Authors:
Mizuno, T
Kawasaki, M
Nakahira, M
Kagamiyama, H
Kikuchi, Y
Okamoto, H
Mori, K
Yoshihara, Y
Citation: T. Mizuno et al., Molecular diversity in zebrafish NCAM family: Three members with differentVASE usage and distinct localization, MOL CELL NE, 18(1), 2001, pp. 119-130
Citation: T. Yano et H. Kagamiyama, Directed evolution of ampicillin-resistant activity from a functionally unrelated DNA fragment: A laboratory model of molecular evolution, P NAS US, 98(3), 2001, pp. 903-907
Citation: H. Ikushiro et al., A water-soluble homodimeric serine palmitoyltransferase from Sphingomonas paucimobilis EY2395(T) strain - Purification, characterization, cloning, and overproduction, J BIOL CHEM, 276(21), 2001, pp. 18249-18256
Authors:
Hashimoto, Y
Yano, T
Kuramitsu, S
Kagamiyama, H
Citation: Y. Hashimoto et al., Disruption of Thermus thermophilus genes by homologous recombination usinga thermostable kanamycin-resistant marker, FEBS LETTER, 506(3), 2001, pp. 231-234
Authors:
Matharu, A
Hayashi, H
Kagamiyama, H
Maras, B
John, RA
Citation: A. Matharu et al., Contributions of the substrate-binding arginine residues to maleate-induced closure of the active site of Escherichia coli aspartate aminotransferase, EUR J BIOCH, 268(6), 2001, pp. 1640-1645
Authors:
Okada, K
Hirotsu, K
Hayashi, H
Kagamiyama, H
Citation: K. Okada et al., 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, BIOCHEM, 40(25), 2001, pp. 7453-7463
Authors:
Mizuguchi, H
Hayashi, H
Okada, K
Miyahara, I
Hirotsu, K
Kagamiyama, H
Citation: H. Mizuguchi et al., Strain is more important than electrostatic interaction in controlling thepK(a) of the catalytic group in aspartate aminotransferase, BIOCHEM, 40(2), 2001, pp. 353-360
Authors:
Haruyama, K
Nakai, T
Miyahara, I
Hirotsu, K
Mizuguchi, H
Hayashi, H
Kagamiyama, H
Citation: K. Haruyama et al., 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, BIOCHEM, 40(15), 2001, pp. 4633-4644
Citation: S. Oue et al., Cocrystallization of a mutant aspartate aminotransferase with a C5-dicarboxylic substrate analog: Structural comparison with the enzyme-C4-dicarboxylic analog complex, J BIOCHEM, 127(2), 2000, pp. 337-343
Authors:
Islam, MM
Hayashi, H
Mizuguchi, H
Kagamiyama, H
Citation: Mm. Islam et al., The substrate activation process in the catalytic reaction of Escherichia coli aromatic amino acid aminotransferase, BIOCHEM, 39(50), 2000, pp. 15418-15428
Authors:
Yoshihara, Y
Mizuno, T
Nakahira, M
Kawasaki, M
Watanabe, Y
Kagamiyama, H
Jishage, K
Ueda, O
Suzuki, H
Tabuchi, K
Sawamoto, K
Okano, H
Noda, T
Mori, K
Citation: Y. Yoshihara et al., A genetic approach to visualization of multisynaptic neural pathways usingplant lectin transgene, NEURON, 22(1), 1999, pp. 33-41
Citation: S. Oue et al., Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues, J BIOL CHEM, 274(4), 1999, pp. 2344-2349
Authors:
Hoseki, J
Yano, T
Koyama, Y
Kuramitsu, S
Kagamiyama, H
Citation: J. Hoseki et al., Directed evolution of thermostable kanamycin-resistance gene: A convenientselection marker for Thermus thermophilus, J BIOCHEM, 126(5), 1999, pp. 951-956
Authors:
Hayashi, H
Tsukiyama, F
Ishii, S
Mizuguchi, H
Kagamiyama, H
Citation: H. Hayashi et al., Acid-base chemistry of the reaction of aromatic L-amino acid decarboxylaseand dopa analyzed by transient and steady-state kinetics: Preferential binding of the substrate with its amino group unprotonated, BIOCHEM, 38(47), 1999, pp. 15615-15622
Authors:
Okamoto, A
Ishii, S
Hirotsu, K
Kagamiyama, H
Citation: A. Okamoto et al., The active site of Paracoccus denitrificans aromatic amino acid aminotransferase has contrary properties: Flexibility and rigidity, BIOCHEM, 38(4), 1999, pp. 1176-1184
Citation: H. Hayashi et al., 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 (vol 37, pg 15076, 1998), BIOCHEM, 38(2), 1999, pp. 854-854
Authors:
Ishii, S
Hayashi, H
Okamoto, A
Kagamiyama, H
Citation: S. Ishii et al., Aromatic L-amino acid decarboxylase: Conformational change in the flexibleregion around Arg334 is required during the transaldimination process, PROTEIN SCI, 7(8), 1998, pp. 1802-1810