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Volumn 46, Issue 13, 2007, Pages 4077-4089

Mechanistic diversity in the RuBisCO superfamily: The "enolase" in the methionine salvage pathway in Geobacillus kaustophilus

Author keywords

[No Author keywords available]

Indexed keywords

CARBAMATE OXYGEN; GEOBACILLUS KAUSTOPHILUS; HETEROFUNCTIONAL HOMOLOGUES; METHIONINE SALVAGE PATHWAYS;

EID: 34047237283     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7000483     Document Type: Article
Times cited : (52)

References (29)
  • 1
    • 0027367423 scopus 로고
    • Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae
    • Myers, R. W., Wray, J. W., Fish, S., and Abeles, R. H. (1993) Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae, J. Biol. Chem. 268, 24785-24791.
    • (1993) J. Biol. Chem , vol.268 , pp. 24785-24791
    • Myers, R.W.1    Wray, J.W.2    Fish, S.3    Abeles, R.H.4
  • 2
    • 0027436432 scopus 로고
    • Appendix. Cloning and sequence of the gene encoding enzyme E-1 from the methionine salvage pathway of Klebsiella oxytoca
    • Balakrishnan, R., Frohlich, M., Rahaim, P. T., Backman, K., and Yocum, R. R. (1993) Appendix. Cloning and sequence of the gene encoding enzyme E-1 from the methionine salvage pathway of Klebsiella oxytoca, J. Biol. Chem. 268, 24792-24795.
    • (1993) J. Biol. Chem , vol.268 , pp. 24792-24795
    • Balakrishnan, R.1    Frohlich, M.2    Rahaim, P.T.3    Backman, K.4    Yocum, R.R.5
  • 4
    • 9744279773 scopus 로고    scopus 로고
    • Divergent evolution in the enolase superfamily: The interplay of mechanism and specificity
    • Gerlt, J. A., Babbitt, P. C., and Rayment, I. (2005) Divergent evolution in the enolase superfamily: The interplay of mechanism and specificity, Arch. Biochem. Biophys. 433, 59-70.
    • (2005) Arch. Biochem. Biophys , vol.433 , pp. 59-70
    • Gerlt, J.A.1    Babbitt, P.C.2    Rayment, I.3
  • 6
    • 0042859759 scopus 로고    scopus 로고
    • The relationship between side reactions and slow inhibition of ribulose-bisphosphate carboxylase revealed by a loop 6 mutant of the tobacco enzyme
    • Pearce, F. G., and Andrews, T. J. (2003) The relationship between side reactions and slow inhibition of ribulose-bisphosphate carboxylase revealed by a loop 6 mutant of the tobacco enzyme, J. Biol. Chem. 278, 32526-32536.
    • (2003) J. Biol. Chem , vol.278 , pp. 32526-32536
    • Pearce, F.G.1    Andrews, T.J.2
  • 7
    • 0141993683 scopus 로고    scopus 로고
    • A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO
    • Ashida, H., Saito, Y., Kojima, C., Kobayashi, K., Ogasawara, N., and Yokota, A. (2003) A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO, Science 302, 286-290.
    • (2003) Science , vol.302 , pp. 286-290
    • Ashida, H.1    Saito, Y.2    Kojima, C.3    Kobayashi, K.4    Ogasawara, N.5    Yokota, A.6
  • 8
    • 0347506350 scopus 로고    scopus 로고
    • Insights into the stress response and sulfur metabolism revealed by proteome analysis of a Chlorobium tepidum mutant lacking the RuBisCO-like protein
    • Hanson, T. E., and Tabita, F. R. (2003) Insights into the stress response and sulfur metabolism revealed by proteome analysis of a Chlorobium tepidum mutant lacking the RuBisCO-like protein, Photosynth. Res. 78, 231-248.
    • (2003) Photosynth. Res , vol.78 , pp. 231-248
    • Hanson, T.E.1    Tabita, F.R.2
  • 9
    • 18944389308 scopus 로고    scopus 로고
    • Crystal structure of a RuBisCO-like protein from the green sulfur bacterium Chlorobium tepidum
    • Li, H., Sawaya, M. R., Tabita, F. R., and Eisenberg, D. (2005) Crystal structure of a RuBisCO-like protein from the green sulfur bacterium Chlorobium tepidum, Structure 13, 779-789.
    • (2005) Structure , vol.13 , pp. 779-789
    • Li, H.1    Sawaya, M.R.2    Tabita, F.R.3    Eisenberg, D.4
  • 10
    • 0034923923 scopus 로고    scopus 로고
    • Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies
    • Gerlt, J. A., and Babbitt, P. C. (2001) Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies, Annu. Rev. Biochem. 70, 209-246.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 209-246
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 11
    • 0023718385 scopus 로고
    • Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae
    • Furfine, E. S., and Abeles, R. H. (1988) Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae, J. Biol. Chem. 263, 9598-9606.
    • (1988) J. Biol. Chem , vol.263 , pp. 9598-9606
    • Furfine, E.S.1    Abeles, R.H.2
  • 13
    • 0028116826 scopus 로고
    • Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search
    • Koonin, E. V., and Tatusov, R. L. (1994) Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search, J. Mol. Biol. 244, 125-132.
    • (1994) J. Mol. Biol , vol.244 , pp. 125-132
    • Koonin, E.V.1    Tatusov, R.L.2
  • 14
    • 17444387092 scopus 로고    scopus 로고
    • Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity
    • Wang, H., Pang, H., Bartlam, M., and Rao, Z. (2005) Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity, J. Mol. Biol. 348, 917-926.
    • (2005) J. Mol. Biol , vol.348 , pp. 917-926
    • Wang, H.1    Pang, H.2    Bartlam, M.3    Rao, Z.4
  • 15
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phosphatases
    • Ames, B. N. (1966) Assay of inorganic phosphate, total phosphate and phosphatases, Methods Enzymol. 8, 115-118.
    • (1966) Methods Enzymol , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 16
    • 0016410895 scopus 로고
    • Colorimetric ultramicro assay for reducing sugars
    • Avidad, G. (1975) Colorimetric ultramicro assay for reducing sugars, Methods Enzymol. 41, 27-29.
    • (1975) Methods Enzymol , vol.41 , pp. 27-29
    • Avidad, G.1
  • 17
    • 13544277381 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: Enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase
    • Yew, W. S., Akana, J., Wise, E. L., Rayment, I., and Gerlt, J. A. (2005) Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: Enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase, Biochemistry 44, 1807-1815.
    • (2005) Biochemistry , vol.44 , pp. 1807-1815
    • Yew, W.S.1    Akana, J.2    Wise, E.L.3    Rayment, I.4    Gerlt, J.A.5
  • 18
    • 6444240139 scopus 로고    scopus 로고
    • Isopolar phosphonate analogue of adenosine diphosphate ribose
    • Van derpoorten, K., and Migaud, M. E. (2004) Isopolar phosphonate analogue of adenosine diphosphate ribose, Org. Lett. 6, 3461-3464.
    • (2004) Org. Lett , vol.6 , pp. 3461-3464
    • Van derpoorten, K.1    Migaud, M.E.2
  • 19
    • 0025043264 scopus 로고
    • Conversion of 5-S-methyl-5-thio-D- ribose to methionine in Klebsiella pneumoniae. Stable isotope incorporation studies of the terminal enzymatic reactions in the pathway
    • Myers, R. W., and Abeles, R. H. (1990) Conversion of 5-S-methyl-5-thio-D- ribose to methionine in Klebsiella pneumoniae. Stable isotope incorporation studies of the terminal enzymatic reactions in the pathway, J. Biol. Chem. 265, 16913-16921.
    • (1990) J. Biol. Chem , vol.265 , pp. 16913-16921
    • Myers, R.W.1    Abeles, R.H.2
  • 20
    • 2942753912 scopus 로고    scopus 로고
    • Analogs of 1-phosphonooxy-2,2-dihydroxy-3-oxo-5(methylthio)pentane, an acyclic intermediate in the methionine salvage pathway: A new preparation and characterization of activity with E1 enolase/phosphatase from Klebsiella oxytoca
    • Zhang, Y., Heinsen, M. H., Kostic, M., Pagani, G. M., Riera, T. V., Perovic, I., Hedstrom, L., Snider, B. B., and Pochapsky, T. C. (2004) Analogs of 1-phosphonooxy-2,2-dihydroxy-3-oxo-5(methylthio)pentane, an acyclic intermediate in the methionine salvage pathway: A new preparation and characterization of activity with E1 enolase/phosphatase from Klebsiella oxytoca, Bioorg. Med. Chem. 12, 3847-3855.
    • (2004) Bioorg. Med. Chem , vol.12 , pp. 3847-3855
    • Zhang, Y.1    Heinsen, M.H.2    Kostic, M.3    Pagani, G.M.4    Riera, T.V.5    Perovic, I.6    Hedstrom, L.7    Snider, B.B.8    Pochapsky, T.C.9
  • 21
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter, C. W. J, Sweet, R. M, Abelson, J. N, and Simon, M. I, Eds, pp, Academic Pres, New York
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, in Methods in Enzymology (Carter, C. W. J., Sweet, R. M., Abelson, J. N., and Simon, M. I., Eds.) pp 307-326, Academic Pres, New York.
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger, T. C., and Berendzen, J. (1999) Automated MAD and MIR structure solution, Acta Crystallogr. D55, 849-861.
    • (1999) Acta Crystallogr , vol.D55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 23
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger, T. C. (2000) Maximum-likelihood density modification, Acta Crystallogr. D56, 965-972.
    • (2000) Acta Crystallogr , vol.D56 , pp. 965-972
    • Terwilliger, T.C.1
  • 24
    • 0022333120 scopus 로고
    • Interactive computer graphics: FRODO
    • Jones, A. T. (1985) Interactive computer graphics: FRODO, Methods Enzymol. 115, 157-171.
    • (1985) Methods Enzymol , vol.115 , pp. 157-171
    • Jones, A.T.1
  • 27
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V. S., and Wilson, K. S. (1993) Automated refinement of protein models, Acta Crystallogr. D49, 129-147.
    • (1993) Acta Crystallogr , vol.D49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 28
    • 0017253134 scopus 로고
    • The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications
    • Lorimer, G. H., Badger, M. R., and Andrews, T. J. (1976) The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications, Biochemistry 15, 529-536.
    • (1976) Biochemistry , vol.15 , pp. 529-536
    • Lorimer, G.H.1    Badger, M.R.2    Andrews, T.J.3
  • 29
    • 0030003964 scopus 로고    scopus 로고
    • Large structures at high resolution: The 1.6 Å crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate
    • Andersson, I. (1996) Large structures at high resolution: The 1.6 Å crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate, J. Mol. Biol. 259, 160-174.
    • (1996) J. Mol. Biol , vol.259 , pp. 160-174
    • Andersson, I.1


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