An archaeal 2-deoxyribose 5-phosphate aldolase that exhibits closer homology to bacteria rather than Archaea. | [Journal of Chemical Society of Pakistan • 2008]

Author(s):

1. Naeem Rashid: School of Biological Sciences, University of the Punjab, Lahore, Pakistan

2. Hiroyuki Imanaka: Department of Bioscience and Biotechnology, Okayama University, Okayama, Japan

3. Tadayuki Imanaka: Department of Synthetic Chemistry and Biological Chemistry. Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, Japan

Abstract:

This study reports on primary structure comparison and some enzymatic characterization of 2-deoxyribose 5-phosphate aldolase from the hypcrthermophilic archaeon, Thermococcus kodakaraensis KODI (Tk-DeoC), The Tk-DeoCexhibited a significant closer homology to bacterial 2=deoxyribose 5=phosphate aldolases (DeoC)than those of archaeal counterparts. Recombinant Tk-DeoC catalyzed the conversion of 2-deoxyribosc 5-phosphate to acetaldehyde and glyceraldehyde 3-phosphate with a highest activity at 95oC and the pH optimum of 4.0. In T kodakaraensis transcription of deoC.was readily detectable and the corresponding DeoCactivity was measurable in the cell-free extracts, indicating the constitutive expression of deoCin T kodakaraensiscells.However, in contrast to the finding in bacteria where DeoC, together with DeoA, DeoB and DeoD, participate in the catabolism of exogenous DNA and presence of nucleotides in the growth medium induces these genes, supplementation of DNA to the growth medium showed no detectable induction of deoC transcription.

Page(s): 740-749

DOI: DOI not available

Published: Journal: Journal of Chemical Society of Pakistan, Volume: 30, Issue: 5, Year: 2008

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