Effect of P2' substituents on kinetic constants for hydrolysis by cysteine proteinases.

Abstract:

:Intramolecularly quenched fluorogenic peptide substrates with the general sequence: DABCYL-Lys-Phe-Gly-Gly-Xxx-Ala-EDANS have been utilized to explore the effect of the hydrophobicity of amino acid side chains in the P2' position on the steady-state kinetic constants for papain catalyzed hydrolysis. The results demonstrate that subsite interactions between the enzyme and the peptide substrate modulate the enzyme specificity by slowing the release of the C-terminal product. This series of substrates can be used to characterize substrate specificity studies of other cysteine proteinases.

authors

García-Echeverría C,Rich DH

doi

10.1016/0006-291x(92)91239-m

subject

Has Abstract

pub_date

1992-09-16 00:00:00

pages

615-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(92)91239-M

journal_volume

187

pub_type

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