Literature DB >> 6439205

Induction of deoxyribose-5-phosphate aldolase of Bacillus cereus by deoxyribonucleosides.

M G Tozzi, F Sgarrella, D Barsacchi, P L Ipata.   

Abstract

In Bacillus cereus purine ribonucleosides and deoxyribonucleosides share a common inducible catabolic pathway, leading to the formation of ribose-5-P or deoxyribose-5-P respectively inside the cell, while the purine ring remains in the external medium. Both ribo- and deoxyribonucleosides are inducers of adenosine deaminase, inosine-guanosine phosphorylase and phosphopentomutase, the enzymes of the catabolic pathway. We now show that deoxyribonucleosides, but not ribonucleosides, induce the aldolase specific for deoxyribose-5-P (2-deoxy-D-ribose-5-phosphate acetaldehyde lyase, EC 4.1.2.4), thus allowing the sugar moiety of exogenous deoxyribonucleosides to be utilized as an energy source.

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Year:  1984        PMID: 6439205

Source DB:  PubMed          Journal:  Biochem Int        ISSN: 0158-5231


  2 in total

1.  Presence of a novel phosphopentomutase and a 2-deoxyribose 5-phosphate aldolase reveals a metabolic link between pentoses and central carbon metabolism in the hyperthermophilic archaeon Thermococcus kodakaraensis.

Authors:  Naeem Rashid; Hiroyuki Imanaka; Toshiaki Fukui; Haruyuki Atomi; Tadayuki Imanaka
Journal:  J Bacteriol       Date:  2004-07       Impact factor: 3.490

2.  Identification of proteins involved in the heat stress response of Bacillus cereus ATCC 14579.

Authors:  Paula M Periago; Willem van Schaik; Tjakko Abee; Jeroen A Wouters
Journal:  Appl Environ Microbiol       Date:  2002-07       Impact factor: 4.792

  2 in total

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