메뉴 건너뛰기




Volumn 287, Issue 4, 1999, Pages 761-771

Structure and mechanism of the amphibolic enzyme D-ribulose-5-phosphate 3-epimerase from potato chloroplasts

Author keywords

( )8 barrel; Calvin cycle; Evolutionary conservation; Pentose phosphate epimerase; X ray structure analysis

Indexed keywords

AMPHIBOLE; EPIMERASE; RIBULOSE PHOSPHATE;

EID: 0033537899     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2643     Document Type: Article
Times cited : (42)

References (38)
  • 1
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton G. L. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.L.1
  • 2
    • 0026736606 scopus 로고
    • The molecular structure of UDP-galactose 4-epimerase from Escherichia coli detemined at 2.5 Å resolution
    • Bauer A. J., Rayment I., Frey P. A., Holden H. M. The molecular structure of UDP-galactose 4-epimerase from Escherichia coli detemined at 2.5 Å resolution. Proteins: Struct. Funct. Genet. 12:1992;372-381.
    • (1992) Proteins: Struct. Funct. Genet. , vol.12 , pp. 372-381
    • Bauer, A.J.1    Rayment, I.2    Frey, P.A.3    Holden, H.M.4
  • 4
    • 0031569392 scopus 로고    scopus 로고
    • New applications of simulated annealing in X-ray crystallography and solution NMR
    • Brünger A. T., Adams P. D., Rice L. M. New applications of simulated annealing in X-ray crystallography and solution NMR. Structure. 15:1997;325-335.
    • (1997) Structure , vol.15 , pp. 325-335
    • Brünger, A.T.1    Adams, P.D.2    Rice, L.M.3
  • 5
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4. Programs for protein crystallography
    • Ccp4
    • CCP4. Collaborative Computational Project Number 4. Programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 6
    • 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., Hartmann F. C. Identification of a catalytic aspartyl residue of D -ribulose-5-phosphate 3-epimerase by site-directed mutagenesis. J. Biol. Chem. 274:1999;2132-2136.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2132-2136
    • Chen, Y.-R.1    Larimer, F.W.2    Serpersu, E.H.3    Hartmann, F.C.4
  • 7
    • 0015523705 scopus 로고
    • On the mechanism of the pentose phosphate epimerases
    • Davis L., Lee N., Glaser L. On the mechanism of the pentose phosphate epimerases. J. Biol. Chem. 247:1972;5862-5866.
    • (1972) J. Biol. Chem. , vol.247 , pp. 5862-5866
    • Davis, L.1    Lee, N.2    Glaser, L.3
  • 8
    • 0030513295 scopus 로고    scopus 로고
    • Refined high-resolution structure of the metal-ion dependent L -fuculose-1-phosphate aldolase (class II) from Escherichia coli
    • Dreyer M. K., Schulz G. E. Refined high-resolution structure of the metal-ion dependent L -fuculose-1-phosphate aldolase (class II) from Escherichia coli. Acta Crystallog. sect. D. 52:1996a;1082-1091.
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 1082-1091
    • Dreyer, M.K.1    Schulz, G.E.2
  • 9
    • 0029942857 scopus 로고    scopus 로고
    • Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure
    • Dreyer M. K., Schulz G. E. Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure. J. Mol. Biol. 259:1996b;458-466.
    • (1996) J. Mol. Biol. , vol.259 , pp. 458-466
    • Dreyer, M.K.1    Schulz, G.E.2
  • 10
    • 0025284257 scopus 로고
    • The evolution of α/β barrel enzymes
    • Farber G. K., Petsko G. A. The evolution of α/β barrel enzymes. Trends Biochem. Sci. 15:1990;228-234.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 11
    • 0023057529 scopus 로고
    • Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins
    • Gribskov M., Burgess R. R. Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins. Nucl. Acids Res. 14:1986;6745-6763.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 6745-6763
    • Gribskov, M.1    Burgess, R.R.2
  • 12
    • 0032554660 scopus 로고    scopus 로고
    • Epimerization via carbon-carbon bond cleavage. L -Ribulose-5-phosphate 4-epimerase as a masked class II aldolase
    • Johnson A. E., Tanner M. E. Epimerization via carbon-carbon bond cleavage. L -Ribulose-5-phosphate 4-epimerase as a masked class II aldolase. Biochemistry. 37:1998;5746-5754.
    • (1998) Biochemistry , vol.37 , pp. 5746-5754
    • Johnson, A.E.1    Tanner, M.E.2
  • 13
    • 84889120137 scopus 로고
    • Improved methods of 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 of building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 14
    • 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., Entian K.-D. 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. 252:1996;456-464.
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 456-464
    • Juhnke, H.1    Krems, B.2    Kötter, P.3    Entian, K.-D.4
  • 15
    • 85027632383 scopus 로고
    • Automatic indexing of rotation diffraction patterns
    • Kabsch W. Automatic indexing of rotation diffraction patterns. J. Appl. Crystallog. 21:1988;67-71.
    • (1988) J. Appl. Crystallog. , vol.21 , pp. 67-71
    • Kabsch, W.1
  • 16
    • 0020640999 scopus 로고
    • Purification, properties and assay of D -ribulose-5-phosphate 3-epimerase from human erythrocytes
    • Karmali A., Drake A. F., Spencer N. Purification, properties and assay of D -ribulose-5-phosphate 3-epimerase from human erythrocytes. Biochem. J. 211:1983;617-623.
    • (1983) Biochem. J. , vol.211 , pp. 617-623
    • Karmali, A.1    Drake, A.F.2    Spencer, N.3
  • 17
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 18
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 19
    • 0030850422 scopus 로고    scopus 로고
    • The evolution of the Calvin cycle from prokaryotic to eukaryotic chromosomes: A case study of functional redundancy in ancient pathways through endosymbiosis
    • Martin W., Schnarrenberger C. The evolution of the Calvin cycle from prokaryotic to eukaryotic chromosomes: a case study of functional redundancy in ancient pathways through endosymbiosis. Curr. Genet. 32:1997;1-18.
    • (1997) Curr. Genet. , vol.32 , pp. 1-18
    • Martin, W.1    Schnarrenberger, C.2
  • 21
    • 0028057108 scopus 로고
    • Raster3D version 2.0 - A program for photorealistic molecular graphics
    • Meritt E. A., Murphy M. E. P. Raster3D version 2.0 - a program for photorealistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Meritt, E.A.1    Murphy, M.E.P.2
  • 22
    • 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., Martin W. 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. 29:1995;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
  • 23
    • 0000771669 scopus 로고
    • Structure factor probabilities for related structures
    • Read R. J. Structure factor probabilities for related structures. Acta Crystallog. sect. A. 46:1990;900-912.
    • (1990) Acta Crystallog. Sect. a , vol.46 , pp. 900-912
    • Read, R.J.1
  • 25
    • 0031576360 scopus 로고    scopus 로고
    • Structure and mechanism of L -fuculose isomerase from Escherichia coli
    • Seemann J. E., Schulz G. E. Structure and mechanism of L -fuculose isomerase from Escherichia coli. J. Mol. Biol. 273:1997;256-268.
    • (1997) J. Mol. Biol. , vol.273 , pp. 256-268
    • Seemann, J.E.1    Schulz, G.E.2
  • 26
    • 0029828902 scopus 로고    scopus 로고
    • The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection
    • Slekar K. H., Kosman D. J., Culotta V. C. The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection. J. Biol. Chem. 271:1996;28831-28836.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28831-28836
    • Slekar, K.H.1    Kosman, D.J.2    Culotta, V.C.3
  • 27
    • 0028884775 scopus 로고
    • Genetics of the pentose-phosphate pathway enzymes of Escherichia coli K-12
    • Sprenger G. A. Genetics of the pentose-phosphate pathway enzymes of Escherichia coli K-12. Arch. Microbiol. 164:1995;324-330.
    • (1995) Arch. Microbiol. , vol.164 , pp. 324-330
    • Sprenger, G.A.1
  • 28
    • 0027173978 scopus 로고
    • Calvin cycle multienzyme complexes are bound to the chloroplast thylakoid membrane of higher plants in situ
    • Süss K.-H., Arkona C., Manteuffel R., Adler K. Calvin cycle multienzyme complexes are bound to the chloroplast thylakoid membrane of higher plants in situ. Proc. Natl Acad. Sci. USA. 90:1993;5514-5518.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5514-5518
    • Süss, K.-H.1    Arkona, C.2    Manteuffel, R.3    Adler, K.4
  • 29
    • 0029110706 scopus 로고
    • +reductase, and nitrite reductase with thylakoid and pyrenoid membranes of Chlamydomonas reinhardtii chloroplasts as revealed by immunoelectron microscopy
    • +reductase, and nitrite reductase with thylakoid and pyrenoid membranes of Chlamydomonas reinhardtii chloroplasts as revealed by immunoelectron microscopy. Plant Physiol. 107:1995;1387-1397.
    • (1995) Plant Physiol. , vol.107 , pp. 1387-1397
    • Süss, K.-H.1    Prokhorenko, I.2    Adler, K.3
  • 30
    • 0029565173 scopus 로고
    • Chloroplast pentose-5-phosphate 3-epimerase from potato: Cloning, cDNA sequence, and tissue-specific enzyme accumulation
    • Teige M., Kopriva S., Bauwe H., Süss K.-H. Chloroplast pentose-5-phosphate 3-epimerase from potato: cloning, cDNA sequence, and tissue-specific enzyme accumulation. FEBS Letters. 377:1995;349-352.
    • (1995) FEBS Letters , vol.377 , pp. 349-352
    • Teige, M.1    Kopriva, S.2    Bauwe, H.3    Süss, K.-H.4
  • 31
    • 0032030782 scopus 로고    scopus 로고
    • Purification, properties and in situ localization of the amphibolic chloroplast enzymes pentose-5-phosphate 3-epimerase and transketolase from spinach
    • Teige M., Melzer M., Süss K.-H. Purification, properties and in situ localization of the amphibolic chloroplast enzymes pentose-5-phosphate 3-epimerase and transketolase from spinach. Eur. J. Biochem. 252:1998;237-244.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 237-244
    • Teige, M.1    Melzer, M.2    Süss, K.-H.3
  • 32
    • 0030969906 scopus 로고    scopus 로고
    • Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli
    • Thoden J. B., Hegeman A. D., Wesenberg G., Chapeau M. C., Frey P. A., Holden H. M. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Biochemistry. 36:1997;6294-6304.
    • (1997) Biochemistry , vol.36 , pp. 6294-6304
    • Thoden, J.B.1    Hegeman, A.D.2    Wesenberg, G.3    Chapeau, M.C.4    Frey, P.A.5    Holden, H.M.6
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J. D., Higgins D. G., Gibson T. J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22:1994;4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 0032924978 scopus 로고    scopus 로고
    • Locating proper non-crystallographic symmetry in low-resolution electron-density maps with the program GETAX
    • Vonrhein C., Schulz G. E. Locating proper non-crystallographic symmetry in low-resolution electron-density maps with the program GETAX. Acta Crystallog. sect. D. 55:1999;225-229.
    • (1999) Acta Crystallog. Sect. D , vol.55 , pp. 225-229
    • Vonrhein, C.1    Schulz, G.E.2
  • 35
    • 0013500827 scopus 로고
    • D-ribulose-5-phosphate 3-epimerase
    • Williamson W. T., Wood W. A. D-ribulose-5-phosphate 3-epimerase. Methods Enzymol. 9:1966;605-608.
    • (1966) Methods Enzymol. , vol.9 , pp. 605-608
    • Williamson, W.T.1    Wood, W.A.2
  • 36
    • 0026014458 scopus 로고
    • Structural conservation in parallel β/α-barrel enzymes that catalyze three sequential reactions in the pathway of tryptophan biosynthesis
    • Wilmanns M., Hyde C. C., Davies D. R., Kirschner K., Jansonius J. N. Structural conservation in parallel β/α-barrel enzymes that catalyze three sequential reactions in the pathway of tryptophan biosynthesis. Biochemistry. 30:1991;9161-9169.
    • (1991) Biochemistry , vol.30 , pp. 9161-9169
    • Wilmanns, M.1    Hyde, C.C.2    Davies, D.R.3    Kirschner, K.4    Jansonius, J.N.5
  • 37
    • 0018680647 scopus 로고
    • Purification and properties of D-ribulose-5-phosphate 3-epimerase from calf liver
    • Wood T. Purification and properties of D-ribulose-5-phosphate 3-epimerase from calf liver. Biochim. Biophys. Acta. 570:1979;352-362.
    • (1979) Biochim. Biophys. Acta , vol.570 , pp. 352-362
    • Wood, T.1
  • 38
    • 0028209049 scopus 로고
    • Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8 Å resolution
    • Zhang Z., Sugio S., Komives E. A., Liu K. D., Knowles J. R., Petsko G. A., Ringe D. Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8 Å resolution. Biochemistry. 33:1994;2830-2837.
    • (1994) Biochemistry , vol.33 , pp. 2830-2837
    • Zhang, Z.1    Sugio, S.2    Komives, E.A.3    Liu, K.D.4    Knowles, J.R.5    Petsko, G.A.6    Ringe, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.