Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?
Alber
T C
TC
Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.
Davenport
R C
RC
Giammona
D A
DA
Lolis
E
E
Petsko
G A
GA
Ringe
D
D
D001665:Binding Sites; D002238:Carbohydrate Epimerases / Q000235:genetics*; D002384:Catalysis; D003461:Crystallography; D007700:Kinetics; D008958:Models, Molecular; D009154:Mutation; D011485:Protein Binding; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D014305:Triose-Phosphate Isomerase / Q000235:genetics* / Q000378:metabolism
D002238:Carbohydrate Epimerases; D014305:Triose-Phosphate Isomerase