alpha-chymotrypsin has been researched along with maleic-acid* in 1 studies
1 other study(ies) available for alpha-chymotrypsin and maleic-acid
| Article | Year |
|---|---|
A low-barrier hydrogen bond in the catalytic triad of serine proteases.
Spectroscopic properties of chymotrypsin and model compounds indicate that a low-barrier hydrogen bond participates in the mechanism of serine protease action. A low-barrier hydrogen bond between N delta 1 of His57 and the beta-carboxyl group of Asp102 in chymotrypsin can facilitate the formation of the tetrahedral adduct, and the nuclear magnetic resonance properties of this proton indicate that it is a low-barrier hydrogen bond. These conclusions are supported by the chemical shift of this proton, the deuterium isotope effect on the chemical shift, and the properties of hydrogen-bonded model compounds in organic solvents, including the hydrogen bond in cis-urocanic acid, in which the imidazole ring is internally hydrogen-bonded to the carboxyl group. Topics: Aspartic Acid; Catalysis; Chymotrypsin; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Maleates; Malonates; Serine; Serine Endopeptidases; Temperature; Urocanic Acid | 1994 |