The roles of Ser-36, Asp-132 and Asp-201 in the reaction of Pseudomonas fluorescens Kynureninase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry
Reference32 articles.
1. Kynureninases: enzymological properties and regulation mechanism;Soda;Adv. Enzymol. Relat. Areas Mol. Biol.,1979
2. The catalytic mechanism of kynureninase from Pseudomonas fluorescens: insights from the effects of pH and isotopic substitution on steady-state and pre-steady-state kinetics;Koushik;Biochemistry,1998
3. The catalytic mechanism of kynureninase from Pseudomonas fluorescens: evidence for transient quinonoid and ketimine intermediates from rapid-scanning stopped-flow spectrophotometry;Phillips;Biochemistry,1998
4. Aspartic acid 214 in Citrobacter freundii tyrosine phenol-lyase ensures sufficient C–H-acidity of the external aldimine intermediate and proper orientation of the cofactor at the active site;Demidkina;Biochim. Biophys. Acta (BBA) - Protein Proteomics,2006
5. Crystal structure of Citrobacter freundii Asp214Ala tyrosine phenol-lyase reveals that Asp214 is critical for maintaining a strain in the internal Aldimine;Milić;Croat. Chem. Acta,2012
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