Radiation damage at the active site of human alanine:glyoxylate aminotransferase reveals that the cofactor position is finely tuned during catalysis
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-017-11948-w.pdf
Reference32 articles.
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4. Hayashi, H. et al. Strain and catalysis in aspartate aminotransferase. Biochim. Biophys. Acta - Proteins Proteomics 1647, 103–109 (2003).
5. Hayashi, H., Mizuguchi, H. & Kagamiyama, H. The imine-pyridine torsion of the pyridoxal 5′-phosphate schiff base of aspartate aminotransferase lowers its pK(a) in the unliganded enzyme and is crucial for the successive increase in the pK(a) during catalysis. Biochemistry 37, 15076–15085 (1998).
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