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Volumn 25, Issue 2, 2011, Pages 497-504

Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: New insights from structural and biochemical studies on human RPE

Author keywords

Metalloenzyme; Oxidative stress; Pentose phospate pathway

Indexed keywords

ALANINE; ASPARTIC ACID; DEXTRO RIBULOSE 5 PHOSPHATE 3 EPIMERASE; DEXTRO XYLULOSE 5 PHOSPHATE; EPIMERASE; FERROUS ION; SERINE; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG;

EID: 79551616370     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.10-171207     Document Type: Article
Times cited : (24)

References (26)
  • 1
    • 0013500827 scopus 로고
    • d-Ribulose 5-phosphate 3-epimerase
    • Wood, W. A., ed., Academic Press, New York
    • Williamson, W. T., and Wood, W. A. (1966) d-Ribulose 5-phosphate 3-epimerase. In Methods of Enzymology, Vol. 9 (Wood, W. A., ed.), Academic Press, New York
    • (1966) Methods of Enzymology , vol.9
    • Williamson, W.T.1    Wood, W.2
  • 2
    • 0029556742 scopus 로고
    • Cloning of the amphibolic Calvin cycle/OPPP enzyme d-ribulose-5-phosphate 3-epimerase (EC 5.1.3.1) from spinach chloroplasts: Functional and evolutionary aspects
    • Nowitzki, U., Wyrich, R., Westhoff, P., Henze, K., Schnarrenberger, C., and Martin, W. (1995) Cloning of the amphibolic Calvin cycle/OPPP enzyme d-ribulose-5-phosphate 3-epimerase (EC 5.1.3.1) from spinach chloroplasts: functional and evolutionary aspects. Plant Mol. Biol. 29, 1279-1291
    • (1995) Plant Mol. Biol. , vol.29 , pp. 1279-1291
    • Nowitzki, U.1    Wyrich, R.2    Westhoff, P.3    Henze, K.4    Schnarrenberger, C.5    Martin, W.6
  • 3
    • 0037795745 scopus 로고    scopus 로고
    • The oxidative pentose phosphate pathway: Structure and organisation
    • Kruger, N. J., and von Schaewen, A. (2003) The oxidative pentose phosphate pathway: structure and organisation. Curr. Op. Plant Biol. 6, 236-246
    • (2003) Curr. Op. Plant Biol. , vol.6 , pp. 236-246
    • Kruger, N.J.1    Von Schaewen, A.2
  • 5
    • 0022803107 scopus 로고
    • Physiological functions of the pentose phosphate pathway
    • Wood, T. (1986) Physiological functions of the pentose phosphate pathway. Cell. Biochem. Funct. 4, 241-247
    • (1986) Cell. Biochem. Funct. , vol.4 , pp. 241-247
    • Wood, T.1
  • 6
    • 2342487990 scopus 로고    scopus 로고
    • Cells have distinct mechanisms to maintain protection against different reactive oxygen species: Oxidative-stress-response genes
    • Thorpe, G. W., Fong, C. S., Alic, N., Higgins, V. J., and Dawes, I. W. (2004) Cells have distinct mechanisms to maintain protection against different reactive oxygen species: oxidative-stress-response genes. Proc. Natl. Acad. Sci. U. S. A. 101, 6564-6569
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 6564-6569
    • Thorpe, G.W.1    Fong, C.S.2    Alic, N.3    Higgins, V.J.4    Dawes, I.W.5
  • 7
    • 0029829625 scopus 로고    scopus 로고
    • Mutants that show increased sensitivity to hydrogen peroxide reveal an important role for the pentose phosphate pathway in protection of yeast against oxidative stress
    • Juhnke, H., Krems, B., Kötter, P., and Entian, K. (1996) Mutants that show increased sensitivity to hydrogen peroxide reveal an important role for the pentose phosphate pathway in protection of yeast against oxidative stress. Mol. Gen. Genet. MGG 252, 456-464
    • (1996) Mol. Gen. Genet. MGG , vol.252 , pp. 456-464
    • Juhnke, H.1    Krems, B.2    Kötter, P.3    Entian, K.4
  • 8
    • 39949084153 scopus 로고    scopus 로고
    • Adaptation to hydrogen peroxide in Saccharomyces cerevisiae: The role of NADPH-generating systems and the SKN7 transcription factor
    • Ng, C.-H., Tan, S.-X., Perrone, G. G., Thorpe, G. W., Higgins, V. J., and Dawes, I. W. (2008) Adaptation to hydrogen peroxide in Saccharomyces cerevisiae: the role of NADPH-generating systems and the SKN7 transcription factor. Free Radical Biol. Med. 44, 1131-1145
    • (2008) Free Radical Biol. Med. , vol.44 , pp. 1131-1145
    • Ng, C.-H.1    Tan, S.-X.2    Perrone, G.G.3    Thorpe, G.W.4    Higgins, V.J.5    Dawes, I.W.6
  • 9
    • 65249134998 scopus 로고    scopus 로고
    • Cu, Zn superoxide dismutase and NADP(H) homeostasis are required for tolerance of endoplasmic reticulum stress in Saccharomyces cerevisiae
    • Tan, S.-X., Teo, M., Lam, Y. T., Dawes, I. W., and Perrone, G. G. (2009) Cu, Zn superoxide dismutase and NADP(H) homeostasis are required for tolerance of endoplasmic reticulum stress in Saccharomyces cerevisiae. Mol. Biol. Cell 20, 1493-1508
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1493-1508
    • Tan, S.-X.1    Teo, M.2    Lam, Y.T.3    Dawes, I.W.4    Perrone, G.G.5
  • 10
    • 33644499463 scopus 로고    scopus 로고
    • d-Ribulose 5-phosphate 3-epimerase: Functional and structural relationships to members of the ribulose-phosphate binding (β/α)8- barrel superfamily
    • Akana, J., Fedorov, A. A., Fedorov, E., Novak, W. R. P., Babbitt, P. C., Almo, S. C., and Gerlt, J. A. (2006) d-Ribulose 5-phosphate 3-epimerase: functional and structural relationships to members of the ribulose-phosphate binding (β/α)8-barrel superfamily. Biochemistry 45, 2493-2503
    • (2006) Biochemistry , vol.45 , pp. 2493-2503
    • Akana, J.1    Fedorov, A.A.2    Fedorov, E.3    Novak, W.R.P.4    Babbitt, P.C.5    Almo, S.C.6    Gerlt, J.A.7
  • 11
    • 0037423701 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of the cytosolic d-ribulose-5- Phosphate 3-epimerase from rice
    • Jelakovic, S., Kopriva, S., Süss, K.-H., and Schulz, G. E. (2003) structure and catalytic mechanism of the cytosolic d-ribulose-5- phosphate 3-epimerase from rice. J. Mol. Biol. 326, 127-135
    • (2003) J. Mol. Biol. , vol.326 , pp. 127-135
    • Jelakovic, S.1    Kopriva, S.2    Süss, K.-H.3    Schulz, G.E.4
  • 12
    • 16644398999 scopus 로고    scopus 로고
    • Structure of d-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 a resolution
    • Wise, E. L., Akana, J., Gerlt, J. A., and Rayment, I. (2004) Structure of d-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 A resolution. Acta Crystallogr. D 60, 1687-1690
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1687-1690
    • Wise, E.L.1    Akana, J.2    Gerlt, J.A.3    Rayment, I.4
  • 14
    • 0033537899 scopus 로고    scopus 로고
    • Structure and mechanism of the amphibolic enzyme -ribulose- 5-phosphate 3-epimerase from potato chloroplasts
    • Kopp, J., Kopriva, S., Süss, K.-H., and Schulz, G. E. (1999) Structure and mechanism of the amphibolic enzyme -ribulose- 5-phosphate 3-epimerase from potato chloroplasts. J. Mol. Biol. 287, 761-771
    • (1999) J. Mol. Biol. , vol.287 , pp. 761-771
    • Kopp, J.1    Kopriva, S.2    Süss, K.-H.3    Schulz, G.E.4
  • 15
    • 0033593204 scopus 로고    scopus 로고
    • Identification of a catalytic aspartyl residue of d-ribulose 5-phosphate 3-epimerase by site-directed mutagenesis
    • Chen, Y.-R., Larimer, F. W., Serpersu, E. H., and Hartman, F. C. (1999) Identification of a catalytic aspartyl residue of d-ribulose 5-phosphate 3-epimerase by site-directed mutagenesis. J. Biol. Chem. 274, 2132-2136
    • (1999) J. Biol. Chem. , vol.274 , pp. 2132-2136
    • Chen, Y.-R.1    Larimer, F.W.2    Serpersu, E.H.3    Hartman, F.C.4
  • 16
    • 0015523705 scopus 로고
    • On the mechanism of the pentose phosphate epimerases
    • Davies, L., Lee, N., and Glaser, L. (1972) On the mechanism of the pentose phosphate epimerases. J. Biol. Chem. 247, 5862-5866
    • (1972) J. Biol. Chem. , vol.247 , pp. 5862-5866
    • Davies, L.1    Lee, N.2    Glaser, L.3
  • 17
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 20
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 21
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 24
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 25
    • 20444415235 scopus 로고    scopus 로고
    • Complex cellular responses to reactive oxygen species
    • Temple, M. D., Perrone, G. G., and Dawes, I. W. (2005) Complex cellular responses to reactive oxygen species. Trends Cell. Biol. 15, 319-326
    • (2005) Trends Cell. Biol. , vol.15 , pp. 319-326
    • Temple, M.D.1    Perrone, G.G.2    Dawes, I.W.3
  • 26
    • 18544371009 scopus 로고    scopus 로고
    • Metals, toxicity and oxidative stress
    • Valko, M., Morris, H., and Cronin, M. T. D. (2005) Metals, toxicity and oxidative stress. Curr. Med. Chem. 12, 1161-1208
    • (2005) Curr. Med. Chem. , vol.12 , pp. 1161-1208
    • Valko, M.1    Morris, H.2    Cronin, M.T.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.