Tsang, Wing Y., Ahmed, Naveed, Harding, Lindsay P., Hemming, Karl, Laws, Andrew P. and Page, Michael I. (2005) Acylation versus sulfonylation in the inhibition of elastase by 3-oxo-beta-sultams. Journal of the American Chemical Society, 127 (25). pp. 8946-8947. ISSN 1520-5126Metadata only available from this repository.
-Sultams are the sulfonyl analogues of
-lactams, and 3-oxo- -sultams are both
-lactams and -sultams and, therefore,
susceptible to nucleophilic attack at either
the acyl or the sulfonyl center. They are
novel inactivators of serine enzymes. The
second-order rate constant for the
inactivation of elastase at pH 6 by N-benzyl-4,4-dimethyl-3-oxo- -sultam is 768 M-1 s-1, which is 103-fold greater than However, in contrast to N-acyl -sultams, which sulfonylate the active site serine residue to form a sulfonate ester, 3
acylation followed by slow deacylation to regenerate the active enzyme.
|Additional Information:||Copyright © 2005 American Chemical Society|
|Subjects:||Q Science > Q Science (General)|
Q Science > QD Chemistry
|Schools:||School of Applied Sciences|
School of Applied Sciences > Biomolecular Sciences Research Centre
(1) Baxter, N. J.; Rigoreau, L. J. M.; Laws, A. P.; Page, M. I. J. Am. Chem.
|Depositing User:||Sara Taylor|
|Date Deposited:||08 Feb 2008 09:37|
|Last Modified:||24 Mar 2010 09:20|
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