Substrate inhibition of cruzipain is not affected by the C‐terminal domain

FEBS Letters

McKerrow, James H³  Cazzulo, Juan José¹  Turk, Vito²  Stoka, Veronika² 

[1] Instituto de Investigaciones Biotecnológicas, Universidad Nacional de General San Martı́n, Casilla de Correo 30, 1650 San Martı́n, Buenos Aires, Argentina;Department of Biochemistry and Molecular Biology, J. Stefan Institute, Jamova 39, Sl-1000 Ljubljana, Slovenia;Department of Pathology, University of California, San Francisco, CA 94143-0446, USA

关键词: Cruzipain;    Cysteine proteinase;    Substrate inhibition;    C-terminal domain;    Substrate specificity;    Trypanosoma cruzi;    CD;    circular dichroism;    EDTA;    ethylenediaminetetraacetic acid;    E-64;    1-[l-N-(trans-epoxysuccinyl)leucyl]amino-4-guanidinobutane;    HEPES;    N-(2-hydroxyethyl)piperazine-N′-(2-ethanesulfonic acid);    MCA;    4-methyl-7-coumarylamide;    Z;    benzyloxycarbonyl;   

DOI  :  10.1016/S0014-5793(98)00532-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown