Yagi T - Search Results

1

Crystallization and preliminary X-ray analysis of AAMS amidohydrolase, the final enzyme in degradation pathway I of pyridoxine.

Kobayashi J, Yoshida H, Chu HN, Yoshikane Y, Kamitori S, Yagi T. Kobayashi J, et al. Among authors: yagi t. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Aug 1;65(Pt 8):829-31. doi: 10.1107/S1744309109026864. Epub 2009 Jul 30. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009. PMID: 19652351 Free PMC article.

2

Crystallization and preliminary X-ray analysis of pyridoxal 4-dehydrogenase, the second enzyme in degradation pathway I of pyridoxine.

Yokochi N, Yoshikane Y, Yagi T, Yamasaki M, Mikami B. Yokochi N, et al. Among authors: yagi t. Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):2061-2. doi: 10.1107/S0907444904021754. Epub 2004 Oct 20. Acta Crystallogr D Biol Crystallogr. 2004. PMID: 15502327

3

Gene identification and characterization of the pyridoxine degradative enzyme alpha-(N-acetylaminomethylene)succinic acid amidohydrolase from Mesorhizobium loti MAFF303099.

Yuan B, Yokochi N, Yoshikane Y, Ohnishi K, Ge F, Yagi T. Yuan B, et al. Among authors: yagi t. J Nutr Sci Vitaminol (Tokyo). 2008 Jun;54(3):185-90. doi: 10.3177/jnsv.54.185. J Nutr Sci Vitaminol (Tokyo). 2008. PMID: 18635903 Free article.

4

Crystallization and preliminary X-ray analysis of 4-pyridoxolactonase from Mesorhizobium loti.

Matsuda S, Yokochi N, Yoshikane Y, Kobayashi J, Huy CN, Baba S, Kuramitsu S, Mikami B, Yagi T. Matsuda S, et al. Among authors: yagi t. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt 9):886-9. doi: 10.1107/S1744309109028772. Epub 2009 Aug 22. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009. PMID: 19724124 Free PMC article.

5

Crystallization and preliminary X-ray analysis of SDR-type pyridoxal dehydrogenase from Mesorhizobium loti.

Chu HN, Kobayashi J, Yoshikane Y, Mikami B, Yagi T. Chu HN, et al. Among authors: yagi t. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jun 1;66(Pt 6):718-20. doi: 10.1107/S1744309110015101. Epub 2010 May 29. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010. PMID: 20516609 Free PMC article.

6

The crystal structure of SDR-type pyridoxal 4-dehydrogenase of Mesorhizobium loti.

Chu HN, Kobayashi J, Mikami B, Yagi T. Chu HN, et al. Among authors: yagi t. Biosci Biotechnol Biochem. 2011;75(2):388-90. doi: 10.1271/bbb.100748. Epub 2011 Feb 7. Biosci Biotechnol Biochem. 2011. PMID: 21307574 Free article.

7

Crystallization and preliminary X-ray analysis of pyridoxine 4-oxidase, the first enzyme in pyridoxine degradation pathway I.

Mugo AN, Kobayashi J, Mikami B, Ohnishi K, Yagi T. Mugo AN, et al. Among authors: yagi t. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jan 1;68(Pt 1):66-8. doi: 10.1107/S1744309111048688. Epub 2011 Dec 24. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012. PMID: 22232175 Free PMC article.

8

Structure of 4-pyridoxolactonase from Mesorhizobium loti.

Kobayashi J, Yoshikane Y, Yagi T, Baba S, Mizutani K, Takahashi N, Mikami B. Kobayashi J, et al. Among authors: yagi t. Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):424-32. doi: 10.1107/S2053230X14003926. Epub 2014 Mar 25. Acta Crystallogr F Struct Biol Commun. 2014. PMID: 24699732 Free PMC article.

9

The nitrogen-fixing symbiotic bacterium Mesorhizobium loti has and expresses the gene encoding pyridoxine 4-oxidase involved in the degradation of vitamin B6.

Yuan B, Yoshikane Y, Yokochi N, Ohnishi K, Yagi T. Yuan B, et al. Among authors: yagi t. FEMS Microbiol Lett. 2004 May 15;234(2):225-30. doi: 10.1016/j.femsle.2004.03.031. FEMS Microbiol Lett. 2004. PMID: 15135526

10

Identification of a new tetrameric pyridoxal 4-dehydrogenase as the second enzyme in the degradation pathway for pyridoxine in a nitrogen-fixing symbiotic bacterium, Mesorhizobium loti.

Yokochi N, Nishimura S, Yoshikane Y, Ohnishi K, Yagi T. Yokochi N, et al. Among authors: yagi t. Arch Biochem Biophys. 2006 Aug 1;452(1):1-8. doi: 10.1016/j.abb.2006.06.002. Epub 2006 Jun 16. Arch Biochem Biophys. 2006. PMID: 16824480

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