Inactivation of carboxypeptidase Y by mutational removal of the putative essential histidyl residue
Author:
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,General Medicine
Link
http://link.springer.com/content/pdf/10.1007/BF02904470.pdf
Reference36 articles.
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3. Betzel, C., G.P. Pal, M. Struck, K.-D. Jany &W. Saenger: Active-site geometry of proteinase K. Crystallographic study of its complex with a dipeptide chloromethyl ketone inhibitor. FEBS Lett. 197, 105–110(1986)
4. Betzel, C., G.P. Pal &W. Saenger: Three-dimensional structure of proteinase K at 0.15-nm resolution. Eur. J. Biochem. 178, 155–171 (1988)
5. Breddam, K.: Modification of the single sulfhydryl group of carboxypeptidase Y with mercurials. Influence on enzyme specificity. Carlsberg Res. Commun. 48, 9–19(1983)
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