Crystallography and mutagenesis of transketolase: mechanistic implications for enzymatic thiamin catalysis.
The ThDP dependent enzyme transketolase is a convenient model system to study enzymatic thiamin catalysis. Crystallographic studies of the enzyme have identified the ThDP binding fold, the V-conformation of ThDP as the relevant conformation in enzymatic catalysis and details of enzyme-substrate interactions. Based on this structural information, the function of various active site residues in substrate binding and catalysis has been probed by site-directed mutagenesis.
Schneider
G
G
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden. gunter@alfa.mbb.ki.se
Lindqvist
Y
Y
D001051:Apoenzymes / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D004789:Enzyme Activation; D008958:Models, Molecular; D009154:Mutation; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013831:Thiamine / Q000378:metabolism*; D013835:Thiamine Pyrophosphate / Q000378:metabolism; D014174:Transketolase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D001051:Apoenzymes; D014174:Transketolase; D013835:Thiamine Pyrophosphate; D013831:Thiamine