Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold.
- K. Nakajima, A. Yamashita, Y. Yamada
- Chemistry, BiologyProceedings of the National Academy of Sciences…
- 28 April 1998
The results obtained herein raise the possibility that in certain cases different stereospecificities can be acquired in enzymes by changing a few amino acid residues within substrate binding sites.
Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase
- T. Nakatsu, H. Kato, J. Oda
- Chemistry, BiologyNature Structural Biology
- 1 March 1998
The crystal structure of E. coli asparagine synthetase has been determined by X-ray diffraction analysis at 2.5 Å resolution and it is suggested that new enzymatic activites would generally follow the recruitment of a protein catalyzing a similiar chemical reaction.
Purification, molecular cloning, and expression of lipase from Pseudomonas aeruginosa.
- M. Chihara-Siomi, K. Yoshikawa, J. Oda
- Biology, EngineeringArchives of Biochemistry and Biophysics
- 1 August 1992
Crystal structure of tobacco PR-5d protein at 1.8 A resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins.
- H. Koiwa, H. Kato, T. Nakatsu, J. Oda, Y. Yamada, F. Sato
- ChemistryJournal of Molecular Biology
- 5 March 1999
Sequence and secondary structure analyses showed that the amino acid residues comprising the acidic cleft of PR-5d are conserved among other antifungal PR-7 proteins, which provides insight into the function of pathogenesis-related proteins.
Site-directed Mutagenesis of Putative Substrate-binding Residues Reveals a Mechanism Controlling the Different Stereospecificities of Two Tropinone Reductases*
- K. Nakajima, H. Kato, J. Oda, Y. Yamada, T. Hashimoto
- Biology, ChemistryJournal of Biological Chemistry
- 4 June 1999
Kinetic analysis of the mutant TR structures has shown that TR stereospecificity is determined by varying the contributions from electrostatic and hydrophobic interactions and that the present TR structures represent highly evolved forms, in which strict stereOSpecificities and rapid turnover are accomplished together.
Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 A resolution.
- H. Yamaguchi, H. Kato, Y. Katsube
- Chemistry, BiologyJournal of Molecular Biology
- 31 January 1994
The crystal structure of the enzyme has been determined by isomorphous replacement and refined to a 2.0 A resolution and two regions, Gly164 to Gly167 and Ile226 to Arg241, are invisible on the electron density map.
A pseudo-michaelis quaternary complex in the reverse reaction of a ligase: structure of Escherichia coli B glutathione synthetase complexed with ADP, glutathione, and sulfate at 2.0 A resolution.
- T. Hara, H. Kato, Y. Katsube, J. Oda
- Chemistry, BiologyBiochemistry
- 17 September 1996
Functional aspects of the active site architecture in the substrate-binding form are discussed and this quaternary complex structure represents a pseudo enzyme-substrate complex in the reverse reaction and consequently allows us to understand theactive site architecture of the E. coli glutathione synthetase.
Lipase from Pseudomonas aeruginosa. Production in Escherichia coli and activation in vitro with a protein from the downstream gene.
- N. Oshima-Hirayama, K. Yoshikawa, T. Nishioka, J. Oda
- BiologyEuropean Journal of Biochemistry
- 1 July 1993
The lipase gene from Pseudomonas aeruginosa TE3285 is followed by another gene, lipB, which probably proceeds to form a 1:1 complex with the inactive, solubilized lipase protein but by a different mode from known chaperones.
Isolation and structure of the novel dihydroxamate siderophore alcaligin
- T. Nishio, N. Tanaka, J. Hiratake, Y. Katsube, Y. Ishida, J. Oda
- 1 December 1988
Crystal structure of gamma-glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis.
- T. Hibi, H. Nii, J. Oda
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 19 October 2004
The crystal structures of E. coli gammaGCS unliganded and complexed with a sulfoximine-based transition-state analog inhibitor are determined and the cysteine-binding site was identified; it is formed inductively at the transition state.