Site-directed mutagenesis of Tyr354 in Geobacillus stearothermophilus alanine racemase identifies a role in controlling substrate specificity and a possible role in the evolution of antibiotic resistance.
Patrick
Wayne M
WM
Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, (UK).
Weisner
Jan
J
Blackburn
Jonathan M
JM
D000409:Alanine / Q000378:metabolism; D000411:Alanine Racemase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001406:Bacillaceae / Q000201:enzymology*; D001665:Binding Sites; D024881:Drug Resistance, Bacterial / Q000235:genetics*; D007700:Kinetics; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D010710:Phosphates / Q000378:metabolism; D019998:Racemases and Epimerases / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014443:Tyrosine / Q000235:genetics / Q000378:metabolism*; D000099300:Serine Racemase
D000409:Alanine; D000411:Alanine Racemase; D010710:Phosphates; D019998:Racemases and Epimerases; D014443:Tyrosine; D000099300:Serine Racemase