H. Kagamiyama

发表

A Genetic Approach to Visualization of Multisynaptic Neural Pathways Using Plant Lectin Transgene

H. Okano, K. Mori, T. Noda, 1999, Neuron.

Activation of protein phosphatase 2A by cAMP‐dependent protein kinase‐catalyzed phosphorylation of the 74‐kDa B″ (δ) regulatory subunit in vitro and identification of the phosphorylation sites

H. Hayashi, H. Kagamiyama, R. Inoue, 1998, FEBS letters.

Cloning and characterization of the tyrB gene from Salmonella typhimurium.

H. Hayashi, H. Kagamiyama, Y. Nakai, 1996, Biochimica et biophysica acta.

The primary structure of the beta-subunit of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa.

H. Kagamiyama, M. Iwaki, M. Nozaki, 1981, Archives of biochemistry and biophysics.

Nonidentical subunits of pyrocatechase from Pseudomonas arvilla C-1.

H. Kagamiyama, C. Nakai, M. Nozaki, 1979, Archives of biochemistry and biophysics.

Amino acid sequence of fifty two residues from the N-terminus of mitochondrial aspartate aminotransferase.

H. Kagamiyama, H. Wada, 1975, Biochemical and biophysical research communications.

Branched-chain amino acid aminotransferase of Escherichia coli: overproduction and properties.

A. Ikai, H. Kagamiyama, S. Kuramitsu, 1988, Journal of biochemistry.

Crystallization and preliminary X-ray characterization of branched-chain amino acid aminotransferase from Escherichia coli.

H. Kagamiyama, S. Kuramitsu, Y. Matsuura, 1989, Journal of biochemistry.

The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase.

H. Kagamiyama, S. Tanase, Y. Morino, 1991, Journal of Biological Chemistry.

Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.

H. Kagamiyama, S. Tanase, Y. Morino, 1992, Biochemistry.

Three Isozymes of Catechol 1,2-Dioxygenase (Pyrocatechase) from Pseudomonas arvilla C-1

H. Kagamiyama, S. Kuramitsu, K. Horiike, 1990 .

Nuclear Localization of Yeast Nfs1p Is Required for Cell Survival*

H. Hayashi, H. Kagamiyama, M. Nakai, 2001, Journal of Biological Chemistry.

Introduction and implementation of problem-solving lectures for instruction in medical biochemistry at Osaka University Medical School in Japan

H. Kagamiyama, N. Taniguchi, T. Higashi, 1991 .

Complete nucleotide sequence of the metapyrocatechase gene on the TOI plasmid of Pseudomonas putida mt-2.

H. Kagamiyama, A. Nakazawa, Y. Ebina, 1983, The Journal of biological chemistry.

Molecular cloning and nucleotide sequence of the cDNA for rat peroxisomal enoyl-CoA: hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme.

H. Kagamiyama, M. Hijikata, S. Miyazawa, 1985, The Journal of biological chemistry.

ADP-ribosylation of histone H1. Identification of glutamic acid residues 2, 14, and the COOH-terminal lysine residue as modification sites.

H. Kagamiyama, O. Hayaishi, K. Ueda, 1980, The Journal of biological chemistry.

Redesigning the Substrate Specificity of an Enzyme by Cumulative Effects of the Mutations of Non-active Site Residues*

A. Okamoto, H. Kagamiyama, T. Yano, 1999, The Journal of Biological Chemistry.

[Arg292----Val] or [Arg292----Leu] mutation enhances the reactivity of Escherichia coli aspartate aminotransferase with aromatic amino acids.

H. Hayashi, H. Kagamiyama, Y. Morino, 1989, Biochemical and biophysical research communications.

Substitution of a lysyl residue for arginine 386 of Escherichia coli aspartate aminotransferase.

H. Kagamiyama, S. Tanase, Y. Morino, 1989, The Journal of biological chemistry.

A hydrogen-bonding network modulating enzyme function: asparagine-194 and tyrosine-225 of Escherichia coli aspartate aminotransferase.

H. Kagamiyama, T. Yano, T. Mizuno, 1993, Biochemistry.

Rat liver aromatic L-amino acid decarboxylase: spectroscopic and kinetic analysis of the coenzyme and reaction intermediates.

H. Hayashi, H. Kagamiyama, H. Mizuguchi, 1993, Biochemistry.

Control of cell-cycle-associated tetrahydrobiopterin synthesis in rat thymocytes.

T. Werner, H. Kagamiyama, J. Maier, 1992, Experimental cell research.

Three isozymes of catechol 1,2-dioxygenase (pyrocatechase), alpha alpha, alpha beta, and beta beta, from Pseudomonas arvilla C-1.

H. Kagamiyama, S. Kuramitsu, K. Horiike, 1990, The Journal of biological chemistry.

Nonidentical subunits of protocatechuate 3,4-dioxygenase.

H. Kagamiyama, Y. Saeki, R. Yoshida, 1976, Biochemistry.

Purification, subunit structure, and partial amino acid sequence of metapyrocatechase.

H. Kagamiyama, K. Hori, T. Nakazawa, 1983, The Journal of biological chemistry.

Glucose tolerance factor stimulates 3-O-methylglucose transport into isolated rat adipocytes.

H. Kagamiyama, A. Kashiwagi, M. Mino, 1987, Biochemical and biophysical research communications.

Molecular cloning of a 74-kDa regulatory subunit (B" or delta) of human protein phosphatase 2A.

H. Hayashi, H. Kagamiyama, T. Nagase, 1996, FEBS letters.

Structural analysis of cDNA for rat peroxisomal 3-ketoacyl-CoA thiolase.

H. Kagamiyama, M. Hijikata, T. Hashimoto, 1987, The Journal of biological chemistry.

Complete nucleotide sequence of cDNA and predicted amino acid sequence of rat acyl-CoA oxidase.

H. Kagamiyama, M. Hijikata, T. Hashimoto, 1987, The Journal of biological chemistry.

IMMUNOCHEMICAL DISTINCTION BETWEEN GLUTAMIC-OXALOACETIC TRANSAMINASES FROM THE SOLUBLE AND MITOCHONDRIAL FRACTIONS OF MAMMALIAN TISSUES.

H. Kagamiyama, Y. Morino, H. Wada, 1964, The Journal of biological chemistry.

A phospholipase A2 in the supernatant fraction of rat spleen. Its similarity to rat pancreatic phospholipase A2.

H. Tojo, H. Kagamiyama, S. Kuramitsu, 1988, The Journal of biological chemistry.

Tetrahydrobiopterin synthesis and inducible nitric oxide production in pulmonary artery smooth muscle.

H. Kagamiyama, T. Billiar, D. Geller, 1994, The American journal of physiology.

Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase.

H. Hayashi, H. Kagamiyama, S. Kuramitsu, 1993, Biochemistry.

Three-dimensional structures of aspartate aminotransferase from Escherichia coli and its mutant enzyme at 2.5 A resolution.

A. Okamoto, H. Kagamiyama, S. Kuramitsu, 1990, Journal of biochemistry.

Disruption of Thermus thermophilus genes by homologous recombination using a thermostable kanamycin‐resistant marker

H. Kagamiyama, S. Kuramitsu, T. Yano, 2001, FEBS letters.

Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.

H. Hayashi, H. Kagamiyama, H. Mizuguchi, 1996, Journal of biochemistry.

Use of 1H-15N heteronuclear multiple-quantum coherence NMR spectroscopy to study the active site of aspartate aminotransferase.

I. Miyahara, H. Hayashi, H. Kagamiyama, 1997, Biochemistry.

Molecular cloning and sequence analysis of full-length cDNA for mRNA of adrenodoxin oxidoreductase from bovine adrenal cortex.

H. Murakami, H. Kagamiyama, S. Kuramitsu, 1987, Biochemical and biophysical research communications.

cDNA cloning and expression of pig cytosolic aspartate aminotransferase in Escherichia coli: amino-terminal heterogeneity of expressed products and lack of its correlation with enzyme function.

H. Kagamiyama, T. Tsuzuki, S. Tanase, 1989, Biochemistry.

Complete primary structures of two subunits of purothionin A, a lethal protein for brewer's yeast from wheat flour.

H. Kagamiyama, H. Yoshizumi, T. Okada, 1977, Journal of biochemistry.

Substitution of an arginyl residue for the active site lysyl residue (Lys258) of aspartate aminotransferase.

H. Kagamiyama, S. Tanase, Y. Morino, 1987, Biochemical and biophysical research communications.

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.

Purification and cDNA cloning of rat 6-pyruvoyl-tetrahydropterin synthase.

H. Kagamiyama, T. Harada, Y. Inoue, 1991, The Journal of biological chemistry.

IMP dehydrogenase inhibitors reduce intracellular tetrahydrobiopterin levels through reduction of intracellular GTP levels. Indications of the regulation of GTP cyclohydrolase I activity by restriction of GTP availability in the cells.

H. Kagamiyama, T. Harada, K. Hatakeyama, 1992, The Journal of biological chemistry.

Aromatic L‐amino acid decarboxylase: Conformational change in the flexible region around arg334 is required during the transaldimination process

A. Okamoto, H. Hayashi, H. Kagamiyama, 1998, Protein science : a publication of the Protein Society.

A sensitive method for the detection of aspartate: 2-oxoglutarate aminotransferase activity of polyacrylamide gels.

H. Kagamiyama, T. Yagi, M. Nozaki, 1981, Analytical biochemistry.

Crystallization and properties of aspartate aminotransferase from escherichia coli B

H. Kagamiyama, K. Soda, T. Yagi, 1979, FEBS letters.

Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene.

H. Kagamiyama, T. Ogawa, S. Kuramitsu, 1985, Biochemical and biophysical research communications.

cDNA cloning, expression in Escherichia coli and purification of human 6-pyruvoyl-tetrahydropterin synthase.

H. Kagamiyama, K. Hatakeyama, A. Ashida, 1993, Biochemical and biophysical research communications.

The protective effect of polyriboinosinic acid-polyribocytidylic acid against the occurrence of galactosamine-induced liver cell injury in rat

H. Kagamiyama, Y. Shibayama, S. Sakakibara, 1983, Experientia.

Intensification of galactosamine hepatotoxicity by polyriboinosinic acid-polyribocytidylic acid.

H. Kagamiyama, K. Shiomi, S. Sakakibara, 1985, Life sciences.

[17] Glutamate-aspartate transaminase from microorganisms

H. Kagamiyama, K. Soda, T. Yagi, 1985 .

A new assay for L-aspartate:2-oxoglutarate aminotransferase.

H. Kagamiyama, K. Soda, T. Yagi, 1979, Analytical biochemistry.

Purification and characterization of rat liver GTP cyclohydrolase I. Cooperative binding of GTP to the enzyme.

H. Kagamiyama, Y. Watanabe, S. Suzuki, 1989, The Journal of biological chemistry.

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.

Aspartate transaminase from E. coli: amino acid sequences of the NH2-terminal 33 residues and chymotryptic pyridoxyl tetrapeptide.

H. Kagamiyama, T. Yagi, 1979, Biochemical and biophysical research communications.

Purification and characterization of thermostable aspartate aminotransferase from a thermophilic Bacillus species

H. Kagamiyama, S. Kuramitsu, H. Tanaka, 1990, Journal of bacteriology.

The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes.

H. Kagamiyama, S. Wakabayashi, T. Yagi, 1984, Biochemical and biophysical research communications.

Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization.

A. Okamoto, H. Kagamiyama, S. Kuramitsu, 1991, The Journal of biological chemistry.

The substrate activation process in the catalytic reaction of Escherichia coli aromatic amino acid aminotransferase.

H. Hayashi, H. Kagamiyama, H. Mizuguchi, 2000, Biochemistry.

Strain and catalysis in aspartate aminotransferase.

H. Ikushiro, M. M. Islam, I. Miyahara, 2003, Biochimica et biophysica acta.

Decrease in tetrahydrobiopterin content and neurotransmitter amine biosynthesis in rat brain by an inhibitor of guanosine triphosphate cyclohydrolase

Yasuyoshi Watanabe, H. Kagamiyama, O. Hayaishi, 1988, Brain Research.

Crystallization and some properties of metapyrocatechase.

H. Kagamiyama, O. Hayaishi, M. Nozaki, 1963, Biochemical and biophysical research communications.

Reactions of serine palmitoyltransferase with serine and molecular mechanisms of the actions of serine derivatives as inhibitors.

H. Ikushiro, H. Hayashi, H. Kagamiyama, 2004, Biochemistry.

Conformational Change in Aspartate Aminotransferase on Substrate Binding Induces Strain in the Catalytic Group and Enhances Catalysis*

I. Miyahara, H. Hayashi, H. Kagamiyama, 2003, The Journal of Biological Chemistry.

Release of enzyme strain during catalysis reduces the activation energy barrier.

H. Hayashi, H. Kagamiyama, 2001, Chemical record.

The active site of Paracoccus denitrificans aromatic amino acid aminotransferase has contrary properties: flexibility and rigidity.

A. Okamoto, H. Kagamiyama, S. Ishii, 1999, Biochemistry.

Structures of Escherichia coli branched-chain amino acid aminotransferase and its complexes with 4-methylvalerate and 2-methylleucine: induced fit and substrate recognition of the enzyme.

H. Hayashi, H. Kagamiyama, K. Okada, 2001, Biochemistry.

Paracoccus denitrificans aromatic amino acid aminotransferase: a model enzyme for the study of dual substrate recognition mechanism.

H Hayashi, A. Okamoto, H. Hayashi, 1997, Journal of 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.

Characterization of histidinol phosphate aminotransferase from Escherichia coli.

I. Miyahara, H. Hayashi, H. Kagamiyama, 2003, Biochimica et biophysica acta.

The imine-pyridine torsion of the pyridoxal 5'-phosphate Schiff base of aspartate aminotransferase lowers its pKa in the unliganded enzyme and is crucial for the successive increase in the pKa during catalysis.

H. Hayashi, H. Kagamiyama, H. Mizuguchi, 1998, Biochemistry.

Glutamine:phenylpyruvate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8.

I. Miyahara, H. Hayashi, H. Kagamiyama, 2003, Journal of 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.

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.

X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form.

A. Okamoto, H. Kagamiyama, S. Kuramitsu, 1994, Journal of biochemistry.

METAPYROCATECHASE. I. PURIFICATION, CRYSTALLIZATION AND SOME PROPERTIES.

H. Kagamiyama, O. Hayaishi, M. Nozaki, 1963, Biochemische Zeitschrift.

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.

Amino acid sequence of 37 residues surrounding Nxi-pyridoxyllysine in mitochondrial aspartate aminotransferase.

H. Kagamiyama, H. Wada, K. Teranishi, 1975, Biochemical and biophysical research communications.

Feedback regulation mechanisms for the control of GTP cyclohydrolase I activity.

H. Kagamiyama, T. Harada, K. Hatakeyama, 1993, Science.

Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes.

A. Okamoto, H. Kagamiyama, S. Kuramitsu, 1991, Biochemistry.

Purification and characterization of rho-crystallin from Japanese common bullfrog lens.

H. Hayashi, H. Kagamiyama, Y. Urade, 1990, The Journal of biological chemistry.

S. Nakanishi, H. Kagamiyama, K. Watanabe, 1988, Proceedings of the National Academy of Sciences of the United States of America.

ANALYSIS OF THE PH- AND LIGAND-INDUCED SPECTRAL TRANSITIONS OF TRYPTOPHANASE : ACTIVATION OF THE COENZYME AT THE EARLY STEPS OF THE CATALYTIC CYCLE

H. Ikushiro, H. Hayashi, H. Kagamiyama, 1998 .

An anomalous side reaction of the Lys303 mutant aromatic L-amino acid decarboxylase unravels the role of the residue in catalysis.

H. Hayashi, H. Kagamiyama, S. Ishii, 1997, Journal of biochemistry.

Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure.

H. Kagamiyama, S. Wakabayashi, K. Kondo, 1987, The Journal of biological chemistry.

Cocrystallization of a mutant aspartate aminotransferase with a C5-dicarboxylic substrate analog: structural comparison with the enzyme-C4-dicarboxylic analog complex.

A. Okamoto, H. Kagamiyama, T. Yano, 2000, Journal of biochemistry.

Reaction of aspartate aminotransferase with L-erythro-3-hydroxyaspartate: involvement of Tyr70 in stabilization of the catalytic intermediates.

H. Hayashi, H. Kagamiyama, 1995, Biochemistry.

Aspartate aminotransferase of E. coli: effects of site-directed mutagenesis on substrate recognition.

H. Kagamiyama, 1992, Journal of nutritional science and vitaminology.

The chemical structure of tryptophanase from Escherichia coli. 3. Isolation and amino acid sequence of the tryptic peptides.

H. Kagamiyama, H. Matsubara, E. Snell, 1972, The Journal of biological chemistry.

Bacterial serine palmitoyltransferase: a water-soluble homodimeric prototype of the eukaryotic enzyme.

H. Ikushiro, H. Hayashi, H. Kagamiyama, 2003, Biochimica et biophysica acta.

BIG-1: A new TAG-1/F3-related member of the immunoglobulin superfamily with neurite outgrowth-promoting activity

K. Mori, Y. Yoshihara, M. Kawasaki, 1994, Neuron.

Expression and Purification of Serine Palmitoyltransferase

H. Ikushiro, H. Hayashi, H. Kagamiyama, 2000 .

Crystal Structures of Threonine Synthase from Thermus thermophilus HB8

I. Miyahara, H. Hayashi, H. Kagamiyama, 2003, Journal of Biological Chemistry.

The primary structure of thermostable D-amino acid aminotransferase from a thermophilic Bacillus species and its correlation with L-amino acid aminotransferases.

H. Kagamiyama, Shigehiro Asano, S. Kuramitsu, 1989, The Journal of biological chemistry.

Overproduction and preliminary X-ray characterization of aspartate aminotransferase from Escherichia coli.

H. Kagamiyama, N. Yasuoka, S. Kuramitsu, 1987, Journal of biochemistry.

A Water-soluble Homodimeric Serine Palmitoyltransferase fromSphingomonas paucimobilis EY2395T Strain

H. Ikushiro, H. Hayashi, H. Kagamiyama, 2001, The Journal of Biological Chemistry.

A water-soluble homodimeric serine palmitoyltransferase from Sphingomonas paucimobilis EY2395T strain. Purification, characterization, cloning, and overproduction.

H. Ikushiro, H. Hayashi, H. Kagamiyama, 2001, The Journal of biological chemistry.

Directed evolution of ampicillin-resistant activity from a functionally unrelated DNA fragment: A laboratory model of molecular evolution.

H. Kagamiyama, T. Yano, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Purification and characterization of a membrane-associated phospholipase A2 from rat spleen. Its comparison with a cytosolic phospholipase A2 S-1.

H. Tojo, H. Kagamiyama, S. Kuramitsu, 1988, The Journal of biological chemistry.

Demonstration of the importance and usefulness of manipulating non-active-site residues in protein design.

H. Kagamiyama, S. Kuramitsu, T. Yano, 2001, Journal of biochemistry.

Directed evolution of an aspartate aminotransferase with new substrate specificities.

H. Kagamiyama, T. Yano, S. Oue, 1998, Proceedings of the National Academy of Sciences of the United States of America.

OCAM: A New Member of the Neural Cell Adhesion Molecule Family Related to Zone-to-Zone Projection of Olfactory and Vomeronasal Axons

H. Hayashi, Y. Yoshihara, M. Kawasaki, 1997, The Journal of Neuroscience.

Mitochondrial Localization of Eukaryotic NifS-Like Proteins

H. Hayashi, H. Kagamiyama, M. Nakai, 2000 .

cDNA cloning and characterization of mouse nifS‐like protein, m‐Nfs1: mitochondrial localization of eukaryotic NifS‐like proteins

H. Hayashi, Y. Yoshihara, H. Kagamiyama, 1998, FEBS letters.

Expression of bovine lung prostaglandin F synthase in Escherichia coli.

H. Kagamiyama, K. Watanabe, S. Kuramitsu, 1991, Biochemical and biophysical research communications.

K. Mori, Y. Yoshihara, Yasuyoshi Watanabe, 1994, Neuron.

Rat pancreatic phospholipase A2: purification, characterization, and N-terminal amino acid sequence.

H. Tojo, H. Kagamiyama, M. Okamoto, 1984, Journal of Biochemistry (Tokyo).

Directed evolution of thermostable kanamycin-resistance gene: a convenient selection marker for Thermus thermophilus.

J. Hoseki, H. Kagamiyama, S. Kuramitsu, 1999, Journal of biochemistry.

X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from Escherichia coli in three forms.

H Hayashi, I. Miyahara, H. Hayashi, 1994, Journal of biochemistry.

Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures.

H. Hayashi, S. Yamamoto, H. Kagamiyama, 1992, Journal of biochemistry.

Glutamate-aspartate transaminase from microorganisms.

H. Kagamiyama, K. Soda, T. Yagi, 1985, Methods in enzymology.

Cysteine sulfinate transamination activity of aspartate aminotransferases.

H. Kagamiyama, T. Yagi, M. Nozaki, 1979, Biochemical and biophysical research communications.

Crystal Structures of Glutamine:Phenylpyruvate Aminotransferase from Thermus thermophilus HB8

I. Miyahara, H. Hayashi, H. Kagamiyama, 2004, Journal of Biological Chemistry.

Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence.

H. Kagamiyama, T. Ogawa, S. Kuramitsu, 1985, Journal of biochemistry.

Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene.

H. Kagamiyama, T. Ogawa, S. Kuramitsu, 1985, Journal of biochemistry.

Enzyme-substrate interactions modulating protonation and tautomerization states of the aldimines of pyridoxal enzymes

H. Hayashi, H. Kagamiyama, H. Mizuguchi, 1994 .

Properties of the bound coenzyme and subunit structure of omega-amino acid:pyruvate aminotransferase.

H. Kagamiyama, S. Toyama, K. Yonaha, 1983, The Journal of biological chemistry.

Molecular cloning of a 74‐kDa regulatory subunit (B″ or δ) of human protein phosphatase 2A

H. Hayashi, H. Kagamiyama, T. Nagase, 1996 .

Aspartate aminotransferase from a thermophilic formate-utilizing methanogen, Methanobacterium thermoformicicum strain SF-4: relation to serine and phosphoserine aminotransferases, but not to the aspartate aminotransferase family.

H. Hayashi, S. Yamamoto, H. Kagamiyama, 1994, Journal of biochemistry.

Branched-chain amino-acid aminotransferase of Escherichia coli.

H. Hayashi, H. Kagamiyama, 2000, Methods in enzymology.

The complete amino acid seqeunce of mitochondrial asparatate aminotransferase from pig heart.

H. Kagamiyama, R. Sakakibara, S. Tanase, 1977, Journal of biochemistry.

The Amino Acid Sequence of Purothionin A, A Lethal Toxic Protein for Brewer’s Yeasts from Wheat

H. Kagamiyama, H. Yoshizumi, T. Okada, 1975 .

Ferredoxin from a blue-green alga, Aphanothece sacrum (Suringar) Okada.

H. Kagamiyama, H. Matsubara, K. Wada, 1974, Journal of biochemistry.

The nucleotide sequence surrounding the promoter region of colicin E1 gene.

H. Kagamiyama, F. Kishi, A. Nakazawa, 1981, Gene.

Mycophenolic acid simultaneously reduces intracellular GTP and tetrahydrobiopterin levels in neuro-2A cells.

H. Kagamiyama, T. Harada, K. Hatakeyama, 1993, Advances in experimental medicine and biology.

Overlapping and differential expression of BIG-2, BIG-1, TAG-1, and F3: four members of an axon-associated cell adhesion molecule subgroup of the immunoglobulin superfamily.

K. Mori, Y. Yoshihara, M. Kawasaki, 1995, Journal of neurobiology.

Phosphorylation by protein kinase C of a synthetic heptapeptide bearing a lysine residue on the C terminal side of serine.

H. Kagamiyama, Y. Baba, H. Kondo, 1987, Biochemical and biophysical research communications.

Cloning and sequencing of cDNA encoding rat GTP cyclohydrolase I. The first enzyme of the tetrahydrobiopterin biosynthetic pathway.

H. Kagamiyama, T. Harada, Y. Inoue, 1991, The Journal of biological chemistry.

cDNA Cloning and Chromosomal Localization of the Human Telencephalin and Its Distinctive Interaction with Lymphocyte Function-associated Antigen-1*

J. Inazawa, Y. Yoshihara, T. Mizuno, 1997, The Journal of Biological Chemistry.

Yeast Nfs1p Is Involved in Thio-modification of Both Mitochondrial and Cytoplasmic tRNAs*

H. Hayashi, Tsutomu Suzuki, H. Kagamiyama, 2004, Journal of Biological Chemistry.

Instability of the apo form of aromatic L-amino acid decarboxylase in vivo and in vitro: implications for the involvement of the flexible loop that covers the active site.

H. Hayashi, H. Kagamiyama, T. Kuroiwa, 2004, Journal of biochemistry.

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.

H. Hayashi, H. Kagamiyama, M. Iwasaki, 1994, Journal of Biochemistry (Tokyo).

Contributions of the substrate-binding arginine residues to maleate-induced closure of the active site of Escherichia coli aspartate aminotransferase.

H. Hayashi, A. Matharu, H. Kagamiyama, 2001, European journal of biochemistry.

Crystal structures of branched-chain amino acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme.

I. Miyahara, H. Hayashi, H. Kagamiyama, 2003, Biochemistry.

Tyr225 in aspartate aminotransferase: contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction.

A. Okamoto, H. Kagamiyama, Y. Morino, 1991, Journal of biochemistry.

Activation of the coenzyme at the early step of the catalytic cycle of tryptophanase.

H. Ikushiro, H. Kagamiyama, 2000, BioFactors.

Replacement of an interdomain residue Val39 of Escherichia coli aspartate aminotransferase affects the catalytic competence without altering the substrate specificity of the enzyme.

H. Hayashi, H. Kagamiyama, S. Kuramitsu, 1991, Journal of biochemistry.

Molecular Diversity in Zebrafish NCAM Family: Three Members with Different VASE Usage and Distinct Localization

H. Okamoto, Y. Yoshihara, T. Mizuno, 2001, Molecular and Cellular Neuroscience.

Purification and properties of poly(ADP-ribose) synthetase from mouse testicle.

H. Kagamiyama, M. Nishikimi, Y. Shizuta, 1982, Archives of biochemistry and biophysics.

Terminal amino acids of aspartate aminotransferase isozymes.

H. Kagamiyama, H. Wada, T. Watanabe, 1968, Biochemical and biophysical research communications.

Reaction Mechanism of Alanine Racemase from Bacillus stearothermophilus

H. Hayashi, H. Kagamiyama, B. Mikami, 2002, The Journal of Biological Chemistry.

Neuronal adhesion molecule telencephalin induces rapid cell spreading of microglia

K. Mori, Y. Yoshihara, T. Mizuno, 1999, Brain Research.

Amino acid sequence of a presynaptic neurotoxin, agkistrodotoxin, from the venom of Agkistrodon halys Pallas.

H. Kagamiyama, K. Kondo, K. Xu, 1989, Journal of biochemistry.

Escherichia coli Aspartate Aminotransferase: Effects of Site-Specific Mutations on Substrate Binding and Catalysis

H. Hayashi, H. Kagamiyama, S. Kuramitsu, 1991 .

Three-dimensional structure of aspartate aminotransferase from Escherichia coli at 2.8 A resolution.

H. Kagamiyama, N. Yasuoka, S. Kuramitsu, 1988, Journal of biochemistry.

The chemical structure of tryptophanase from Escherichia coli. I. Isolation and structure of a pyridoxyl decapeptide from borohydride-reduced holotryptophanase.

H. Kagamiyama, Y. Morino, E. Snell, 1970, Journal of Biological Chemistry.

Aspartate aminotransferase isozymes from rabbit liver. Purification and properties.

H. Kagamiyama, S. Kuramitsu, K. Inoue, 1985, Journal of biochemistry.

Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution.

H. Hayashi, H. Kagamiyama, K. Okada, 1997, Journal of biochemistry.

Autoradiographic distribution of [14C]tetrahydrobiopterin and its developmental change in mice.

H. Kagamiyama, M. Hoshiga, M. Shimada, 1993, The Journal of pharmacology and experimental therapeutics.

Determination of human aspartate aminotransferase isoenzymes by their differential sensitivity to proteases.

H. Kagamiyama, Y. Morino, T. Yagi, 1988, Clinical biochemistry.

Pyridoxamine-α-keto acid transamination activity of aspartate apoaminotransferases

H. Kagamiyama, T. Yagi, M. Nozaki, 1982 .

Complete amino acid sequence of mitochondrial aspartate aminotransferase from pig heart muscle. Peptide ordering procedures and the complete sequence.

H. Kagamiyama, R. Sakakibara, S. Tanase, 1980, The Journal of biological chemistry.

Cytosolic and mitochondrial isoenzymes of glutamic-oxalacetic transaminase from human heart. Structural comparison with the isoenzymes from pig heart.

H. Kagamiyama, Y. Morino, H. Wada, 1978, The Journal of biological chemistry.

Studies on the Heterotropic Interaction of Hemoglobin

H. Kagamiyama, S. Tanase, Y. Morino, 1977 .

Large-scale preparation of cytosolic and mitochondrial asparatate aminotransferases from pig heart.

H. Kagamiyama, S. Tanase, Y. Morino, 1977, Journal of biochemistry.

Using 1H-and 15N-NMR spectroscopy to observe active sites of porcine cytosolic and Escherichia coli aspartate aminotransferases

I. Miyahara, H. Hayashi, H. Kagamiyama, 1994 .

Aspartate aminotransferase from E. coli--a comparative study among E. coli, and yeast enzymes and pig heart isozymes.

H. Kagamiyama, T. Yagi, K. Kondo, 1984, Progress in clinical and biological research.

Monoclonal and Polyclonal Antibodies Against Porcine Mitochondrial Aspartate Aminotransferase: Their Inhibition Modes and Application to Enzyme Immunoassay

H. Kagamiyama, M. Totani, T. Murachi, 1987, Biotechnology and applied biochemistry.

NMR studies of 1H resonances in the 10-18-ppm range for aspartate aminotransferase from Escherichia coli.

I. Miyahara, H. Hayashi, H. Kagamiyama, 1994, The Journal of biological chemistry.

Complete Amino Acid Sequence of Mitochondrial Aspartate Aminotransferase from Pig Heart Muscle

H. Kagamiyama, S. Tanase, Y. Morino, 1984 .

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.

Refined Reaction Mechanism of Aspartate Aminotransferase

I. Miyahara, H. Hayashi, H. Kagamiyama, 2000 .

Complete amino acid sequence of mitochondrial aspartate aminotransferase from pig heart muscle. Cyanogen bromide peptides.

H. Kagamiyama, R. Sakakibara, S. Tanase, 1980, The Journal of biological chemistry.

Complete amino acid sequence of mitochondrial aspartate aminotransferase from pig heart muscle. Tryptic peptides.

H. Kagamiyama, R. Sakakibara, S. Tanase, 1980, The Journal of biological chemistry.

Aspartate: 2-oxoglutarate aminotransferase from bakers' yeast: crystallization and characterization.

H. Kagamiyama, T. Yagi, M. Nozaki, 1982, Journal of biochemistry.

The chemical structure of tryptophanase from Escherichia coli. II. The structure of tryptophanase monomer.

H. Kagamiyama, H. Matsubara, H. Wada, 1972, The Journal of biological chemistry.

Mammalian Aspartate Aminotransferase Isozymes

H. Kagamiyama, Y. Morino, YOSHIMASA MORINO, 1990, Annals of the New York Academy of Sciences.

Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8: open-closed conformational change and ammonia tunneling.

Masaru Goto, Hiroyuki Kagamiyama, Hiroyuki Mizuguchi, 2002, Journal of biochemistry.

Structure, Induced Fit and Substrate Recognition of E. coli Branched-Chain Amino Acid Aminotransferase

I. Miyahara, H. Hayashi, H. Kagamiyama, 2000 .

Identification of autophosphorylation sites in c-Yes purified from rat liver plasma membranes.

H. Hayashi, H. Kagamiyama, R. Inoue, 1997, Journal of biochemistry.

A simple immunological method for differential determination of serum glutamic-oxaloacetic transaminase isoenzymes. (I) Using anti-human-GOT antibody.

H. Kagamiyama, H. Wada, H. Ohyanagi, 1978, Medical journal of Osaka University.

Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase.

H. Kagamiyama, T. Tsuzuki, S. Tanase, 1987, The Journal of biological chemistry.

Equisetum (horsetail) ferredoxin: characterization of the active centre and position of the four cysteine residues in this 2Fe-2S protein.

D. Hall, H. Kagamiyama, H. Matsubara, 1975, The Biochemical journal.

Cloning, DNA sequencing, and amino acid sequencing of catechol 1,2-dioxygenases (pyrocatechase) from Pseudomonas putida mt-2 and Pseudomonas arvilla C-1.

H. Kagamiyama, F. Kishi, A. Nakazawa, 1995, Archives of biochemistry and biophysics.

The complete amino acid sequence of the beta-subunit of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa.

H. Kagamiyama, M. Iwaki, M. Nozaki, 1979, Journal of biochemistry.

Unique stereospecificity of D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase for C-4' hydrogen transfer of the coenzyme

H. Kagamiyama, K. Soda, T. Yoshimura, 1993 .

Branched-Chain Amino Acid Aminotransferase from Escherichia Coli

H. Kagamiyama, S. Kuramitsu, Katsura Inoue, 1998 .

Asp222, His143, and Tyr70 in Escherichia coli Aspartate Aminotransferase

H. Kagamiyama, S. Kuramitsu, T. Yano, 1991 .

Role of an active site residue analyzed by combination of mutagenesis and coenzyme analog.

I. Miyahara, H. Kagamiyama, D. Metzler, 1993, Journal of molecular biology.

A convenient and sensitive method for the determination of serum aspartate aminotransferase isozymes after electrophoresis.

H. Kagamiyama, S. Kobayashi, T. Ikeda, 1983, Clinica chimica acta; international journal of clinical chemistry.