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7600 Biochemistry 1989, 28, 7600-7609 Sugio, S.,Oka, K., Ohishi, H., Tomita, K., & Saenger, W.
 

Summary: 7600 Biochemistry 1989, 28, 7600-7609
Sugio, S.,Oka, K., Ohishi, H., Tomita, K., & Saenger, W.
Sugio, S., Amisaki, T., Ohishi, H., & Tomita, K. (1988) J.
Wlodawer, A., Miller, M., & Sjolin, L. (1983) Proc. Natl.
Yu, H.-A., Karplus, M., & Hendrickson, W. A. (1985) Acta
(1985b) FEBS Lett. 183, 115-118.
Biochem. 103, 354-366.
Acad. Sci. U.S.A.80, 3628-3631.
Crystallogr. B41, 191-20 1.
Structural Analysis of Specificity: a-Lytic Protease Complexes with Analogues of
Reaction Intermediates+?$
Roger Bone,! Dan Frank, Charles A. Kettner," and David A. Agard*Vg
Department of Biochemistry and Biophysics and The Howard Hughes Medical Institute,
University of California at San Francisco, San Francisco, California 94143-0448, and Central Research and Development
Department, Experimental Station, E. I. du Pont de Nemours and Company, Inc., Wilmington, Delaware 19898
Received December 27, 1988; Revised Manuscript Received May 10, 1989
ABSTRACT: To better understand the structural basis of enzyme specificity, the structures of complexes formed
between a-lytic protease, an extracellular serine protease of Lysobacter enzymogenes, and five inhibitory
peptide boronic acids (R2-boroX, where R2is methoxysuccinyl-Ala-Ala-Pro-and boroX is the a-aminoboronic
acid analogue of Ala, Val, Ile, Norleu, or Phe) have been studied at high resolution by X-ray crystallography.

  

Source: Agard, David - Department of Biochemistry and Biophysics, University of California at San Francisco

 

Collections: Biotechnology; Biology and Medicine