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Volumn 44, Issue 24, 2005, Pages 8697-8700

Kinetic control of thiamin diphosphate activation in enzymes studied by proton-nitrogen correlated NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CARRIER CONCENTRATION; CATALYSIS; NITROGEN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PROTONS; REACTION KINETICS;

EID: 20544474785     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050522x     Document Type: Article
Times cited : (16)

References (19)
  • 2
    • 0028841587 scopus 로고
    • The replacement of Trp392 by alanine influences the decarboxylase/ carboligase activity and stability of pyruvate decarboxylase from Zymomonas mobilis
    • Bruhn, H., Pohl, M., Grötzinger, J., and Kula, M. R. (1995) The replacement of Trp392 by alanine influences the decarboxylase/ carboligase activity and stability of pyruvate decarboxylase from Zymomonas mobilis, Eur. J. Biochem. 234, 650-655.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 650-655
    • Bruhn, H.1    Pohl, M.2    Grötzinger, J.3    Kula, M.R.4
  • 3
    • 0027714721 scopus 로고
    • Effects of metal ions, thiamin diphosphate analogues and subunit interactions on the reconstitution behaviour of pyruvate decarboxylase from brewer's yeast
    • Eppendorfer, S., König, S., Golbik, R., Neef, H., Lehle, K., Jaenicke, R., Schellenberger, A., and Hübner, G. (1993) Effects of metal ions, thiamin diphosphate analogues and subunit interactions on the reconstitution behaviour of pyruvate decarboxylase from brewer's yeast, Biol. Chem. Hoppe-Seyler 374, 1129-1134.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 1129-1134
    • Eppendorfer, S.1    König, S.2    Golbik, R.3    Neef, H.4    Lehle, K.5    Jaenicke, R.6    Schellenberger, A.7    Hübner, G.8
  • 5
    • 0028575439 scopus 로고
    • Analysis of an invariant cofactor-protein interaction in thiamin diphosphate-dependent enzymes by site-directed mutagenesis. Glutamic acid 418 in transketolase is essential for catalysis
    • Wikner, C., Meshalkina, L., Nilsson, U., Nikkola, M., Lindqvist, Y., Sundström, M., and Schneider, G. (1994) Analysis of an invariant cofactor-protein interaction in thiamin diphosphate-dependent enzymes by site-directed mutagenesis. Glutamic acid 418 in transketolase is essential for catalysis. J. Biol. Chem. 269, 32144-32150.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32144-32150
    • Wikner, C.1    Meshalkina, L.2    Nilsson, U.3    Nikkola, M.4    Lindqvist, Y.5    Sundström, M.6    Schneider, G.7
  • 6
    • 37049172468 scopus 로고
    • Aneurin. Part VII. A synthesis of aneurin
    • Todd, A. R., and Bergel, F. (1937) Aneurin. Part VII. A synthesis of aneurin, J. Chem. Soc., 364-367.
    • (1937) J. Chem. Soc. , pp. 364-367
    • Todd, A.R.1    Bergel, F.2
  • 8
    • 84982340434 scopus 로고
    • Zur frage des wirkungs-mechanismus des vitamins B1 und zur kenntnis der cocarboxylase
    • Karrer, P., and Viscontini, M. (1946) Zur Frage des Wirkungs-mechanismus des Vitamins B1 und zur Kenntnis der Cocarboxylase, Helv. Chim. Acta 29, 711-718.
    • (1946) Helv. Chim. Acta , vol.29 , pp. 711-718
    • Karrer, P.1    Viscontini, M.2
  • 9
    • 2542557579 scopus 로고    scopus 로고
    • Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1′,4′-imino tautomeric form of the coenzyme, unlike the Michaelis complex or the free coenzyme
    • Nemeria, N., Baykal, A., Joseph, E., Zhang, S., Yan, Y., Furey, W., and Jordan, F. (2004) Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1′,4′-imino tautomeric form of the coenzyme, unlike the Michaelis complex or the free coenzyme, Biochemistry 43, 6565-6575.
    • (2004) Biochemistry , vol.43 , pp. 6565-6575
    • Nemeria, N.1    Baykal, A.2    Joseph, E.3    Zhang, S.4    Yan, Y.5    Furey, W.6    Jordan, F.7
  • 10
    • 0001267046 scopus 로고
    • N1′-Methylthiaminium diiodide. Model study on the effect of a coenzyme bound positive charge on reaction mechanisms requiring thiamin pyrophosphate
    • Jordan, F., and Mariam, Y. H. (1978) N1′-Methylthiaminium diiodide. Model study on the effect of a coenzyme bound positive charge on reaction mechanisms requiring thiamin pyrophosphate, J. Am. Chem. Soc. 100, 2534-2541.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 2534-2541
    • Jordan, F.1    Mariam, Y.H.2
  • 11
    • 0032424138 scopus 로고    scopus 로고
    • Activation of thiamine diphosphate in pyruvate decarboxylase from Zymomonas mobilis
    • Tittmann, K., Mesch, K., Pohl, M., and Hübner, G. (1998) Activation of thiamine diphosphate in pyruvate decarboxylase from Zymomonas mobilis, FEBS Lett. 441, 404-406.
    • (1998) FEBS Lett. , vol.441 , pp. 404-406
    • Tittmann, K.1    Mesch, K.2    Pohl, M.3    Hübner, G.4
  • 12
    • 0026762799 scopus 로고
    • Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 Å resolution
    • Lindqvist, Y., Schneider, G., Ermler, U., and Sundström, M. (1992) Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 Å resolution, EMBO J. 11, 2373-2379.
    • (1992) EMBO J. , vol.11 , pp. 2373-2379
    • Lindqvist, Y.1    Schneider, G.2    Ermler, U.3    Sundström, M.4
  • 13
    • 0028305456 scopus 로고
    • Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution
    • Nikkola, M., Lindqvist, Y., and Schneider, G. (1994) Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution, J. Mol. Biol. 238, 387-404.
    • (1994) J. Mol. Biol. , vol.238 , pp. 387-404
    • Nikkola, M.1    Lindqvist, Y.2    Schneider, G.3
  • 14
    • 0027479683 scopus 로고
    • Structure of the thiamine-and flavin-dependent enzyme pyruvate oxidase
    • Muller, Y. A., and Schulz, G. E. (1993) Structure of the thiamine-and flavin-dependent enzyme pyruvate oxidase, Science 259, 965-967.
    • (1993) Science , vol.259 , pp. 965-967
    • Muller, Y.A.1    Schulz, G.E.2
  • 15
    • 0028296918 scopus 로고
    • The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum
    • Muller, Y. A., Schumacher, G., Rudolph, R., and Schulz, G. E. (1994) The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum, J. Mol. Biol. 237, 315-335.
    • (1994) J. Mol. Biol. , vol.237 , pp. 315-335
    • Muller, Y.A.1    Schumacher, G.2    Rudolph, R.3    Schulz, G.E.4
  • 16
    • 0027195094 scopus 로고
    • Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-Å resolution
    • Dyda, F., Furey, W., Swaminathan, S., Sax, M., Farrenkopf, B., and Jordan, F. (1993) Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-Å resolution, Biochemistry 32, 6165-6170.
    • (1993) Biochemistry , vol.32 , pp. 6165-6170
    • Dyda, F.1    Furey, W.2    Swaminathan, S.3    Sax, M.4    Farrenkopf, B.5    Jordan, F.6
  • 17
    • 0029967678 scopus 로고    scopus 로고
    • Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 Å resolution
    • Arjunan, P., Umland, T., Dyda, F., Swaminathan, S., Furey, W., Sax, M., Farrenkopf, B., Gao, Y., Zhang, D., and Jordan, F. (1996) Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 Å resolution, J. Mol. Biol. 256, 590-600.
    • (1996) J. Mol. Biol. , vol.256 , pp. 590-600
    • Arjunan, P.1    Umland, T.2    Dyda, F.3    Swaminathan, S.4    Furey, W.5    Sax, M.6    Farrenkopf, B.7    Gao, Y.8    Zhang, D.9    Jordan, F.10
  • 18
    • 0028040716 scopus 로고
    • A low-barrier hydrogen bond in the catalytic triad of serine proteases
    • Frey, P. A., Whitt, S. A., and Tobin, J. B. (1994) A low-barrier hydrogen bond in the catalytic triad of serine proteases, Science 264, 1927-1930.
    • (1994) Science , vol.264 , pp. 1927-1930
    • Frey, P.A.1    Whitt, S.A.2    Tobin, J.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.