| Literature DB >> 16345474 |
R E Hodson1, F Azam.
Abstract
The mechanism of d-glucose transport in the marine bacterium Serratia marinorubra was investigated. Uptake is mediated by a single, constitutive phosphoenolpyruvate:sugar phosphotransferase system (PTS), resulting in phosphorylation of d-glucose to d-glucose phosphate during transport. The system is saturable (K(m) = 6.4 x 10 M) and highly temperature dependent, with a Q(10) of 3.5 between 5 and 15 degrees C. The system is highly specific for d-glucose; structurally related sugars and sugar alcohols did not significantly compete with d-glucose for transport. The PTS requires Mg (K(m) = 2.5 x 10 M), but its activity is otherwise unaffected by salinity changes over the range tested (0 to 35 per thousand). S. marinorubra differs from other gram-negative organisms (Escherichia coli and Salmonella typhimurium) in that its glycerol (non-PTS substrate) permease is not regulated by the presence of glucose (PTS substrate).Entities:
Year: 1979 PMID: 16345474 PMCID: PMC291250 DOI: 10.1128/aem.38.6.1086-1091.1979
Source DB: PubMed Journal: Appl Environ Microbiol ISSN: 0099-2240 Impact factor: 4.792