Treponema denticolacystalysin catalyzes β-desulfination ofL-cysteine sulfinic acid and β-decarboxylation ofL-aspartate and oxalacetate
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Reference24 articles.
1. Crystal structure of cystalysin from Treponema denticola: a pyridoxal 5'-phosphate-dependent protein acting as a haemolytic enzyme
2. Cystalysin, a 46-kilodalton cysteine desulfhydrase from Treponema denticola, with hemolytic and hemoxidative activities
3. Spectroscopic and Kinetic Analyses Reveal the Pyridoxal 5‘-Phosphate Binding Mode and the Catalytic Features of Treponema denticola Cystalysin
4. Treponema denticola cystalysin exhibits significant alanine racemase activity accompanied by transamination: mechanistic implications
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