Site-directed Mutagenesis Provides Insight into Racemization and Transamination of Alanine Catalyzed by Treponema denticola Cystalysin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference23 articles.
1. Cystalysin, a 46-kilodalton cysteine desulfhydrase from Treponema denticola, with hemolytic and hemoxidative activities
2. Spectroscopic and Kinetic Analyses Reveal the Pyridoxal 5‘-Phosphate Binding Mode and the Catalytic Features of Treponema denticola Cystalysin
3. Crystal structure of cystalysin from Treponema denticola: a pyridoxal 5'-phosphate-dependent protein acting as a haemolytic enzyme
4. Lysine 238 Is an Essential Residue for α,β-Elimination Catalyzed by Treponema denticola Cystalysin
5. Treponema denticola cystalysin exhibits significant alanine racemase activity accompanied by transamination: mechanistic implications
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