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(Received for publication, July 5, 1995) The catalytic efficiency of the mature HSV-1 protease has been
examined as a function of solvent composition. With the peptide
substrate HTYLQASEKFKMWG-amide, the specificity constant (k
Volume 270,
Number 39,
Issue of September 29, pp. 22697-22700, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
/K
) at pH 7.5
for cleavage is 5.2 M
s
.
This value increases to 38 M
s
when 25% glycerol is present in the reaction mixture. It was
found that glycerol activation is but one case of the general
phenomenon of HSV-1 protease activation by kosmotropes, or water
structure-forming cosolvents. For example, an 860-fold increase in the
protease activity (k
/K
= 4500 M
s
) occurs in the presence of 0.8 M sodium citrate. Similarly, the presence of 0.8 M sodium
phosphate activates the catalytic efficiency by 420-fold (k
/K
= 2200 M
s
). The extent of
HSV-1 protease activation by various anions correlates with the
Hofmeister series. Both the susceptibility to proteolysis by trypsin
and the protein fluorescence spectra of the HSV-1 protease change in
the presence of activating solvents, suggesting a conformational change
accompanying activation.
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