Lysine 238 Is an Essential Residue for α,β-Elimination Catalyzed by Treponema denticola Cystalysin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference30 articles.
1. Crystal structure of cystalysin from Treponema denticola: a pyridoxal 5'-phosphate-dependent protein acting as a haemolytic enzyme
2. Spectroscopic and Kinetic Analyses Reveal the Pyridoxal 5‘-Phosphate Binding Mode and the Catalytic Features of Treponema denticola Cystalysin
3. The 46-kilodalton-hemolysin gene from Treponema denticola encodes a novel hemolysin homologous to aminotransferases
4. Effect of substitution of a pyridoxal phosphate-binding lysyl residue of thermostable D-amino acid aminotransferase by arginine and alanine
5. Lysine 87 in the beta subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transimination, catalysis, and product release.
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