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Volumn 4, Issue 2, 2008, Pages 113-118

Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes

Author keywords

[No Author keywords available]

Indexed keywords

COCARBOXYLASE; GLUTAMIC ACID; GLYOXYLIC ACID CARBOLIGASE; GLYOXYLIC ACID DERIVATIVE; LIGASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; THIAZOLE; UNCLASSIFIED DRUG; VALINE;

EID: 38349004540     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.62     Document Type: Article
Times cited : (51)

References (44)
  • 1
    • 0027918180 scopus 로고
    • A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase
    • Muller, Y.A. et al. A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase. Structure 1, 95-103 (1993).
    • (1993) Structure , vol.1 , pp. 95-103
    • Muller, Y.A.1
  • 2
    • 0031013992 scopus 로고    scopus 로고
    • How thiamine diphosphate is activated in enzymes
    • Kern, D. et al. How thiamine diphosphate is activated in enzymes. Science 275, 67-70 (1997).
    • (1997) Science , vol.275 , pp. 67-70
    • Kern, D.1
  • 3
    • 3142640259 scopus 로고
    • On the mechanism of thiamine action: IV. Evidence from studies on model systems
    • Breslow, R. On the mechanism of thiamine action: IV. Evidence from studies on model systems. J. Am. Chem. Soc. 80, 3719-3726 (1958).
    • (1958) J. Am. Chem. Soc , vol.80 , pp. 3719-3726
    • Breslow, R.1
  • 4
    • 84971097881 scopus 로고
    • Structure and mechanism of action of the active center of yeast pyruvate decarboxylase
    • Schellenberger, A. Structure and mechanism of action of the active center of yeast pyruvate decarboxylase. Angew. Chem. Int. Ed. Engl. 6, 1024-1035 (1967).
    • (1967) Angew. Chem. Int. Ed. Engl , vol.6 , pp. 1024-1035
    • Schellenberger, A.1
  • 5
    • 33646894143 scopus 로고    scopus 로고
    • The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography
    • Wille, G. et al. The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography. Nat. Chem. Biol. 2, 324-328 (2006).
    • (2006) Nat. Chem. Biol , vol.2 , pp. 324-328
    • Wille, G.1
  • 6
    • 0013881668 scopus 로고
    • Glyoxylate carboligase of Escherichia coli: Some properties of the enzyme
    • Gupta, N. & Vennesland, B. Glyoxylate carboligase of Escherichia coli: some properties of the enzyme. Arch. Biochem. Biophys. 113, 255-264 (1966).
    • (1966) Arch. Biochem. Biophys , vol.113 , pp. 255-264
    • Gupta, N.1    Vennesland, B.2
  • 7
    • 0001279638 scopus 로고
    • Conversion of glyoxylate to hydroxypyruvate by extracts of Escherichia coli
    • Krakow, G. & Barkulis, S.S. Conversion of glyoxylate to hydroxypyruvate by extracts of Escherichia coli. Biochim. Biophys. Acta 21, 593-594 (1956).
    • (1956) Biochim. Biophys. Acta , vol.21 , pp. 593-594
    • Krakow, G.1    Barkulis, S.S.2
  • 8
    • 0038360240 scopus 로고
    • The metabolism of C2 compounds in micro-organisms. 7. Preparation and properties of crystalline tartronic semialdehyde reductase
    • Gotto, A.M. & Kornberg, H.L. The metabolism of C2 compounds in micro-organisms. 7. Preparation and properties of crystalline tartronic semialdehyde reductase. Biochem. J. 81, 273-284 (1961).
    • (1961) Biochem. J , vol.81 , pp. 273-284
    • Gotto, A.M.1    Kornberg, H.L.2
  • 9
    • 20444426493 scopus 로고    scopus 로고
    • Monitoring the acetohydroxy acid synthase reaction and related carboligations by circular dichroism spectroscopy
    • Vinogradov, M. et al. Monitoring the acetohydroxy acid synthase reaction and related carboligations by circular dichroism spectroscopy. Anal. Biochem. 342, 126-133 (2005).
    • (2005) Anal. Biochem , vol.342 , pp. 126-133
    • Vinogradov, M.1
  • 10
    • 0344735908 scopus 로고
    • Glyoxylic acid carboligase: An enzyme present in glycolate-grown Escherichia coli
    • Krakow, G., Barkulis, S.S. & Hayashi, J.A. Glyoxylic acid carboligase: an enzyme present in glycolate-grown Escherichia coli. J. Bacteriol. 81, 509-518 (1961).
    • (1961) J. Bacteriol , vol.81 , pp. 509-518
    • Krakow, G.1    Barkulis, S.S.2    Hayashi, J.A.3
  • 11
    • 0020559855 scopus 로고
    • Glyoxylate conversion by Hyphomicrobium species grown on allantoin as nitrogen source
    • Van der Drift, C. & De Windt, F.E. Glyoxylate conversion by Hyphomicrobium species grown on allantoin as nitrogen source. Antonie Van Leeuwenhoek 49, 167-172 (1983).
    • (1983) Antonie Van Leeuwenhoek , vol.49 , pp. 167-172
    • Van der Drift, C.1    De Windt, F.E.2
  • 12
    • 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. et al. The 1′,4′-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes. Proc. Natl. Acad. Sci. USA 104, 78-82 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 78-82
    • Nemeria, N.1
  • 13
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W.A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58 (1991).
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 14
    • 33748345821 scopus 로고    scopus 로고
    • Domain relationships in thiamine diphosphate-dependent enzymes
    • Duggleby, R.G. Domain relationships in thiamine diphosphate-dependent enzymes. Acc. Chem. Res. 39, 550-557 (2006).
    • (2006) Acc. Chem. Res , vol.39 , pp. 550-557
    • Duggleby, R.G.1
  • 15
    • 28244449299 scopus 로고    scopus 로고
    • Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens
    • Mosbacher, T.G., Mueller, M. & Schulz, G.E. Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens. FEBS J. 272, 6067-6076 (2005).
    • (2005) FEBS J , vol.272 , pp. 6067-6076
    • Mosbacher, T.G.1    Mueller, M.2    Schulz, G.E.3
  • 16
    • 0027195094 scopus 로고
    • Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4 Å resolution
    • Dyda, F. et al. Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4 Å resolution. Biochemistry 32, 6165-6170 (1993).
    • (1993) Biochemistry , vol.32 , pp. 6165-6170
    • Dyda, F.1
  • 17
    • 0027140297 scopus 로고
    • Thiamin diphosphate dependent enzymes: Transketolase, pyruvate oxidase and pyruvate decarboxylase
    • Lindqvist, Y. & Schneider, G. Thiamin diphosphate dependent enzymes: transketolase, pyruvate oxidase and pyruvate decarboxylase. Curr. Opin. Struct. Biol. 3, 896-901 (1993).
    • (1993) Curr. Opin. Struct. Biol , vol.3 , pp. 896-901
    • Lindqvist, Y.1    Schneider, G.2
  • 18
    • 0026762799 scopus 로고
    • Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 resolution
    • Lindqvist, Y., Schneider, G., Ermler, U. & Sundstrom, M. Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 resolution. EMBO J. 11, 2373-2379 (1992).
    • (1992) EMBO J , vol.11 , pp. 2373-2379
    • Lindqvist, Y.1    Schneider, G.2    Ermler, U.3    Sundstrom, M.4
  • 19
    • 0000170889 scopus 로고
    • Die Funktion der 4′-Aminopyrimidin-Komponente im Katalysemechanismus von Thiamin pyrophosphat-Enzymen aus heutiger Sicht
    • Schellenberger, A. Die Funktion der 4′-Aminopyrimidin-Komponente im Katalysemechanismus von Thiamin pyrophosphat-Enzymen aus heutiger Sicht. Chem. Ber. 123, 1489-1494 (1990).
    • (1990) Chem. Ber , vol.123 , pp. 1489-1494
    • Schellenberger, A.1
  • 20
    • 0035797880 scopus 로고    scopus 로고
    • Binding and activation of thiamin diphosphate in acetohydroxyacid synthase
    • Bar-Ilan, A. et al. Binding and activation of thiamin diphosphate in acetohydroxyacid synthase. Biochemistry 40, 11946-11954 (2001).
    • (2001) Biochemistry , vol.40 , pp. 11946-11954
    • Bar-Ilan, A.1
  • 21
    • 0026013077 scopus 로고
    • Function of the aminopyrimidine part in thiamine pyrophosphate enzymes
    • Golbik, R. et al. Function of the aminopyrimidine part in thiamine pyrophosphate enzymes. Bioorg. Chem. 19, 10-17 (1991).
    • (1991) Bioorg. Chem , vol.19 , pp. 10-17
    • Golbik, R.1
  • 22
    • 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. et al. 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).
    • (2004) Biochemistry , vol.43 , pp. 6565-6575
    • Nemeria, N.1
  • 23
    • 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. et al. 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).
    • (2007) Biochemistry , vol.46 , pp. 10739-10744
    • Nemeria, N.1
  • 24
    • 14144249867 scopus 로고    scopus 로고
    • The carboligation reaction of acetohydroxyacid synthase II: Steady-state intermediate distributions in wild type and mutants by NMR
    • Tittmann, K., Vyazmensky, M., Hubner, G., Barak, Z. & Chipman, D.M. The carboligation reaction of acetohydroxyacid synthase II: steady-state intermediate distributions in wild type and mutants by NMR. Proc. Natl. Acad. Sci. USA 102, 553-558 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 553-558
    • Tittmann, K.1    Vyazmensky, M.2    Hubner, G.3    Barak, Z.4    Chipman, D.M.5
  • 25
    • 0017072736 scopus 로고
    • Transition state analogs for thiamin pyrophosphate-dependent enzymes
    • Gutowski, J.A. & Lienhard, G.E. Transition state analogs for thiamin pyrophosphate-dependent enzymes. J. Biol. Chem. 251, 2863-2866 (1976).
    • (1976) J. Biol. Chem , vol.251 , pp. 2863-2866
    • Gutowski, J.A.1    Lienhard, G.E.2
  • 26
    • 0014958369 scopus 로고
    • Base catalysis of thiazolium salt hydrogen exchange and its implications for enzymatic thiamine cofactor catalysis
    • Kemp, D.S. & O'Brien, J.T. Base catalysis of thiazolium salt hydrogen exchange and its implications for enzymatic thiamine cofactor catalysis. J. Am. Chem. Soc. 92, 2554-2555 (1970).
    • (1970) J. Am. Chem. Soc , vol.92 , pp. 2554-2555
    • Kemp, D.S.1    O'Brien, J.T.2
  • 27
    • 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. et al. Evidence for dramatic acceleration of a C-H bond ionization rate in thiamin diphosphate enzymes by the protein environment. Biochemistry 44, 2237-2243 (2005).
    • (2005) Biochemistry , vol.44 , pp. 2237-2243
    • Zhang, S.1
  • 28
    • 11144246292 scopus 로고    scopus 로고
    • Zhang, S., Liu, M., Yan, Y., Zhang, Z. & Jordan, F. C2-alpha-lactylthiamin diphosphate is an intermediate on the pathway of thiamin diphosphate-dependent pyruvate decarboxylation. Evidence on enzymes and models. J. Biol. Chem. 279, 54312-54318 (2004).
    • Zhang, S., Liu, M., Yan, Y., Zhang, Z. & Jordan, F. C2-alpha-lactylthiamin diphosphate is an intermediate on the pathway of thiamin diphosphate-dependent pyruvate decarboxylation. Evidence on enzymes and models. J. Biol. Chem. 279, 54312-54318 (2004).
  • 29
    • 0033580678 scopus 로고    scopus 로고
    • Remarkable stabilization of zwitterionic intermediates may account for a billion-fold rate acceleration by thiamin diphosphate-dependent decarboxylases
    • Jordan, F., Li, H. & Brown, A. Remarkable stabilization of zwitterionic intermediates may account for a billion-fold rate acceleration by thiamin diphosphate-dependent decarboxylases. Biochemistry 38, 6369-6373 (1999).
    • (1999) Biochemistry , vol.38 , pp. 6369-6373
    • Jordan, F.1    Li, H.2    Brown, A.3
  • 30
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne, G.D., Standaert, R.F., Karplus, P.A., Schreiber, S.L. & Clardy, J. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229, 105-124 (1993).
    • (1993) J. Mol. Biol , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 31
    • 0015245103 scopus 로고
    • Glyoxylate carboligase of Pseudomonas oxalaticus. A possible structural role for flavine-adenine dinucleotide
    • Chung, S.T., Tan, R.T. & Suzuki, I. Glyoxylate carboligase of Pseudomonas oxalaticus. A possible structural role for flavine-adenine dinucleotide. Biochemistry 10, 1205-1209 (1971).
    • (1971) Biochemistry , vol.10 , pp. 1205-1209
    • Chung, S.T.1    Tan, R.T.2    Suzuki, I.3
  • 32
    • 0027417393 scopus 로고
    • Molecular cloning, DNA sequencing, and biochemical analyses of Escherichia coli glyoxylate carboligase: An enzyme of the acetohydroxy acid synthase-pyruvate oxidase family
    • Chang, Y.Y., Wang, A.Y. & Cronan, J.E., Jr. Molecular cloning, DNA sequencing, and biochemical analyses of Escherichia coli glyoxylate carboligase: an enzyme of the acetohydroxy acid synthase-pyruvate oxidase family. J. Biol. Chem. 268, 3911-3919 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 3911-3919
    • Chang, Y.Y.1    Wang, A.Y.2    Cronan Jr., J.E.3
  • 33
    • 0000579231 scopus 로고
    • Origin of the herbicide binding site of acetolactate synthase
    • Schloss, J.V., Ciskanik, L.M. & Van Dyk, D.E. Origin of the herbicide binding site of acetolactate synthase. Nature 331, 360-362 (1988).
    • (1988) Nature , vol.331 , pp. 360-362
    • Schloss, J.V.1    Ciskanik, L.M.2    Van Dyk, D.E.3
  • 34
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800 (1993).
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 35
    • 0028103275 scopus 로고
    • Number 4. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr , vol.50 , pp. 760-763
  • 37
    • 0031058188 scopus 로고    scopus 로고
    • Maximum likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de la Fortelle, E. & Bricogne, G. Maximum likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997).
    • (1997) Methods Enzymol , vol.276 , pp. 472-494
    • de la Fortelle, E.1    Bricogne, G.2
  • 38
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 40
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software for macromolecular structure determination
    • Brünger, A. et al. Crystallography and NMR system: a new software for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr , vol.54 , pp. 905-921
    • Brünger, A.1
  • 41
    • 0347383757 scopus 로고    scopus 로고
    • New tools and data for improving structures, using all-atom contacts
    • Richardson, J.S., Arendall, W.B., III & Richardson, D.C. New tools and data for improving structures, using all-atom contacts. Methods Enzymol. 374, 385-412 (2003).
    • (2003) Methods Enzymol , vol.374 , pp. 385-412
    • Richardson, J.S.1    Arendall III, W.B.2    Richardson, D.C.3
  • 42
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138 (1993).
    • (1993) J. Mol. Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 43
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - a visualization system for exploratory research and analysis
    • Pettersen, E.F. et al. UCSF Chimera - a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 44
    • 0038724492 scopus 로고    scopus 로고
    • NMR analysis of covalent intermediates in thiamin diphosphate enzymes
    • Tittmann, K. et al. NMR analysis of covalent intermediates in thiamin diphosphate enzymes. Biochemistry 42, 7885-7891 (2003).
    • (2003) Biochemistry , vol.42 , pp. 7885-7891
    • Tittmann, K.1


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