Phosphate-irrepressible Alkaline Phosphatase of Zymomonas mobilis
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چکیده
منابع مشابه
Cloning, sequencing and characterization of the alkaline phosphatase gene (phoD) from Zymomonas mobilis.
The phoD gene encoding the membrane-bound alkaline phosphatase (ALPI) from Zymomonas mobilis CP4 was cloned and sequenced. Both the translated sequence and the properties of the recombinant enzyme were unusual. Z. mobilis ALPI was monomeric (M(r) 62,926) and hydrolysed nucleotides more effectively than sugar phosphates. The translated sequence contained a single hydrophobic segment near the N-t...
متن کاملCharacterization and sequence of PhoC, the principal phosphate-irrepressible acid phosphatase of Morganella morganii.
Phosphatase activities were investigated in Morganella morganii, which is one of the few enterobacterial species producing high-level phosphate-irrepressible acid phosphatase activity (HPAP phenotype), and the gene encoding the major phosphate-irrepressible acid phosphatase was cloned, sequenced, and its product characterized. Using p-nitrophenyl phosphate as substrate, Morganella produced a ma...
متن کاملGlycolytic enzymes in Zymomonas mobilis.
Raps, Shirley (University of Illinois, Urbana) and R. D. DeMoss. Glycolytic enzymes in Zymomonas mobilis. J. Bacteriol. 84:115-118. 1962-An enzyme extract of Zymomonas mobilis (Pseudomonas lindneri) was capable of fermenting glucose-6-phosphate to CO(2) and ethanol. The extract was found to contain phosphohexoisomerase, aldolase, and glyceraldehyde-3-phosphate dehydrogenase, but no demonstrable...
متن کاملPhosphate Binding to Alkaline Phosphatase
The metal ion dependence of a2P binding to Escherichia coli alkaline phosphatase has been studied by means of equilibrium dialysis. Whereas the apoenzyme does not bind phosphate (no sites with K < 5 X 10-5 M), the addition of 2 Zn(I1) cations per molecule induces the tight binding of 1 phosphate dianion (K = 6 X 1OF M). The magnitude of this binding constant is affected by ionic strength, pH, a...
متن کاملProduction of Acetaldehyde by Zymomonas mobilis.
Mutants of Zymomonas mobilis were selected for decreased alcohol dehydrogenase activity by using consecutively higher concentrations of allyl alcohol. A mutant selected by using 100 mM allyl alcohol produced acetaldehyde at a level of 4.08 g/liter when the organism was grown in aerated batch cultures on a medium containing 4.0% (wt/wt) glucose. On the basis of the amount of glucose utilized, th...
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ژورنال
عنوان ژورنال: Microbiology
سال: 1989
ISSN: 1350-0872,1465-2080
DOI: 10.1099/00221287-135-2-453