메뉴 건너뛰기




Volumn 584, Issue 1, 2010, Pages 219-223

Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases

Author keywords

Butanediol dehydrogenase; Chiral recognition; Short chain dehydrogenase reductase family; Stereoisomer; X ray crystallography

Indexed keywords

2,3 BUTANEDIOL DEHYDROGENASE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 71549166006     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.11.068     Document Type: Article
Times cited : (36)

References (18)
  • 1
    • 0001331433 scopus 로고
    • Mechanism for the formation of 2, 3-butanediol stereoisomers in Klebsiella pneumoniae
    • Ui S., Matsuyama N., Masuda H., and Muraki H. Mechanism for the formation of 2, 3-butanediol stereoisomers in Klebsiella pneumoniae. J. Ferment. Techol. 62 (1984) 551-559
    • (1984) J. Ferment. Techol. , vol.62 , pp. 551-559
    • Ui, S.1    Matsuyama, N.2    Masuda, H.3    Muraki, H.4
  • 2
    • 0031664034 scopus 로고    scopus 로고
    • Sequence analysis of the gene for and characterization of D-acetoin forming meso-2, 3-butanediol dehydrogenase of Klebsiella pneumoniae expressed in Escherichia coli
    • Ui S., Okajima Y., Mimura A., Kanai H., Kobayashi T., and Kudo T. Sequence analysis of the gene for and characterization of D-acetoin forming meso-2, 3-butanediol dehydrogenase of Klebsiella pneumoniae expressed in Escherichia coli. J. Ferment. Bioeng. 86 (1997) 290-295
    • (1997) J. Ferment. Bioeng. , vol.86 , pp. 290-295
    • Ui, S.1    Okajima, Y.2    Mimura, A.3    Kanai, H.4    Kobayashi, T.5    Kudo, T.6
  • 3
    • 0005957153 scopus 로고    scopus 로고
    • Cloning, expression and nucleotide sequence of the l-2, 3-butanediol dehydrogenase gene from Brevibacterium saccharolyticum C-1012
    • Ui S., Otagiri M., Mimura A., Dohmae N., Takio K., Ohkuma M., and Kudo T. Cloning, expression and nucleotide sequence of the l-2, 3-butanediol dehydrogenase gene from Brevibacterium saccharolyticum C-1012. J. Ferment. Bioeng. 83 (1998) 32-37
    • (1998) J. Ferment. Bioeng. , vol.83 , pp. 32-37
    • Ui, S.1    Otagiri, M.2    Mimura, A.3    Dohmae, N.4    Takio, K.5    Ohkuma, M.6    Kudo, T.7
  • 6
    • 0025838697 scopus 로고
    • Three-dimensional structure of holo 3,20-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family
    • Gosh D., Weeks C.M., Grouchlski P., Duax W.L., Erman M., Rimsay R.L., and Orr J.C. Three-dimensional structure of holo 3,20-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family. Proc. Natl. Acad. Sci. USA 88 (1991) 10064-10068
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10064-10068
    • Gosh, D.1    Weeks, C.M.2    Grouchlski, P.3    Duax, W.L.4    Erman, M.5    Rimsay, R.L.6    Orr, J.C.7
  • 7
    • 0032544367 scopus 로고    scopus 로고
    • The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 Å resolution
    • Brenach J., Atrian S., Gonzalez-Duarte R., and Ladenstein R. The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 Å resolution. J. Mol. Biol. 282 (1998) 383-399
    • (1998) J. Mol. Biol. , vol.282 , pp. 383-399
    • Brenach, J.1    Atrian, S.2    Gonzalez-Duarte, R.3    Ladenstein, R.4
  • 8
    • 0029643855 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family
    • Tanaka N., Nonaka T., Nakanishi M., Deyashiki Y., Hara A., and Mitsui Y. Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family. Structure 4 (1996) 33-45
    • (1996) Structure , vol.4 , pp. 33-45
    • Tanaka, N.1    Nonaka, T.2    Nakanishi, M.3    Deyashiki, Y.4    Hara, A.5    Mitsui, Y.6
  • 11
    • 0035016629 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray studies of l-(+)-2,3-butanediol dehydrogenase from Brevibacterium saccharolyticum C-I012
    • Otagiri M., Kurisu G., Ui S., Ohkuma M., Kudo T., and Kusunoki M. Crystallization and preliminary X-ray studies of l-(+)-2,3-butanediol dehydrogenase from Brevibacterium saccharolyticum C-I012. Protein Peptide Lett. 8 (2001) 57-61
    • (2001) Protein Peptide Lett. , vol.8 , pp. 57-61
    • Otagiri, M.1    Kurisu, G.2    Ui, S.3    Ohkuma, M.4    Kudo, T.5    Kusunoki, M.6
  • 12
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. Sect. A 50 (1994) 157-163
    • (1994) Acta Crystallogr. Sect. A , vol.50 , pp. 157-163
    • Navza, J.1
  • 14
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47 (1991) 110-119
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 15
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon M. The determination of enzyme inhibitor constants. Biochem. J. 55 (1953) 170-171
    • (1953) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 16
    • 1542563485 scopus 로고
    • Evolutionary and structural relationships among dehydrogenases
    • Boyer P.D. (Ed), Academic Press, New York
    • Rossmnn M.G., Liljas A., Branden C.I., and Banaszak L.J. Evolutionary and structural relationships among dehydrogenases. In: Boyer P.D. (Ed). The enzymes. third ed. vol. 11A (1975), Academic Press, New York 61-102
    • (1975) The enzymes. third ed. , vol.11 A , pp. 61-102
    • Rossmnn, M.G.1    Liljas, A.2    Branden, C.I.3    Banaszak, L.J.4
  • 18
    • 0035110378 scopus 로고    scopus 로고
    • Crystal structure of glucose dehydrogenase from Bacillus megaterium IWG3 at 1.7 Å resolution
    • Yamamoto K., Kurisu G., Kusunoki M., Tabata S., Urabe I., and Osaki S. Crystal structure of glucose dehydrogenase from Bacillus megaterium IWG3 at 1.7 Å resolution. J. Biochem. (Tokyo) 129 (2001) 303-312
    • (2001) J. Biochem. (Tokyo) , vol.129 , pp. 303-312
    • Yamamoto, K.1    Kurisu, G.2    Kusunoki, M.3    Tabata, S.4    Urabe, I.5    Osaki, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.