Release of enzyme strain during catalysis reduces the activation energy barrier
Author:
Publisher
Wiley
Subject
Materials Chemistry,General Chemical Engineering,Biochemistry,General Chemistry
Reference32 articles.
1. 1985. In Transaminases Eds.; John Wiley and Sons: New York p 37.
2. Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure
3. The Imine−Pyridine Torsion of the Pyridoxal 5‘-Phosphate Schiff Base of Aspartate Aminotransferase Lowers Its pKa in the Unliganded Enzyme and Is Crucial for the Successive Increase in the pKa during Catalysis
4. Pyridoxal Enzymes: Mechanistic Diversity and Uniformity
5. 1985. In Transaminases Eds.; John Wiley and Sons: New York p 109.
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