Inhibition of serine proteases by oxygen, sulfur and selenium dialkyl phosphoryl derivatives: Biochemical and sup 31 P NMR studies
{sup 31}P NMR spectroscopy was employed to investigate the interaction of chymotrypsin with various organophosphorus inhibitors. The {sup 31}P NMR spectrum of diethyl selenophosphoryl chymotrypsin revealed two resonances at approximately 71 ppm and a single resonance at 48 ppm attributed to the covalent and non-covalent enzyme-inhibitor complexes, respectively. The goal of this investigation was to elucidate the basis of the two peaks at {approx}71 ppm in the {sup 31}P NMR spectrum of diethyl selenophosphosphoryl-{alpha}-chymotrypsin. The possibility that the selenium atom in the structure of the organophosphorus inhibitor might have been responsible for the two peaks was addressed by extending the {sup 31}P NMR studies to diethyl thiophosphoryl- and diethyl phosphoryl-{alpha}-chymotrypsin. The fact that the latter modified enzyme derivatives also yielded {sup 31}P NMR spectra that exhibited two resonances assigned to covalent species discounted this possibility. The effect of the alkyl group of the inhibitor on the {sup 31}P NMR spectrum of the enzyme-inhibitor complex was further investigated by examining diisopropyl phosphoryl-{alpha}-chymotrypsin by {sup 31}P NMR spectroscopy.
- Research Organization:
- South Carolina Univ., Columbia, SC (USA)
- OSTI ID:
- 7255455
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
CARBOXYLIC ACIDS
CHYMOTRYPSIN
COMPLEXES
ENZYME INHIBITORS
ENZYMES
HYDROLASES
HYDROXY ACIDS
INHIBITION
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MOLECULAR STRUCTURE
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
NUCLEI
ODD-EVEN NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PHOSPHORUS 31
PHOSPHORUS ISOTOPES
RESONANCE
SERINE
SERINE PROTEINASES
SPECTRA
STABLE ISOTOPES
TRACER TECHNIQUES