Lysine 238 Is an Essential Residue for α,β-Elimination Catalyzed by Treponema denticola Cystalysin

This publication has 31 references indexed in Scilit:

• A Change in the Internal Aldimine Lysine (K42) in O-Acetylserine Sulfhydrylase to Alanine Indicates Its Importance in Transimination and as a General Base Catalyst
  Biochemistry, 1996
• Heme biosynthesis in mammalian systems: Evidence of a schiff base linkage between the pyridoxal 5′‐phosphate cofactor and a lysine residue in 5‐aminolevulinate synthase
  Protein Science, 1993
• Effect of substitution of a pyridoxal phosphate-binding lysyl residue of thermostable D-amino acid aminotransferase by arginine and alanine
  Biochemistry, 1991
• Pyridoxal 5'-phosphate dependent histidine decarboxylase: overproduction, purification, biosynthesis of soluble site-directed mutant proteins and replacement of conserved residues
  Biochemistry, 1989
• Substitution of an arginyl residue for the active site lysyl residue (Lys258) of aspartate aminotransferase
  Biochemical and Biophysical Research Communications, 1987
• Site-directed mutagenesis of aspartate aminotransferase from E. coli
  Biochemical and Biophysical Research Communications, 1985
• Reaction kinetics and equilibriums of .beta.-elimination of some Schiff base complexes
  Journal of the American Chemical Society, 1981
• Catalysis of the .beta. elimination of O-phosphoserine and .beta.-chloroalanine by pyridoxal and zinc(II) ion
  Journal of the American Chemical Society, 1977
• Band-shape analysis and resolution of electronic spectra of pyridoxal phosphate and other 3-hydroxypyridine-4-aldehydes
  Biochimica et Biophysica Acta (BBA) - General Subjects, 1976
• Sodium Cyanoborohydride - A Highly Selective Reducing Agent for Organic Functional Groups
  Synthesis, 1975