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Kinetic studies of pepsin active site model compound and porcine pepsin
Author(s) -
Swoboda Bogdan,
BełtowskaBrzezinska Maria,
Schroeder Grzegorz,
Brzezinski Bogumil,
Zundel Georg
Publication year - 2001
Publication title -
journal of physical organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.325
H-Index - 66
eISSN - 1099-1395
pISSN - 0894-3230
DOI - 10.1002/1099-1395(200102)14:2<103::aid-poc342>3.0.co;2-6
Subject(s) - chemistry , pepsin , hydrolysis , substrate (aquarium) , cleavage (geology) , active site , stereochemistry , kinetics , chromatography , enzyme , fumaric acid , organic chemistry , oceanography , physics , geotechnical engineering , quantum mechanics , fracture (geology) , engineering , geology
The kinetic parameters for the hydrolysis of the heptapeptide Pro–Thr–Glu–Phe‐(4‐NO 2 )Phe–Arg–Leu by the pepsin model compound tetrabutylammonium monosalt of m ‐aminobenzoic acid diamide of fumaric acid (TBA m ‐FUM) and porcine pepsin were determined using a spectrophotometric technique. According to the Δ S ≠ values obtained, in the transition state the inner motion in the TBA m ‐FUM–heptapeptide complex is more restricted than that in the pepsin–heptapeptide complex. The model compound TBA m ‐FUM can cause a cleavage of the Phe—(4‐NO 2 )Phe bond in the substrate molecules following a mechanism similar as that suggested for pepsin, but its catalytic activity is much lower. Copyright © 2001 John Wiley & Sons, Ltd.