Genetic modification of substrate specificity of hypoxanthine phosphoribosyltransferase in Salmonella typhimurium
نویسندگان
چکیده
منابع مشابه
Genetic separation of hypoxanthine and guanine-xanthine phosphoribosyltransferase activities by deletion mutations in Salmonella typhimurium.
Certain proAB deletion mutants of Salmonella typhimurium were found to be simultaneously deleted in a gene required for the utilization of guanine and xanthine (designated gxu). These mutants were resistant to 8-azaguanine and when carrying an additional pur mutation were unable to use guanine or xanthine as a purine source. The defect was correlated with deficiencies in the uptake and phosphor...
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The amino acid sequence of ATP phosphoribosyltransferase [1-(5'-phosphoribosyl)-ATP:pyrophosphate phosphoribosyltransferase, EC 2.4.2.17] of Salmonella typhimurium has been determined. The amino acid sequence analysis was carried out with a combination of manual and automated methods. It was complemented by DNA sequence analysis (done in another laboratory) of the hisG gene, which codes for it....
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A B S T R A C T We have previously described a 14-yrold boy with hyperuricemia, renal failure, and accelerated purine production resistant in vivo and in vitro to purine analogs. This patient demonstrated normal red cell hypoxanthine-guanine phosphoribosyltransferase (HPRT) heat stability, electrophoresis at high pH, and activity at standard substrate levels. In the present report an abnormal H...
متن کاملHuman hypoxanthine-guanine phosphoribosyltransferase.
A mutant form of human hypoxanthine-guanine phosphoribosyltransferase (HPRTToronto) was isolated from erythrocytes of a male patient with gout due to a partial deficiency of enzyme activity. The tryptic peptides of HPRTToronto were mapped by reverse-phase high pressure liquid chromatography in an attempt to define the precise abnormality in its primary structure. Sequence analysis of the single...
متن کاملHuman Hypoxanthine Phosphoribosyltransferase
Hypoxanthine phosphoribosyltransferase (inosine monophosphate: pyrophosphate phosphoribosyltransferase EC 2.4.2.8) has been purified SO-fold from an acid-treated lysate of human erythrocytes. The average particle weight of the enzyme was estimated by gel filtration at 60,000. Between the pH values of 7.1 and 9.1 no marked difference in the initial velocity of IMP synthesis was observed. Kinetic...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1975
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.121.1.77-82.1975