A Covalent Enzyme-Substrate Intermediate with Saccharide Distortion in a Mutant T4 Lysozyme
Author:
Affiliation:
1. Institute of Molecular Biology, Howard Hughes Medical Institute, University of Oregon, Eugene, OR 97403 and Department of Physics, University of Oregon, Eugene, OR 97403.
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
Reference35 articles.
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2. BELL, J.A., COMPARISON OF THE CRYSTAL-STRUCTURE OF BACTERIOPHAGE T4-LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS, PROTEINS-STRUCTURE FUNCTION AND GENETICS 10: 10 (1991).
3. BLAKE, CCF, STRUCTURE OF HEN EGG-WHITE LYSOZYME - A 3-DIMENSIONAL FOURIER SYNTHESIS AT 2A RESOLUTION, NATURE 206: 757 (1965).
4. DAHLQUIST, F.W., STEREOSPECIFICITY OF HUMAN HEN AND PAPAYA LYSOZYMES, BIOCHEMISTRY 8: 694 (1969).
5. GEBLER, J.C., GLU-537, NOT GLU-461, IS THE NUCLEOPHILE IN THE ACTIVE-SITE OF (LAC-Z) BETA-GALACTOSIDASE FROM ESCHERICHIA-COLI, JOURNAL OF BIOLOGICAL CHEMISTRY 267: 11126 (1992).
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