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Substrate inhibition of cruzipain is not affected by the C‐terminal domain
Author(s) -
Stoka Veronika,
McKerrow James H,
Cazzulo Juan José,
Turk Vito
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00532-8
Subject(s) - terminal (telecommunication) , substrate (aquarium) , chemistry , biochemistry , biology , computer science , telecommunications , ecology
Endogenous and recombinant cruzipain, the major cysteine proteinase from the protozoan parasite Trypanosoma cruzi , exhibit differences in the protein and circular dichroism spectra probably attributed to the absence of the C‐terminal domain in the recombinant enzyme. Substrate hydrolysis of both molecules at 25°C and neutral pH obeyed Michaelis‐Menten kinetics whereas significant substrate inhibition was observed above neutral pH. The results suggest that substrate inhibition of cruzipain is pH‐dependent, and that the C‐terminal domain does not play an essential role in this process.