Direct evidence for the exploitation of an .alpha.-helix in the catalytic mechanism of triosephosphate isomerase

In previous work, we have shown that the first (and, presumably, the second) pKa of the active-site histidine-95 in triosephosphate isomerase has been lowered by about 2 units [Lodi, P. J., & Knowles, J. R. (1991) Biochemistry 30, 6948-6956]. One reason for the perturbed pKa of this residue appe...

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Bibliographic Details
Published in:	Biochemistry (Easton) Vol. 32; no. 16; pp. 4338 - 4343
Main Authors:	Lodi, Patricia J, Knowles, Jeremy R
Format:	Journal Article
Language:	English
Published:	Washington, DC American Chemical Society 27-04-1993
Subjects:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Base Sequence Binding Sites Biological and medical sciences Cloning, Molecular Enzymes and enzyme inhibitors Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Genetic Vectors Histidine Hydrogen-Ion Concentration Isomerases Kinetics Magnetic Resonance Spectroscopy - methods Models, Structural Molecular Sequence Data Mutagenesis, Site-Directed Oligodeoxyribonucleotides Protein Folding Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - metabolism Saccharomyces cerevisiae - enzymology Thermodynamics Triose-Phosphate Isomerase - chemistry Triose-Phosphate Isomerase - genetics Triose-Phosphate Isomerase - metabolism Enzymatic activity Enzyme Active site Triosephosphate isomerase Reaction mechanism Helical structure Catalysis
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