {alpha}-KG, {alpha}-ketoglutarate; NAD-GDH, NAD-dependent GDH; NADP-GDH, NADP-dependent GDH







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