Crystal structure of the histidine-containing phosphotransfer protein ZmHP2 from maize., Sugawara H, Kawano Y, Hatakeyama T, Yamaya T, Kamiya N, Sakakibara H., Protein science, 14(1):202-8 (2005)
Structure of P-protein of the glycine cleavage system: implications for nonketotic hyperglycinemia., Nakai T, Nakagawa N, Maoka N, Masui R, Kuramitsu S, Kamiya N., EMBO J., 24(8):1523-36 (2005)
Binding of c5-dicarboxylic substrate to aspartate aminotransferase; implications for the conformational change at the transaldimination step., Islam MM, Goto M, Miyahara I,Ikushiro H, Hirotsu K, and Hayashi H., Biochemistry, 44(23) 8218-8229.(2005)
Structural determinants for branched-chain aminotransferase isozyme specific inhibition by the anticonvolsant drug gabapentin., Goto M., Miyahara I., Hirotsu K., Conway M., Yennawar N., Islam MM, Hutson SM., J. Biol. Chem., 280(44), pp.37246-37256 (2005)
Crystal structures of Δ1-piperideine-2-carboxylate/Δ1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases conformational change, substrate recognition, and stereochemistry of the reaction., Goto M., Muramatsu H., Mihara H., Kurihara T., Esaki N., Omi R., Miyahara I., Hirotsu K. J.Biol.Chem.,280(49), 40875-40884. (2005)
A new familiy of NAD(P)H-dependent oxidoreductase distinct from conventional Rossmann-fold proteins., Muramatsu, H., Mihara, H., Goto M., Miyahara, I., Hirotsu, K., Kurihara, T., and Esaki, N., J. Biosci. Bioeng., 99(6), 541-547. (2005)
Binding of c5-dicarboxylic substrate to aspartate aminotransferase:
implications for the conformational change at the transaldimination step. Islam MM, Goto M, Miyahara I,Ikushiro H, Hirotsu K, and Hayashi H., Biochemistry, 44(23) 8218-8229 (2005).
Dual substrate recognition of aminotransferases., K.Hirotsu, M. Goto, A. Okamoto and I.Miyahara, Chem. Rec, 5(3), 160-172. (2005)
原著論文／2004年
Expression, purification and preliminary X-ray characterization of histidinol phosphate phosphatase. R. Omi, M. Goto, N. Nakagawa, I. Miyahara and K. Hirotsu,. Acta Crystallogr D Biol. Crystallogr., 60, 574-576. (2004)
Crystal Structures of CTP Synthetase reveal ATP, UTP, and Glutamine Binding Sites, M. Goto, R. Omi, N. Nakagawa, I. Miyahara, and K. Hirotsu. Structure, 12, 1413-1423. (2004)
Stereochemistry of disilanylene-containing cyclic compounds. Synthesis and reactions of cis- and trans-3,4-benzo-1,2-di(tert-butyl)-1,2-dimethyl-1,2- disilacyclobut-3-ene. , A. Naka, J. Ikadai, J. Sakata, I. Miyahara, K. Hirotsu and M. Ishikawa , Organometalics, 23, 2397-2404 (2004)
Silicon-Carbon Unsaturated Compounds. 69. Reactions of silenes produced thermally from pivaloyl- and admantoyltris(trimethylsilyl)silane with silyl-substituted butadienes and enynes., A. Naka, I. Miyahara, K. Hirotsu, Y. Shiota, K. Yoshizawa, and M. Ishikawa, Organometallics, 23, 4277-4287 (2004).
Crystal Structure of Glutamine:Phenylpyruvate Aminotransferase from Thermus thermophilus HB8:INDUCED FIT AND SUBSTRATE RECOGNITION, Goto M, Omi R, Miyahara I, Hosono A, Mizuguchi H, Hayashi H, Kagamiyama H, Hirotsu K, J.Biol. Chem., 279(16), 16518-16525 (2004)
Glutamine:phenylpyruvate Aminotransferase from an Extremely Thermophilic Bacterium Thermus thermophilus HB8, Hosono A., Mizuguchi H., Hayashi H., Goto M., Miyahara I., Hirotsu K., and Kagamiyama H., J Biochem, 134(5), 843-851 (2003)
Crystal Structures of Threonine Synthase from Thermus thermophilus HB8: Conformational change, substrate recognition, and mechanism, Omi R, Goto M, Miyahara I, Mizuguchi H, Hayashi H, Kagamiyama H, Hirotsu K..J Biol Chem. 278(46), 46035-46045 (2003).
Structure of the Transition State Analog of Medium-Chain Acyl-CoA Dehydrogenase. Crystallographic and Molecular Orbital Studies on the Charge-Transfer Complex of Medium-Chain Acyl-CoA Dehydrogenase with 3-Thiaoctanoyl-CoA. Satoh A, Nakajima Y, Miyahara I, Hirotsu K, Tanaka T, Nishina Y, Shiga K, Tamaoki H, Setoyama C, Miura R., J Biochem, 134(2), 297-304 (2003)
Structures of Argininosuccinate Synthetase in Enzyme-ATP-Substrates and Enzyme-AMP-Product Forms: Stereochemistry of the Catalytic Reaction. Masaru Goto, Rie Omi, Ikuko Miyahara, Mitsuaki Sugahara, and Ken Hirotsu, J. Biol. Chem. 278(25), 22964-22971 (2003)
Strain and catalysis in aspartate aminotransferase. Hayashi H, Mizuguchi H, Miyahara I, Islam MM, Ikushiro H, Nakajima Y, Hirotsu K, Kagamiyama H. Biochim Biophys Acta. 1647(1-2), 103-109 (2003).
Characterization of histidinol phosphate aminotransferase from Escherichia coli. Mizuguchi H, Hayashi H, Miyahara I, Hirotsu K, Kagamiyama H. Biochim. Biophys. Acta.1647(1-2), 321-324 (2003).
Crystal structures of branched-chain amino Acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme. Goto M, Miyahara I, Hayashi H, Kagamiyama H, Hirotsu.K. Biochemistry42(13), 3725-3733 (2003).
The active site structure of quinohemoprotein amine dehydrogenase inhibited by p-nitrophenyl-hydrazine. Atsuko Satoh, Osao Adachi, Katsuyuki Tanizawa, Ken Hirotsu, Biochimica et Biophysica Acta, 1647(1-2), 272-277 (2003).
Expression, purification and preliminary X-ray characterization of CTP synthetase from Thermus thermophilus HB8. Goto M, Omi R, Hoseki J, Nakagawa N, Miyahara I, Hirotsu K Acta Crystallogr D Biol Crystallogr. 59(3), 551-553 (2003).
Expression, purification and preliminary X-ray characterization of N-acetyl-gamma-glutamyl-phosphate reductase from Thermus thermophilus HB8. Goto M, Agari Y, Omi R, Miyahara I, Hirotsu K. Acta Crystallogr. D Biol. Crystallogr.59(2), 356-358 (2003).
Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis. Hayashi H, Mizuguchi H, Miyahara I, Nakajima Y, Hirotsu K, Kagamiyama H. J Biol Chem.278(11):9481-9488 (2003).
Structure of Imidazole Glycerol Phosphate Synthase from Thermus thermophilus HB8: Open-Closed Conformational Change and Ammonia Tunneling. Omi R, Mizuguchi H, Goto M, Miyahara I, Hayashi H, Kagamiyama H, Hirotsu K. J Biochem.132(5):759-65 (2002).
Mechanism of preferential enrichment, an unusual enantiomeric resolution phenomenon caused by polymorphic transition during crystallization of mixed crystals composed of two enantiomers. Tamura R, Fujimoto D, Lepp Z, Misaki K, Miura H, Takahashi H, Ushio T, Nakai T, Hirotsu K. J. Am. Chem. Soc. 124(44), 13139-53 (2002).
Crystal structure of argininosuccinate synthetase from Thermus thermophilus HB8. Structural basis for the catalytic action. Goto M, Nakajima Y, Hirotsu K. J. Biol. Chem. 277(18), 15890-6 (2002).
Three-dimensional Structure of the Flavoenzyme Acyl-CoA Oxidase-II from Rat Liver, the Peroxisomal Counterpart of Mitochondrial Acyl-CoA Dehydrogenase, Yoshitaka Nakajima, Ikuko Miyahara, Ken Hirotsu, Yasuzo Nishina, Kiyoshi Shiga, Chiaki Setoyama, Haruhiko Tamaoki, and Retsu Miura, J. Biochem. 131(3), 365-374 (2002).
Effects of hydrogen bonds in association with flavin and substrate in flavoenzyme D-amino acid oxidase. The catalytic and structural roles of Gly313 and Thr317. Chiaki Setoyama, Yasuzo Nishina, Haruhiko Tamaoki, Hisashi Mizutani, Ikuko Miyahara, Ken Hirotsu, Kiyoshi Shiga, and Retsu Miura, J. Biochem. 131(1), 59-69 (2002).
Atsuko Satoh, Jong-Keun Kim, Ikuko Miyahara, Bart Devreese, Isabel Vandenberghe, Ayse Hacisalihoglu|, Toshihide Okajima, Shun'ichi Kuroda, Osao Adachi, Johannis A. Duine|, Jozef Van Beeumen, Katsuyuki Tanizawa，, and Ken Hirotsu, Crystal Structure of Quinohemoprotein Amine Dehydrogenase from Pseudomonas putida, Identification of a Novel Quinone Cofactor encaged by Mutiple Thioether Cross-Brudges, J. Biol. Chem.277(4), 2830-2834 (2002).
