Zobrazeno 1 - 10
of 22
pro vyhledávání: '"H.Richard Levy"'
Autor:
W. Theodore Lee, H.Richard Levy
Publikováno v:
Protein Science. 1:329-334
Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase (G6PD) was isolated in high yield and purified to homogeneity from a newly constructed strain of Escherichia coli which lacks its own glucose 6-phosphate dehydrogenase gene. Lys-21 is one of
Autor:
H.Richard Levy, Thomas H. Grove
Publikováno v:
Biochemical and Biophysical Research Communications. 86:387-394
Pyridoxal 5′-phosphate reacts with the anthranilate synthetase-phosphoribosyltransferase enzyme complex of Salmonella typhimurium to inhibit PR transferase activity. Glutamine-dependent anthranilate synthetase is not affected. Spectral and kinetic
Autor:
Peter D. Robison, H.Richard Levy
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 445:475-485
1. Both Mn2+ and Co2+ can replace Mg2+ as the required divalent cation for all activities of the enzyme complex between anthranilate synthase (chorismate pyruvate-lyase (amino-accepting), EC 4.1.3.27) and anthranilate-5-phosphoribosylpyrophosphate ph
Evidence for an Essential Lysine in Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides
Autor:
Michael Milhausen, H.Richard Levy
Publikováno v:
European Journal of Biochemistry. 50:453-461
Pyridoxal 5′-phosphate inhibits glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides reversibly which Ki= 0.04–0.06 mM. This inhibition is competitive with respect to glucose 6-phosphate and non-competitive with respect to NADP+ or NA
Autor:
H.Richard Levy, Thomas H. Grove
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 445:464-474
1. 1.|The anthranilate synthase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase enzyme complex (chorismate pyruvate-lyase (aminoaccepting), EC 4.1.3.27) · ( N-(5′- phosphoribosyl)-anthranilate :pyrophosphate phosphoribosyltran
Publikováno v:
Archives of Biochemistry and Biophysics. 177:307-316
Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides utilizes either NAD+ or NADP+ as coenzyme. Kinetic studies showed that NAD+ and NADP+ interact with different enzyme forms (Olive, C., Geroch, M. E., and Levy, H. R. (1971) J. Biol. Che
Publikováno v:
Archives of Biochemistry and Biophysics. 198:406-413
The dual wavelength assay technique (H. R. Levy, and G. H. Daouk, 1979, J. Biol. Chem.254, 4843–4847) is used to examine the rates of the NADP- and NAD-linked reactions of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase simultaneously u
Autor:
H.Richard Levy, Thomas H. Grove
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 397:80-93
Exposure of the anthranilate synthetase-anthranilate phosphoribosyltransferase enzyme complex (chorismate pyruvate-lyase (amino-accepting) EC 4.1.3.27 and N-(5-phosphoribosyl)-anthranilate pyrophosphate phosphoribosyl-transferase, EC 2.4.2.18) from S
Publikováno v:
Biochemical and Biophysical Research Communications. 59:894-901
Glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides has a subunit molecular weight of 55,000, determined by SDS gel electrophoresis. The amino acid composition of the enzyme is reported. An unusual feature which has not been reported for
Publikováno v:
Journal of Biological Chemistry. 241:2181-2187
Experiments were conducted in order to elucidate the relationship between the structure of mammary glucose 6-phosphate dehydrogenase and its catalytic activities with nicotinamide adenine dinucleotide phosphate and nicotinamide adenine dinucleotide.