(Q27704850)

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Structural plasticity broadens the specificity of an engineered protease

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Structural plasticity broadens the specificity of an engineered protease (English)

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author name string

R Bone

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J L Silen

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D A Agard

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18 May 1989

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339

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6221

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191-5

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Recruitment of substrate-specificity properties from one enzyme into a related one by protein engineering

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Probing steric and hydrophobic effects on enzyme-substrate interactions by protein engineering

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A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework

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Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis.

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Refined structure of alpha-lytic protease at 1.7 A resolution. Analysis of hydrogen bonding and solvent structure

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Molecular structure of the α-lytic protease from Myxobacter 495 at 2·8 Å resolution

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Mechanism of action of serine proteases: tetrahedral intermediate and concerted proton transfer

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Catalytic mechanism of serine proteases: reexamination of the pH dependence of the histidyl 1J13C2-H coupling constant in the catalytic triad of alpha-lytic protease

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High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. II. Polarization of histidine 57 by substrate analogues and competitive inhibitors.

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Serine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid

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On the size of the active site in proteases. I. Papain

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Active site of alpha-lytic protease: enzyme-substrate interactions

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Kinetic properties of the binding of alpha-lytic protease to peptide boronic acids

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The influence of the geometric properties of the active centre on the specificity of α‐chymotrypsin catalysis

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Active site mapping of the serine proteases human leukocyte elastase, cathepsin G, porcine pancreatic elastase, rat mast cell proteases I and II. Bovine chymotrypsin A alpha, and Staphylococcus aureus protease V-8 using tripeptide thiobenzyl ester s

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Analytical molecular surface calculation

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Solvent-accessible surfaces of proteins and nucleic acids

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Analysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity

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Cassette mutagenesis: an efficient method for generation of multiple mutations at defined sites

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Carbon nuclear magnetic resonance studies of the histidine residue in alpha-lytic protease. Implications for the catalytic mechanism of serine proteases.

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17 The kinetics of reversible tight-binding inhibition

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Identifiers

10.1038/339191A0

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