Oda J - Search Results

1

Capturing enzyme structure prior to reaction initiation: tropinone reductase-II-substrate complexes.

Yamashita A, Endo M, Higashi T, Nakatsu T, Yamada Y, Oda J, Kato H. Yamashita A, et al. Among authors: oda j. Biochemistry. 2003 May 20;42(19):5566-73. doi: 10.1021/bi0272712. Biochemistry. 2003. PMID: 12741812

2

Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis.

Yamashita A, Kato H, Wakatsuki S, Tomizaki T, Nakatsu T, Nakajima K, Hashimoto T, Yamada Y, Oda J. Yamashita A, et al. Among authors: oda j. Biochemistry. 1999 Jun 15;38(24):7630-7. doi: 10.1021/bi9825044. Biochemistry. 1999. PMID: 10387002

3

Crystal structure of gamma-glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis.

Hibi T, Nii H, Nakatsu T, Kimura A, Kato H, Hiratake J, Oda J. Hibi T, et al. Among authors: oda j. Proc Natl Acad Sci U S A. 2004 Oct 19;101(42):15052-7. doi: 10.1073/pnas.0403277101. Epub 2004 Oct 11. Proc Natl Acad Sci U S A. 2004. PMID: 15477603 Free PMC article.

4

Mutational and proteolytic studies on a flexible loop in glutathione synthetase from Escherichia coli B: the loop and arginine 233 are critical for the catalytic reaction.

Tanaka T, Kato H, Nishioka T, Oda J. Tanaka T, et al. Among authors: oda j. Biochemistry. 1992 Mar 3;31(8):2259-65. doi: 10.1021/bi00123a007. Biochemistry. 1992. PMID: 1540581

5

Flexibility impaired by mutations revealed the multifunctional roles of the loop in glutathione synthetase.

Tanaka T, Yamaguchi H, Kato H, Nishioka T, Katsube Y, Oda J. Tanaka T, et al. Among authors: oda j. Biochemistry. 1993 Nov 23;32(46):12398-404. doi: 10.1021/bi00097a018. Biochemistry. 1993. PMID: 8241129

The loop from Ile-226 to Arg-241 in the glutathione synthetase (GSHase) from Escherichia coli B is rich in glycine and alanine and too flexible to take a fixed conformation [Yamaguchi, H., Kato, H., Hata, Y., Nishioka, T., Kimura, A., Oda, J., & Katsube, Y. (199 …

The loop from Ile-226 to Arg-241 in the glutathione synthetase (GSHase) from Escherichia coli B is rich in glycine and alanine and too flexi …

6

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.

Hara T, Kato H, Katsube Y, Oda J. Hara T, et al. Among authors: oda j. Biochemistry. 1996 Sep 17;35(37):11967-74. doi: 10.1021/bi9605245. Biochemistry. 1996. PMID: 8810901

7

Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold.

Nakajima K, Yamashita A, Akama H, Nakatsu T, Kato H, Hashimoto T, Oda J, Yamada Y. Nakajima K, et al. Among authors: oda j. Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4876-81. doi: 10.1073/pnas.95.9.4876. Proc Natl Acad Sci U S A. 1998. PMID: 9560196 Free PMC article.

8

Crystallization and preliminary crystallographic study of tropinone reductase II from Datura stramonium.

Yamashita A, Nakajima K, Kato H, Hashimoto T, Yamada Y, Oda J. Yamashita A, et al. Among authors: oda j. Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1405-7. doi: 10.1107/s0907444998005782. Acta Crystallogr D Biol Crystallogr. 1998. PMID: 10089520

9

Flexible loop that is novel catalytic machinery in a ligase. Atomic structure and function of the loopless glutathione synthetase.

Kato H, Tanaka T, Yamaguchi H, Hara T, Nishioka T, Katsube Y, Oda J. Kato H, et al. Among authors: oda j. Biochemistry. 1994 May 3;33(17):4995-9. doi: 10.1021/bi00183a001. Biochemistry. 1994. PMID: 8172874

A flexible loop (Ile226-Gly242) in Escherichia coli B glutathione synthetase is proposed to stabilize the acyl phosphate intermediate by preventing its decomposition by hydrolysis with water [Tanaka, T., Kato, H., Nishioka, T., & Oda, J. (1992) Biochemistry 31, …

A flexible loop (Ile226-Gly242) in Escherichia coli B glutathione synthetase is proposed to stabilize the acyl phosphate intermediate by pre …

10

Site-directed mutagenesis of putative substrate-binding residues reveals a mechanism controlling the different stereospecificities of two tropinone reductases.

Nakajima K, Kato H, Oda J, Yamada Y, Hashimoto T. Nakajima K, et al. Among authors: oda j. J Biol Chem. 1999 Jun 4;274(23):16563-8. doi: 10.1074/jbc.274.23.16563. J Biol Chem. 1999. PMID: 10347221 Free article.

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