Transition state stabilization by chloramphenicol acetyltransferase. Role of a water molecule bound to threonine 174.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. PRINCIPLES THAT DETERMINE THE STRUCTURE OF PROTEINS
2. Initial Steady State Velocities in the Evaluation of Enzyme-Coenzyme-Substrate Reaction Mechanisms.
3. Substrate binding to chloramphenicol acetyltransferase: evidence for negative cooperativity from equilibrium and kinetic constants for binary and ternary complexes
4. Solvent structure in crystals of trypsin determined by X-ray and neutron diffraction
5. The molecular mass and trimeric nature of chloramphenicol transacetylase
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4. Structures of chloramphenicol acetyltransferase III andEscherichia coliβ-ketoacylsynthase III co-crystallized with partially hydrolysed acetyl-oxa(dethia)CoA;Acta Crystallographica Section F Structural Biology Communications;2023-02-23
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