Zobrazeno 1 - 10
of 43
pro vyhledávání: '"H R, Levy"'
Publikováno v:
Journal of Biological Chemistry. 266:13028-13034
Amino acid sequencing of glucose 6-phosphate dehydrogenase (Glc6PD) from Leuconostoc mesenteroides yielded sequence for over 75% of the protein. Two oligonucleotides based on the amino acid sequence were used to isolate a partial Glc6PD gene clone (p
Publikováno v:
Journal of Biological Chemistry. 266:5558-5562
Pyridoxal 5'-diphospho-5'-adenosine (PLP-AMP) inhibits glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides competitively with respect to glucose 6-phosphate and noncompetitively with respect to NAD+ or NADP+, with Ki = 40 microM in the N
Autor:
Shoba Ragunathan, H. R. Levy
Publikováno v:
Archives of biochemistry and biophysics. 310(2)
An NAD-preferring glucose 6-phosphate dehydrogenase of Acetobacter hansenii (formerly known as Acetobacter xylinum) has been purified to apparent homogeneity and kinetically characterized. The purified enzyme was stabilized by the use of glycerol, Mg
Publikováno v:
Protein science : a publication of the Protein Society. 1(3)
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
Publikováno v:
The Journal of biological chemistry. 266(20)
Amino acid sequencing of glucose 6-phosphate dehydrogenase (Glc6PD) from Leuconostoc mesenteroides yielded sequence for over 75% of the protein. Two oligonucleotides based on the amino acid sequence were used to isolate a partial Glc6PD gene clone (p
Publikováno v:
The Journal of biological chemistry. 266(9)
Pyridoxal 5'-diphospho-5'-adenosine (PLP-AMP) inhibits glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides competitively with respect to glucose 6-phosphate and noncompetitively with respect to NAD+ or NADP+, with Ki = 40 microM in the N
Publikováno v:
Archives of Biochemistry and Biophysics. 264:93-102
Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides is inactivated by trypsin, chymotrypsin, pronase E, thermolysin, 4.0 m urea, and by heating to 49 °C. It is protected, to varying degrees, against all these forms of inactivation by gl
Publikováno v:
Journal of Biological Chemistry. 262:1223-1229
Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides is irreversibly inactivated by the 2,3'-dialdehyde of NADP+ (oNADP+) in the absence of substrate. The inactivation is first order with respect to NADP+ concentration and follows saturat
Publikováno v:
Journal of Biological Chemistry. 252:3745-3751
Autor:
Ghaleb Daouk, H R Levy
Publikováno v:
Journal of Biological Chemistry. 254:4843-4847
A method is described which enables one to assay simultaneously the NAD- and NADP-linked reactions of dehydrogenases which can utilize both coenzymes. The method is based on the fact that the thionicotinamide analogs of NADH and NADPH absorb light ma