H. Hayashi

Effects of replacement of tryptophan-140 by phenylalanine or glycine on the function of Escherichia coli aspartate aminotransferase.

H. Hayashi, H. Kagamiyama, Y. Morino, 1990, Biochemical and biophysical research communications.

Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme.

I. Miyahara, H. Hayashi, H. Kagamiyama, 2001, Biochemistry.

Transient-state kinetics of the reaction of aspartate aminotransferase with aspartate at low pH reveals dual routes in the enzyme-substrate association process.

H. Hayashi, H. Kagamiyama, H. Hayashi, 1997, Biochemistry.

Site-directed mutagenesis of the histamine H1 receptor: roles of aspartic acid107, asparagine198 and threonine194.

H Hayashi, H. Hayashi, H. Kagamiyama, 1994, Biochemical and biophysical research communications.

Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase.

I. Miyahara, H. Hayashi, H. Kagamiyama, 2001, Biochemistry.

Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity.

H. Hayashi, H. Kagamiyama, Y. Morino, 1990, Biochemistry.

Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network.

H Hayashi, A. Okamoto, H. Hayashi, 1998, Journal of molecular biology.