메뉴 건너뛰기




Volumn 87, Issue 8, 2005, Pages 763-769

Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: Comparison with the archaeal and bacterial enzymes

Author keywords

Crystal structure; Ribose 5 phosphate isomerase; Sugar metabolism; Yeast

Indexed keywords

ARGININE; BACTERIAL ENZYME; FUNGAL ENZYME; ISOMERASE; LYSINE; RIBOSEPHOSPHATE ISOMERASE; TETRAMER; UNCLASSIFIED DRUG;

EID: 23044486735     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2005.03.001     Document Type: Article
Times cited : (16)

References (20)
  • 1
    • 0030060223 scopus 로고    scopus 로고
    • Ribose catabolism of Escherichia coli: Characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression
    • K.I. Sorensen, and B. Hove-Jensen Ribose catabolism of Escherichia coli: characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression J. Bacteriol. 178 1996 1003 1011
    • (1996) J. Bacteriol. , vol.178 , pp. 1003-1011
    • Sorensen, K.I.1    Hove-Jensen, B.2
  • 2
    • 0014944868 scopus 로고
    • Regulation of ribose metabolism in Escherichia coli. II. Evidence for two ribose-5-phosphate isomerase activities
    • J. David, and H. Wiesmeyer Regulation of ribose metabolism in Escherichia coli. II. Evidence for two ribose-5-phosphate isomerase activities Biochim. Biophys. Acta 208 1970 56 67
    • (1970) Biochim. Biophys. Acta , vol.208 , pp. 56-67
    • David, J.1    Wiesmeyer, H.2
  • 3
    • 0016411449 scopus 로고
    • D-ribose-5-phosphate isomerase from skeletal muscle
    • G.F. Domagk, and W.R. Alexander D-ribose-5-phosphate isomerase from skeletal muscle Methods Enzymol. 41 1975 424 426
    • (1975) Methods Enzymol. , vol.41 , pp. 424-426
    • Domagk, G.F.1    Alexander, W.R.2
  • 4
    • 0016422117 scopus 로고
    • D-ribose-5-phosphate isomerase from Candida utilis
    • G.F. Domagk, and K.M. Doering D-ribose-5-phosphate isomerase from Candida utilis Methods Enzymol. 41 1975 427 429
    • (1975) Methods Enzymol. , vol.41 , pp. 427-429
    • Domagk, G.F.1    Doering, K.M.2
  • 5
    • 0029800865 scopus 로고    scopus 로고
    • Cloning and characterization of the first two genes of the non-oxidative part of the Saccharomyces cerevisiae pentose-phosphate pathway
    • T. Miosga, and F.K. Zimmermann Cloning and characterization of the first two genes of the non-oxidative part of the Saccharomyces cerevisiae pentose-phosphate pathway Curr. Genet. 30 1996 404 409
    • (1996) Curr. Genet. , vol.30 , pp. 404-409
    • Miosga, T.1    Zimmermann, F.K.2
  • 6
    • 0034650538 scopus 로고    scopus 로고
    • D-ribose-5-phosphate isomerase from spinach: Heterologous overexpression, purification, characterization, and site-directed mutagenesis of the recombinant enzyme
    • C.H. Jung, F.C. Hartman, T.Y. Lu, and F.W. Larimer D-ribose-5-phosphate isomerase from spinach: heterologous overexpression, purification, characterization, and site-directed mutagenesis of the recombinant enzyme Arch. Biochem. Biophys. 373 2000 409 417
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 409-417
    • Jung, C.H.1    Hartman, F.C.2    Lu, T.Y.3    Larimer, F.W.4
  • 7
    • 0036278183 scopus 로고    scopus 로고
    • A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure
    • K. Ishikawa, I. Matsui, F. Payan, C. Cambillau, H. Ishida, Y. Kawarabayasi, H. Kikuchi, and A. Roussel A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure Structure (Camb) 10 2002 877 886
    • (2002) Structure (Camb) , vol.10 , pp. 877-886
    • Ishikawa, K.1    Matsui, I.2    Payan, F.3    Cambillau, C.4    Ishida, H.5    Kawarabayasi, Y.6    Kikuchi, H.7    Roussel, A.8
  • 8
    • 0016784251 scopus 로고
    • Two ribose-5-phosphate isomerases from Escherichia coli K12: Partial characterisation of the enzymes and consideration of their possible physiological roles
    • M.K. Essenberg, and R.A. Cooper Two ribose-5-phosphate isomerases from Escherichia coli K12: partial characterisation of the enzymes and consideration of their possible physiological roles Eur. J. Biochem. 55 1975 323 332
    • (1975) Eur. J. Biochem. , vol.55 , pp. 323-332
    • Essenberg, M.K.1    Cooper, R.A.2
  • 9
    • 0036721069 scopus 로고    scopus 로고
    • Crystal structure of D-ribose-5-phosphate isomerase (RpiA) from Escherichia coli
    • E.S. Rangarajan, J. Sivaraman, A. Matte, and M. Cygler Crystal structure of D-ribose-5-phosphate isomerase (RpiA) from Escherichia coli Proteins 48 2002 737 740
    • (2002) Proteins , vol.48 , pp. 737-740
    • Rangarajan, E.S.1    Sivaraman, J.2    Matte, A.3    Cygler, M.4
  • 11
    • 1542782483 scopus 로고    scopus 로고
    • Oxyanion hole-stabilized stereospecific isomerization in ribose-5-phosphate isomerase (Rpi)
    • K. Hamada, H. Ago, M. Sugahara, Y. Nodake, S. Kuramitsu, and M. Miyano Oxyanion hole-stabilized stereospecific isomerization in ribose-5-phosphate isomerase (Rpi) J. Biol. Chem. 278 2003 49183 49190
    • (2003) J. Biol. Chem. , vol.278 , pp. 49183-49190
    • Hamada, K.1    Ago, H.2    Sugahara, M.3    Nodake, Y.4    Kuramitsu, S.5    Miyano, M.6
  • 13
    • 0027424786 scopus 로고
    • Structural and functional properties of a multi-enzyme complex from spinach chloroplasts. 1. Stoichiometry of the polypeptide chains
    • M. Rault, M.T. Giudici-Orticoni, B. Gontero, and J. Ricard Structural and functional properties of a multi-enzyme complex from spinach chloroplasts. 1. Stoichiometry of the polypeptide chains Eur. J. Biochem. 217 1993 1065 1073
    • (1993) Eur. J. Biochem. , vol.217 , pp. 1065-1073
    • Rault, M.1    Giudici-Orticoni, M.T.2    Gontero, B.3    Ricard, J.4
  • 14
    • 1842844302 scopus 로고    scopus 로고
    • Pyridoxine biosynthesis in yeast: Participation of ribose 5-phosphate ketol-isomerase
    • H. Kondo, Y. Nakamura, Y.X. Dong, J. Nikawa, and S. Sueda Pyridoxine biosynthesis in yeast: participation of ribose 5-phosphate ketol-isomerase Biochem. J. 379 2004 65 70
    • (2004) Biochem. J. , vol.379 , pp. 65-70
    • Kondo, H.1    Nakamura, Y.2    Dong, Y.X.3    Nikawa, J.4    Sueda, S.5
  • 15
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • S. Bailey The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
    • Bailey, S.1
  • 16
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelyhood
    • R.J. Read Pushing the boundaries of molecular replacement with maximum likelyhood Acta Crystallogr. D Biol. Crystallogr. 57 2001 1373 1382
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 17
    • 0003973683 scopus 로고
    • Silicon Graphics Mountain View, CA
    • A. Roussel, and C. Cambillau Turbo Frodo 1991 Silicon Graphics Mountain View, CA pp. 77-78
    • (1991) Turbo Frodo
    • Roussel, A.1    Cambillau, C.2
  • 20
    • 0031389475 scopus 로고    scopus 로고
    • Ribose-5-phosphate isomerase from Saccharomyces cerevisiae: Purification and molecular analysis of the enzyme
    • R. Reuter, M. Naumann, J. Bar, T. Miosga, and G. Kopperschlager Ribose-5-phosphate isomerase from Saccharomyces cerevisiae: purification and molecular analysis of the enzyme Bioseparation 7 1998 107 115
    • (1998) Bioseparation , vol.7 , pp. 107-115
    • Reuter, R.1    Naumann, M.2    Bar, J.3    Miosga, T.4    Kopperschlager, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.