Protonation state of the active-site Schiff base of aromatic amino acid aminotransferase: modulation by binding of ligands and implications for its role in catalysis.

doi:10.1093/oxfordjournals.jbchem.a124293

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Article

Protonation state of the active-site Schiff base of aromatic amino acid aminotransferase: modulation by binding of ligands and implications for its role in catalysis.

Journal of biochemistry - 1 Jan 1994

Iwasaki M, Hayashi H, Kagamiyama H

Abstract excerpt

The Schiff base formed between Lys258 of Escherichia coli aromatic amino acid aminotransferase (ArAT) and the coenzyme pyridoxal 5'-phosphate (PLP) has a pKa value of 6.65. The pH dependency of the kinetic parameters was consistent with a mechanism by which the enzymatic form with the nonprotonat...

Topics

Base Sequence
Binding Sites
Catalysis
Escherichia coli
Hydrogen-Ion Concentration
Kinetics
Ligands
Models, Chemical
Molecular Sequence Data
Mutation
Protons
Schiff Bases
Transaminases

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