Investigation of the ATP Binding Site ofEscherichia coliAminoimidazole Ribonucleotide Synthetase Using Affinity Labeling and Site-Directed Mutagenesis†

Biochemistry ◽  
1999 ◽  
Vol 38 (31) ◽  
pp. 9831-9839 ◽  
Author(s):  
E. J. Mueller ◽  
S. Oh ◽  
E. Kavalerchik ◽  
T. J. Kappock ◽  
E. Meyer ◽  
...  
Keyword(s):  
Binding Site ◽  
Site Directed Mutagenesis ◽  
Affinity Labeling ◽  
Directed Mutagenesis ◽  
Atp Binding ◽  
Atp Binding Site

ATP-Binding Site of Human Brain Hexokinase As Studied by Molecular Modeling and Site-Directed Mutagenesis†

Biochemistry ◽  
1996 ◽  
Vol 35 (40) ◽  
pp. 13157-13164 ◽  
Author(s):  
Chenbo Zeng ◽  
Alexander E. Aleshin ◽  
Jason B. Hardie ◽  
Robert W. Harrison ◽  
Herbert J. Fromm
Keyword(s):  
Molecular Modeling ◽  
Human Brain ◽  
Binding Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Atp Binding ◽  
Atp Binding Site

Studies on the ATP-binding Site of Actin Using Site-directed Mutagenesis

1997 ◽  
pp. 261-264
Author(s):  
Herwig Schüler ◽  
Elena Korenbaum ◽  
Uno Lindberg ◽  
Roger Karlsson
Keyword(s):  
Binding Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Atp Binding ◽  
Atp Binding Site

scholarly journals Identification of Functional Amino Acids in the Macrolide 2′-Phosphotransferase II

1999 ◽  
Vol 43 (8) ◽  
pp. 2063-2065 ◽  
Author(s):  
Kazuo Taniguchi ◽  
Akio Nakamura ◽  
Kazue Tsurubuchi ◽  
Aki Ishii ◽  
Koji O’Hara ◽  
...  
Keyword(s):  
Amino Acids ◽  
Binding Site ◽  
Site Directed Mutagenesis ◽  
Macrolide Antibiotics ◽  
Directed Mutagenesis ◽  
Atp Binding ◽  
Atp Binding Site ◽  
Mutant Strains

ABSTRACT Macrolide 2′-phosphotransferase [MPH(2′)] transfers the γ phosphate of ATP to the 2′-OH group of macrolide antibiotics. The role of aspartic acids in the putative ATP-binding site of MPH(2′)II was investigated through the substitution of alanine for aspartate by site-directed mutagenesis. D200A, D209A, D219A, and D231A mutant strains were unable to inactivate the substrate oleandomycin, while a D227A mutant retained 7% of the activity of the original enzyme.

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