Site-directed mutagenesis of rat liver NAD(P)H: quinone oxidoreductase: Roles of lysine 76 and cysteine 179

1992 ◽  
Vol 294 (2) ◽  
pp. 434-439 ◽  
Author(s):  
Qiang Ma ◽  
Kunyuan Cui ◽  
Regina W. Wang ◽  
Anthony Y.H. Lu ◽  
Chung S. Yang
Keyword(s):  
Rat Liver ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Quinone Oxidoreductase

Rat liver NAD(P)H:quinone oxidoreductase: cDNA expression and site-directed mutagenesis

1990 ◽  
Vol 169 (3) ◽  
pp. 1087-1093 ◽  
Author(s):  
Gerald L. Forrest ◽  
Jin Qian ◽  
Jian-Xing Ma ◽  
William D. Kaplan ◽  
Steve Akman ◽  
...  
Keyword(s):  
Rat Liver ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Cdna Expression

scholarly journals Expression and site-directed mutagenesis of hepatic glucokinase

1991 ◽  
Vol 277 (1) ◽  
pp. 159-163 ◽  
Author(s):  
A J Lange ◽  
L Z Xu ◽  
F Van Poelwijk ◽  
K Lin ◽  
D K Granner ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Rat Liver ◽  
Crystallographic Data ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Catalytic Residue ◽  
Base Catalyst ◽  
Wild Type ◽  
Similar Role ◽  
Yeast Hexokinase

Soluble rat liver glucokinase was expressed at high levels at 22 degrees C in the BL21(DE3)pLysS strain of Escherichia coli. Aspartate-211 of yeast hexokinase has been implicated as a catalytic residue from crystallographic data. The corresponding residue in rat liver glucokinase, aspartate-205, was mutated to alanine and the expressed mutant had 1/500th of the activity of the wild type, with no change in the Km values for glucose or ATP. The results support a role for this residue as a base catalyst in the glucokinase reaction and, most probably, a similar role in the reactions of all members of the hexokinase family.

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