Kinetic studies of the binding of inhibitors to thermolysin
| Autor: | James Hoeferlin, Joe Murphy, Roger Rowlett, Susan B. Smith |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Alanine
Steric effects chemistry.chemical_classification Binding Sites Chemical Phenomena Correlation coefficient Stereochemistry Thermolysin Biophysics Substituent Hydrogen-Ion Concentration Kinetic energy Biochemistry Amino acid Chemistry Kinetics chemistry.chemical_compound Residue (chemistry) chemistry Molecular Biology Mathematics Protein Binding |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(80)90444-0 |
| Popis: | The K I values for inhibition of thermolysin activity by N -β-phenylpropionyl-aliphatic amino acids (Gly, Ala, Val, Leu, Ile) are correlated by π, the hydrophobic substituent parameter for the amino acid side chain (log K I = −0.73 π −1.80, correlation coefficient = 0.990). By contrast, the K I values for the corresponding benzyloxycarbonyl amino acids are poorly correlated by π, but show a good correlation with the steric parameter E s (log K I = 0.880 E s − 3.086, correlation coefficient = 0.985). Binding of β-phenylpropionyl- l -alanine is associated with an acidic residue of p K 7.3 and a basic residue of p K 8.0 in the E · I complex, and appears to raise the p K of Glu-143 by 2 units. Binding of benzyloxycarbonyl-Ala and -Phe is associated with an acidic residue of p K 8.0 and two basic residues, both with p K 8.3. Three similar p K values are observed with benzyloxycarbonyl-Phe. These results are interpreted in terms of different modes of binding of β-phenylpropionyl and benzyloxycarbonyl inhibitors. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|