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Volumn 48, Issue 5, 2009, Pages 981-994

Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylase

Author keywords

[No Author keywords available]

Indexed keywords

ABSORBANCE; CHROMOPHORIC SUBSTRATES; COVALENT COMPLEXES; DECARBOXYLASE; DECARBOXYLATION REACTIONS; ENAMINE; ENAMINE INTERMEDIATES; HIGH RESOLUTIONS; NON-OXIDATIVE; REACTION PATHWAYS; THIAMIN DIPHOSPHATE; TIME COURSE; TRANSIENT INTERMEDIATES;

EID: 61449240107     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801810h     Document Type: Article
Times cited : (19)

References (45)
  • 1
    • 0032516465 scopus 로고    scopus 로고
    • The Crystal Structure of Benzoylformate Decarboxylase at 1.6Å Resolution: Diversity of Catalytic Residues in Thiamin Diphos-phate-Dependent Enzymes
    • Hasson, M. S., Muscate, A., Mcleish, M. J., Polovnikova, L. S., Gerlt, J. A., Kenyon, G. L., Petsko, G. A., and Ringe, D. (1998) The Crystal Structure of Benzoylformate Decarboxylase at 1.6Å Resolution: Diversity of Catalytic Residues in Thiamin Diphos-phate-Dependent Enzymes. Biochemistry 37, 9918-9930.
    • (1998) Biochemistry , vol.37 , pp. 9918-9930
    • Hasson, M.S.1    Muscate, A.2    Mcleish, M.J.3    Polovnikova, L.S.4    Gerlt, J.A.5    Kenyon, G.L.6    Petsko, G.A.7    Ringe, D.8
  • 2
    • 0024294289 scopus 로고
    • Kinetics and mechanism of benzoylformate decarboxylase using 13C and solvent deuterium isotope effects on benzoylformate and benzoylformate analogues
    • Weiss, P. M., Garcia, G. A., Kenyon, G. L., Cleland, W. W., and Cook, P. F. (1988) Kinetics and mechanism of benzoylformate decarboxylase using 13C and solvent deuterium isotope effects on benzoylformate and benzoylformate analogues. Biochemistry 27, 2197-2205.
    • (1988) Biochemistry , vol.27 , pp. 2197-2205
    • Weiss, P.M.1    Garcia, G.A.2    Kenyon, G.L.3    Cleland, W.W.4    Cook, P.F.5
  • 3
    • 0037391206 scopus 로고    scopus 로고
    • Current mechanistic understanding of thiamin diphosphate-dependent enzymatic reactions
    • Jordan, F. (2003) Current mechanistic understanding of thiamin diphosphate-dependent enzymatic reactions. Nat. Prod. Rep. 20, 184-201.
    • (2003) Nat. Prod. Rep , vol.20 , pp. 184-201
    • Jordan, F.1
  • 4
    • 18844421838 scopus 로고    scopus 로고
    • Experimental observation of thiamin diphosphate-bound intermediates on enzymes and mechanistic information derived from these observations
    • Jordan, F., and Nemeria, N. S. (2005) Experimental observation of thiamin diphosphate-bound intermediates on enzymes and mechanistic information derived from these observations. Bioorg. Chem. 33, 190-215.
    • (2005) Bioorg. Chem , vol.33 , pp. 190-215
    • Jordan, F.1    Nemeria, N.S.2
  • 5
    • 0000775140 scopus 로고
    • Observation of a 2-α-enamine from a 2-[α-methoxα-R-phenyl]-3,4-dimethylthi- azolium salt in water: Implications for catalysis by thiamin diphosphate - dependent α-keto acid decarboxylases
    • Barletta, G., Huskey, W. P., and Jordan, F. (1992) Observation of a 2-α-enamine from a 2-[α-methoxα-R-phenyl]-3,4-dimethylthi- azolium salt in water: Implications for catalysis by thiamin diphosphate - dependent α-keto acid decarboxylases. J. Am. Chem. Soc. 114, 7607-7608.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 7607-7608
    • Barletta, G.1    Huskey, W.P.2    Jordan, F.3
  • 6
    • 0030960601 scopus 로고    scopus 로고
    • Ionization kinetics at the C2a position of 2- benzylthiazolium salts leading to enamines relevant to thiamin catalyzed enzymatic reactions
    • Barletta, G. L., Huskey, W. P., and Jordan, F. (1997) Ionization kinetics at the C2a position of 2- benzylthiazolium salts leading to enamines relevant to thiamin catalyzed enzymatic reactions. J. Am. Chem. Soc. 119, 2356-2362.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 2356-2362
    • Barletta, G.L.1    Huskey, W.P.2    Jordan, F.3
  • 7
    • 0034649456 scopus 로고    scopus 로고
    • Spectroscopic Detection of Transient Thiamin Diphosphate-Bound Intermediates on Benzoylformate Decarboxylase
    • Sergienko, E. A., Wang, J., Polovnikova, L., Hasson, M. S., McLeish, M. J., Kenyon, G. L., and Jordan, F. (2000) Spectroscopic Detection of Transient Thiamin Diphosphate-Bound Intermediates on Benzoylformate Decarboxylase. Biochemistry 39, 13862-13869.
    • (2000) Biochemistry , vol.39 , pp. 13862-13869
    • Sergienko, E.A.1    Wang, J.2    Polovnikova, L.3    Hasson, M.S.4    McLeish, M.J.5    Kenyon, G.L.6    Jordan, F.7
  • 9
    • 64349104453 scopus 로고    scopus 로고
    • Ph.D. Dissertation, Department of Chemistry, Rutgers University, Newark, NJ
    • Zhang, S. (2004) Ph.D. Dissertation, Department of Chemistry, Rutgers University, Newark, NJ.
    • (2004)
    • Zhang, S.1
  • 10
    • 64349095766 scopus 로고    scopus 로고
    • Ph.D. Dissertation, Department of Chemistry, Rutgers University, Newark, NJ
    • Chakraborty, S. (2007) Ph.D. Dissertation, Department of Chemistry, Rutgers University, Newark, NJ.
    • (2007)
    • Chakraborty, S.1
  • 11
    • 64349117555 scopus 로고    scopus 로고
    • Ph.D. Dissertation, Department of Chemistry, Rutgers University, Newark, NJ
    • Joseph E. (2005) Ph.D. Dissertation, Department of Chemistry, Rutgers University, Newark, NJ.
    • (2005)
    • Joseph, E.1
  • 12
    • 0001267046 scopus 로고
    • N-1'-Methyl thiamin, a model for the role of the pyrimidine ring in thiamin pyrophosphate requiring enzymatic reactions
    • Jordan, F., and Mariam, Y. H. (1978) N-1'-Methyl thiamin, a model for the role of the pyrimidine ring in thiamin pyrophosphate requiring enzymatic reactions. J. Am. Chem. Soc. 100, 2534-2541.
    • (1978) J. Am. Chem. Soc , vol.100 , pp. 2534-2541
    • Jordan, F.1    Mariam, Y.H.2
  • 13
    • 0032537590 scopus 로고    scopus 로고
    • Sixty years of thiamin diphosphate biochemistry
    • Schellenberger, A. (1998) Sixty years of thiamin diphosphate biochemistry. Biochim. Biophys. Acta 1385, 177-186.
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 177-186
    • Schellenberger, A.1
  • 14
    • 33846041174 scopus 로고    scopus 로고
    • The 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes
    • Nemeria, N, Chakraborty, S., Baykal, A., Korotchkina, L. G., Patel, M. S., and Jordan, F. (2007) The 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes. Proc. Natl. Acad. Sci. U.S.A. 104, 78-82.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 78-82
    • Nemeria, N.1    Chakraborty, S.2    Baykal, A.3    Korotchkina, L.G.4    Patel, M.S.5    Jordan, F.6
  • 15
    • 0036619413 scopus 로고    scopus 로고
    • Spectroscopic evidence for participation of the 1',4'-imino tautomer of thiamin diphosphate in catalysis by yeast pyruvate decarboxylase
    • Jordan, F., Zhang, Z., and Sergienko, E. (2002) Spectroscopic evidence for participation of the 1',4'-imino tautomer of thiamin diphosphate in catalysis by yeast pyruvate decarboxylase. Bioorg. Chem. 30, 188-198.
    • (2002) Bioorg. Chem , vol.30 , pp. 188-198
    • Jordan, F.1    Zhang, Z.2    Sergienko, E.3
  • 16
    • 0142135980 scopus 로고    scopus 로고
    • Dual catalytic apparatus of the thiamin diphosphate coenzyme: Acid-base via the 1',4'-iminopyrimidine tautomer along with its electrophilic role
    • Jordan, F., Nemeria, N. S., Zhang, S., Yan, Y., Arjunan, P., and Furey, W. (2003) Dual catalytic apparatus of the thiamin diphosphate coenzyme: acid-base via the 1',4'-iminopyrimidine tautomer along with its electrophilic role. J. Am. Chem. Soc. 125, 12732-12738.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 12732-12738
    • Jordan, F.1    Nemeria, N.S.2    Zhang, S.3    Yan, Y.4    Arjunan, P.5    Furey, W.6
  • 17
    • 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
  • 18
    • 33745157872 scopus 로고    scopus 로고
    • Electronic and nuclear magnetic resonance spectroscopic features of the 1',4'-iminopyrimidine tautomeric form of thiamin diphosphate, a novel intermediate on enzymes requiring this coenzyme
    • Baykal, A. T., Kakalis, L., and Jordan, F. (2006) Electronic and nuclear magnetic resonance spectroscopic features of the 1',4'-iminopyrimidine tautomeric form of thiamin diphosphate, a novel intermediate on enzymes requiring this coenzyme. Biochemistry 45, 7522-7528.
    • (2006) Biochemistry , vol.45 , pp. 7522-7528
    • Baykal, A.T.1    Kakalis, L.2    Jordan, F.3
  • 19
    • 34548671397 scopus 로고    scopus 로고
    • Elucidation of the chemistry of enzyme-bound thiamin diphosphate prior to substrate binding: Defining internal equilibria among tautomeric and ionization states
    • Nemeria, N, Korotchkina, L., McLeish, M. J., Kenyon, G. L., Patel, M. S., and Jordan, F. (2007) Elucidation of the chemistry of enzyme-bound thiamin diphosphate prior to substrate binding: Defining internal equilibria among tautomeric and ionization states. Biochemistry 46, 10739-10744.
    • (2007) Biochemistry , vol.46 , pp. 10739-10744
    • Nemeria, N.1    Korotchkina, L.2    McLeish, M.J.3    Kenyon, G.L.4    Patel, M.S.5    Jordan, F.6
  • 20
    • 34948872723 scopus 로고    scopus 로고
    • A Dynamic Loop at the Active Center of the Escherichia coli Pyruvate Dehydrogenase Complex E1 Component Modulates Substrate Utilization and Chemical Communication with the E2 Component
    • Kale, S., Arjunan, P., Furey, W., and Jordan, F. (2007) A Dynamic Loop at the Active Center of the Escherichia coli Pyruvate Dehydrogenase Complex E1 Component Modulates Substrate Utilization and Chemical Communication with the E2 Component. J. Biol. Chem. 282, 28106-28116.
    • (2007) J. Biol. Chem , vol.282 , pp. 28106-28116
    • Kale, S.1    Arjunan, P.2    Furey, W.3    Jordan, F.4
  • 21
    • 33750731272 scopus 로고    scopus 로고
    • Acetylphosphinate is the most potent mechanism-based substrate-like inhibitor of both the human and Escherichia coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complex
    • Nemeria, N. S., Korotchkina, L. G., Chakraborty, S., Patel, M., and Jordan, F. (2006) Acetylphosphinate is the most potent mechanism-based substrate-like inhibitor of both the human and Escherichia coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complex. Bioorg. Chem. 34, 362-379.
    • (2006) Bioorg. Chem , vol.34 , pp. 362-379
    • Nemeria, N.S.1    Korotchkina, L.G.2    Chakraborty, S.3    Patel, M.4    Jordan, F.5
  • 23
    • 84980118445 scopus 로고
    • Reactions in the pyridine series. II. Some reactions with pyridinealdehydes and cyanopyridines
    • Strell, M., and Kopp, E. (1958) Reactions in the pyridine series. II. Some reactions with pyridinealdehydes and cyanopyridines. Chem. Ber. 91, 1621-1631.
    • (1958) Chem. Ber , vol.91 , pp. 1621-1631
    • Strell, M.1    Kopp, E.2
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 44449095046 scopus 로고    scopus 로고
    • Saturation mutagenesis of putative catalytic residues of benzoylformate decarboxylase provides a challenge to the accepted mechanism
    • Yep, A., Kenyon, G. L., and McLeish, M. J. (2008) Saturation mutagenesis of putative catalytic residues of benzoylformate decarboxylase provides a challenge to the accepted mechanism. Proc. Nat. Acad. Sci. U.S.A. 105, 5733-5738.
    • (2008) Proc. Nat. Acad. Sci. U.S.A , vol.105 , pp. 5733-5738
    • Yep, A.1    Kenyon, G.L.2    McLeish, M.J.3
  • 27
    • 47649132844 scopus 로고    scopus 로고
    • Probing the Active Center of Benzaldehyde Lyase with Substitutions and the Pseudosubstrate Analogue Benzoylphosphonic Acid Methyl Ester
    • Brandt, G. S., Nemeria, N, Chakraborty, S., McLeish, M. J., Yep, A., Kenyon, G. L., Petsko, G. A., Jordan, F., and Ringe, D. (2008) Probing the Active Center of Benzaldehyde Lyase with Substitutions and the Pseudosubstrate Analogue Benzoylphosphonic Acid Methyl Ester. Biochemistry 47, 7734-7743.
    • (2008) Biochemistry , vol.47 , pp. 7734-7743
    • Brandt, G.S.1    Nemeria, N.2    Chakraborty, S.3    McLeish, M.J.4    Yep, A.5    Kenyon, G.L.6    Petsko, G.A.7    Jordan, F.8    Ringe, D.9
  • 28
    • 0021093466 scopus 로고
    • Active Site Directed Irreversible Inactivation of Brewer's Yeast Pyruvate Decarboxylase by the Conjugated Substrate Analog 4(4-Chlorophenyl)-2-oxo-3-butenoic acid
    • Kuo, D. J., and Jordan, F. (1983) Active Site Directed Irreversible Inactivation of Brewer's Yeast Pyruvate Decarboxylase by the Conjugated Substrate Analog 4(4-Chlorophenyl)-2-oxo-3-butenoic acid. Biochemistry 22 3735-3740.
    • (1983) Biochemistry , vol.22 , pp. 3735-3740
    • Kuo, D.J.1    Jordan, F.2
  • 29
    • 0022946325 scopus 로고
    • Conjugated 2 Keto Acids as Mechanism- Based Inactivators of Brewer's Yeast Pyruvate Decarboxylase: Electronic Effects of Substituents and Detection of a Long-lived Intermediate
    • Jordan, F., Adams, J., Farzami, B., and Kudzin, Z. H. (1986) Conjugated 2 Keto Acids as Mechanism- Based Inactivators of Brewer's Yeast Pyruvate Decarboxylase: Electronic Effects of Substituents and Detection of a Long-lived Intermediate". J Enzyme Inhib. 1, 139-144.
    • (1986) J Enzyme Inhib , vol.1 , pp. 139-144
    • Jordan, F.1    Adams, J.2    Farzami, B.3    Kudzin, Z.H.4
  • 30
    • 0024832384 scopus 로고
    • p-Halomethylben-zylidene pyruvic acids inactivate yeast pyruvate decarboxylase by a variety of mechanisms
    • Annan, N, Paris, R., and Jordan, F. (1989) p-Halomethylben-zylidene pyruvic acids inactivate yeast pyruvate decarboxylase by a variety of mechanisms. J. Am. Chem. Soc. 111, 8895-8901.
    • (1989) J. Am. Chem. Soc , vol.111 , pp. 8895-8901
    • Annan, N.1    Paris, R.2    Jordan, F.3
  • 31
    • 64349099301 scopus 로고
    • Ph.D. Dissertation, Rutgers University, Graduate Faculty at Newark
    • Zeng, X. (1992) Ph.D. Dissertation, Rutgers University, Graduate Faculty at Newark.
    • (1992)
    • Zeng, X.1
  • 32
    • 41149172587 scopus 로고    scopus 로고
    • Mechanism of Benzaldehyde Lyase Studied via Thiamin Diphosphate-Bound Intermediates and Kinetic Isotope Effects
    • Chakraborty, S., Nemeria, N, Yep, A., McLeish, M. J., Kenyon, G. L., and Jordan, F. (2008) Mechanism of Benzaldehyde Lyase Studied via Thiamin Diphosphate-Bound Intermediates and Kinetic Isotope Effects. Biochemistry 47, 3800-3809.
    • (2008) Biochemistry , vol.47 , pp. 3800-3809
    • Chakraborty, S.1    Nemeria, N.2    Yep, A.3    McLeish, M.J.4    Kenyon, G.L.5    Jordan, F.6
  • 33
    • 0004202565 scopus 로고
    • Academic Press, New York, San Francisco, London
    • Bernasconi, C. F. (1976) Relaxation Kinetics, pp 24-25, Academic Press, New York, San Francisco, London.
    • (1976) Relaxation Kinetics , pp. 24-25
    • Bernasconi, C.F.1
  • 34
    • 14044251561 scopus 로고    scopus 로고
    • Evidence for Dramatic Acceleration of a C-H Bond Ionization Rate in Thiamin Diphosphate Enzymes by the Protein Environment
    • Zhang, S., Zhou, L., Nemeria, N, Yan, Y., Zhang, Z., Zou, Y., and Jordan, F. (2005) Evidence for Dramatic Acceleration of a C-H Bond Ionization Rate in Thiamin Diphosphate Enzymes by the Protein Environment. Biochemistry 44, 2237-2243.
    • (2005) Biochemistry , vol.44 , pp. 2237-2243
    • Zhang, S.1    Zhou, L.2    Nemeria, N.3    Yan, Y.4    Zhang, Z.5    Zou, Y.6    Jordan, F.7
  • 35
    • 0001128220 scopus 로고
    • Direct Observation of the Kinetic Fate of a ThDP bound Enamine Intermediate on Brewers' Yeast Pyruvate Decarboxylase
    • Zeng, X., Chung, A., Haran, M., and Jordan, F. (1991) Direct Observation of the Kinetic Fate of a ThDP bound Enamine Intermediate on Brewers' Yeast Pyruvate Decarboxylase. J. Am. Chem. Soc. 113, 5842-5849.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 5842-5849
    • Zeng, X.1    Chung, A.2    Haran, M.3    Jordan, F.4
  • 36
    • 37548999032 scopus 로고    scopus 로고
    • Observation of an acryloyl-thiamin diphosphate adduct in the first step of clavulanic acid biosynthesis
    • Merski, M., and Townsend, C. A. (2007) Observation of an acryloyl-thiamin diphosphate adduct in the first step of clavulanic acid biosynthesis. J. Am. Chem. Soc. 129, 15750-15751.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 15750-15751
    • Merski, M.1    Townsend, C.A.2
  • 37
    • 0037177208 scopus 로고    scopus 로고
    • New Model for Activation of Yeast Pyruvate Decarboxylase by Substrate Consistent with the Alternating Sites Mechanism: Demonstration of the Existence of Two Active Forms of the Enzyme
    • Sergienko, E. A., and Jordan, F. (2002) New Model for Activation of Yeast Pyruvate Decarboxylase by Substrate Consistent with the Alternating Sites Mechanism: Demonstration of the Existence of Two Active Forms of the Enzyme. Biochemistry 41, 3952-3967.
    • (2002) Biochemistry , vol.41 , pp. 3952-3967
    • Sergienko, E.A.1    Jordan, F.2
  • 38
    • 0032493736 scopus 로고    scopus 로고
    • High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis
    • Dobritzsch, D., König, S., Schneider, G., and Lu, G. (1998) High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. J. Biol. Chem. 273, 20196-20204.
    • (1998) J. Biol. Chem , vol.273 , pp. 20196-20204
    • Dobritzsch, D.1    König, S.2    Schneider, G.3    Lu, G.4
  • 39
    • 0037031703 scopus 로고    scopus 로고
    • Nitrogenase MoFe-protein at 1.16 Å resolution: A central ligand in the FeMo-cofactor
    • Einsle, O., Tezcan, F. A., Andrade, S. L., Schmid, B., Yoshida, M., Howard, J. B., and Rees, D. C. (2002) Nitrogenase MoFe-protein at 1.16 Å resolution: a central ligand in the FeMo-cofactor. Science 297, 1696-1700.
    • (2002) Science , vol.297 , pp. 1696-1700
    • Einsle, O.1    Tezcan, F.A.2    Andrade, S.L.3    Schmid, B.4    Yoshida, M.5    Howard, J.B.6    Rees, D.C.7
  • 40
    • 36849019179 scopus 로고    scopus 로고
    • Structure of the branched-chain keto acid decarboxylase (KdcA) from Lactococcus lactis provides insights into the structural basis for the chemoselective and enantioselective carboligation reaction
    • Berthold, C. L., Gocke, D., Wood, M. D., Leeper, F. J., Pohl, M., and Schneider, G. (2007) Structure of the branched-chain keto acid decarboxylase (KdcA) from Lactococcus lactis provides insights into the structural basis for the chemoselective and enantioselective carboligation reaction. Acta Crystallogr. D63, 1217-1224.
    • (2007) Acta Crystallogr , vol.D63 , pp. 1217-1224
    • Berthold, C.L.1    Gocke, D.2    Wood, M.D.3    Leeper, F.J.4    Pohl, M.5    Schneider, G.6
  • 41
    • 34447260286 scopus 로고    scopus 로고
    • Crystal-lographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases
    • Berthold, C. L., Toyota, C. G., Moussatche, P., Wood, M. D., Leeper, F., Richards, N. G, and Lindqvist, Y. (2007) Crystal-lographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases. Structure 15, 853-861.
    • (2007) Structure , vol.15 , pp. 853-861
    • Berthold, C.L.1    Toyota, C.G.2    Moussatche, P.3    Wood, M.D.4    Leeper, F.5    Richards, N.G.6    Lindqvist, Y.7
  • 42
    • 33646859093 scopus 로고    scopus 로고
    • A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct
    • Arjunan, P., Sax, M., Brunskill, A., Chandrasekhar, K., Nemeria, N., Zhang, S., Jordan, F., and Furey, W. (2006) A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. J. Biol. Chem. 281, 15296-15303.
    • (2006) J. Biol. Chem , vol.281 , pp. 15296-15303
    • Arjunan, P.1    Sax, M.2    Brunskill, A.3    Chandrasekhar, K.4    Nemeria, N.5    Zhang, S.6    Jordan, F.7    Furey, W.8
  • 43
    • 33646894143 scopus 로고    scopus 로고
    • The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography
    • Wille, G., Meyer, D., Steinmetz, A., Hinze, E., Golbik, R., and Tittmann, K. (2006) The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography. Nat. Chem. Biol. 2, 324-328.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 324-328
    • Wille, G.1    Meyer, D.2    Steinmetz, A.3    Hinze, E.4    Golbik, R.5    Tittmann, K.6
  • 44
    • 35648979411 scopus 로고    scopus 로고
    • Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate
    • Asztalos, P., Parthier, C., Golbik, R., Kleinschmidt, M., Hübner, G., Weiss, M. S., Friedemann, R., Wille, G., and Tittmann, K. (2007) Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate. Biochemistry 46, 12037-12052.
    • (2007) Biochemistry , vol.46 , pp. 12037-12052
    • Asztalos, P.1    Parthier, C.2    Golbik, R.3    Kleinschmidt, M.4    Hübner, G.5    Weiss, M.S.6    Friedemann, R.7    Wille, G.8    Tittmann, K.9
  • 45
    • 0013140574 scopus 로고
    • Synthesis and crystal-structure of an analog of 2-(alpha-lactyl)thiamin, racemic methyl 2-hydroxy-2-(2-thiamin)ethylphos-phonate chloride trihydrate - a conformation for a least-motion, maximum-overlap mechanism for thiamin catalysis
    • Turano, A., Furey, W., Pletcher, J., Sax, M., Pike, D., and Kluger, R. (1982) Synthesis and crystal-structure of an analog of 2-(alpha-lactyl)thiamin, racemic methyl 2-hydroxy-2-(2-thiamin)ethylphos-phonate chloride trihydrate - a conformation for a least-motion, maximum-overlap mechanism for thiamin catalysis. J. Am. Chem. Soc. 104, 3089-3095.
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 3089-3095
    • Turano, A.1    Furey, W.2    Pletcher, J.3    Sax, M.4    Pike, D.5    Kluger, R.6


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