Investigation of the functional role of tryptophan-22 in Escherichia coli dihydrofolate reductase by site-directed mutagenesis

We have applied site-directed mutagenesis methods to change the conserved tryptophan-22 in the substrate binding site of Escherichia coli dihydrofolate reductase to phenylalanine (W22F) and histidine (W22H). The crystal structure of the W22F mutant in a binary complex with the inhibitor methotrexate...

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Veröffentlicht in:	Biochemistry (Easton) 1991-11, Vol.30 (46), p.11092-11103
Hauptverfasser:	Warren, Mark S, Brown, Katherine A, Farnum, Martin F, Howell, Elizabeth E, Kraut, Joseph
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacteriology Biological and medical sciences Coenzymes - chemistry Deuterium Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Histidine - chemistry Histidine - genetics Histidine - physiology Hydrogen-Ion Concentration Kinetics Metabolism. Enzymes Methotrexate - chemistry Microbiology Mutagenesis, Site-Directed NADP - metabolism Protein Binding site-directed mutagenesis Structure-Activity Relationship Substrate Specificity Tetrahydrofolate Dehydrogenase - chemistry Tetrahydrofolate Dehydrogenase - genetics Tetrahydrofolate Dehydrogenase - physiology Tryptophan - chemistry Tryptophan - genetics Tryptophan - physiology
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