The imine-pyridine torsion of the pyridoxal 5'-phosphate schiff base of aspartate aminotransferase lowers its pK(a) in the unliganded enzyme and is crucial for the successive increase in the pK(a) during catalysis

Biochemistry

Volumn 37, Issue 43, 1998, Pages 15076-15085

  Hayashi, Hideyuki ^a   Mizuguchi, Hiroyuki ^a   Kagamiyama, Hiroyuki ^a  

^a OSAKA MEDICAL COLLEGE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTATE AMINOTRANSFERASE; IMINE; LYSINE; PYRIDINE DERIVATIVE; PYRIDOXAL 5 PHOSPHATE;

ARTICLE; BINDING KINETICS; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME MECHANISM; MOLECULAR INTERACTION; PKA; PRIORITY JOURNAL; SPECTRAL SENSITIVITY; STRUCTURE ANALYSIS;

ALANINE; ASPARTATE AMINOTRANSFERASES; BINDING SITES; CATALYSIS; ENERGY TRANSFER; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; KINETICS; LIGANDS; LYSINE; N-METHYLASPARTATE; PROTEIN CONFORMATION; PROTONS; PYRIDINES; PYRIDOXAL PHOSPHATE; SCHIFF BASES; SPECTROPHOTOMETRY; THERMODYNAMICS;

EID: 0032573119     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi981517e     Document Type: Article

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