Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis.
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Using the known three-dimensional structures of the zinc metallopeptidases carboxypeptidase A and thermolysin, the two enzymes are compared by superimposing one active site upon the other and identifying corresponding structural and functional elements. The overall folding of the respective enzymes is quite different, but the active sites have several features in common, and the modes of bindin...
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Competitive inhibition as a function of pH for the metalloendoprotease thermolysin by derivatives of L-alpha-(2-hydroxyphenyl)benzenepropanoyl-L- tryptophanylglycylglycine exhibits a diagnostic bell shape. Binding is maximal between two pKa values: on the acidic limb the apparent Ki value is regulated by an unchanging enzymic ionization (pKa 5.3) which is also seen in the substrate-hydrolysis k...
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The modes of binding to thermolysin of two phosphonamidate peptide inhibitors, carbobenzoxy-GlyP-L-Leu-L-Leu (ZGPLL) and carbobenzoxy-L-PheP-L-Leu-L-Ala (ZFPLA), have been determined by X-ray crystallography and refined at high resolution to crystallographic R-values of 17.7% and 17.0%, respectively. (GlyP is used to indicate that the trigonal carbon of the peptide linkage is replaced by the te...
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عنوان ژورنال:
- Biochemistry
دوره 20 24 شماره
صفحات -
تاریخ انتشار 1981