메뉴 건너뛰기




Volumn 109, Issue 1-3, 1998, Pages 153-167

Redefining reductive sulfate assimilation in higher plants: A role for APS reductase, a new member of the thioredoxin superfamily?

Author keywords

APS reductase; Higher plants; Reductive sulfate assimilation

Indexed keywords

ADENOSINE 3' PHOSPHATE 5' PHOSPHOSULFATE; ADENOSINE 5' PHOSPHOSULFATE; COMPLEMENTARY DNA; CYSTEINE SYNTHASE; OXIDOREDUCTASE; SULFATE; SULFIDE; SULFITE REDUCTASE; SULFOTRANSFERASE; THIOREDOXIN;

EID: 0032549067     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(97)00130-0     Document Type: Conference Paper
Times cited : (16)

References (63)
  • 2
    • 0001907076 scopus 로고
    • Physiological functions and environmental relevance of sulfur-containing secondary metabolites
    • L.J. de Kok, I. Stulen, H. Rennenberg, C. Brunold, & W.E. Rauser. The Hague, The Netherlands: SPB Publishing
    • Schnug E. Physiological functions and environmental relevance of sulfur-containing secondary metabolites. de Kok L.J., Stulen I., Rennenberg H., Brunold C., Rauser W.E. Sulfur Nutrition and Assimilation in Higher Plants. 1993;179-190 SPB Publishing, The Hague, The Netherlands.
    • (1993) Sulfur Nutrition and Assimilation in Higher Plants , pp. 179-190
    • Schnug, E.1
  • 3
    • 0028564046 scopus 로고
    • Secondary metabolites in plant defense mechanisms
    • Bennet R.N., Wallsgrove R.M. Secondary metabolites in plant defense mechanisms. New Phytol. 127:1994;617-633.
    • (1994) New Phytol. , vol.127 , pp. 617-633
    • Bennet, R.N.1    Wallsgrove, R.M.2
  • 4
    • 0008212751 scopus 로고
    • 2 and the evolution of the biosynthesis of organic sulfur compounds on populations and ecosystems
    • L.J. de Kok, I. Stulen, H. Rennenberg, C. Brunold, & W.E. Rauser. The Hague, The Netherlands: SPB Publishing
    • 2 and the evolution of the biosynthesis of organic sulfur compounds on populations and ecosystems. de Kok L.J., Stulen I., Rennenberg H., Brunold C., Rauser W.E. Sulfur Nutrition and Assimilation in Higher Plants. 1993;295-313 SPB Publishing, The Hague, The Netherlands.
    • (1993) Sulfur Nutrition and Assimilation in Higher Plants , pp. 295-313
    • Ernst, W.H.O.1
  • 5
    • 0028121632 scopus 로고
    • Photosynthetic sulfate reduction
    • Schwenn J.D. Photosynthetic sulfate reduction. Z. Naturforsch. 49C:1994;531-539.
    • (1994) Z. Naturforsch. , vol.49 , pp. 531-539
    • Schwenn, J.D.1
  • 6
    • 0002739255 scopus 로고
    • Reduction of sulfate to sulfide
    • H. Rennenberg, C. Brunold, L.J. De Kok, & I. Stulen. The Hague, The Netherlands: SPB Publishing
    • Brunold C. Reduction of sulfate to sulfide. Rennenberg H., Brunold C., De Kok L.J., Stulen I. Sulfur Nutrition and Sulfur Assimilation in Higher Plants. 1990;14-31 SPB Publishing, The Hague, The Netherlands.
    • (1990) Sulfur Nutrition and Sulfur Assimilation in Higher Plants , pp. 14-31
    • Brunold, C.1
  • 7
    • 0030453191 scopus 로고    scopus 로고
    • Molecular genetics of sulfate assimilation in plants
    • Leustek T. Molecular genetics of sulfate assimilation in plants. Physiol. Plant. 97:1996;411-419.
    • (1996) Physiol. Plant. , vol.97 , pp. 411-419
    • Leustek, T.1
  • 9
    • 0010560421 scopus 로고
    • Studies of sulfate utilization by algae: 9. Fractionation of a cell-free system from Chlorella into two activities necessary for the reduction of adenosine 3′-phosphate to acid-volatile radioactivity
    • Hodson R.C., Schiff J.A. Studies of sulfate utilization by algae: 9. Fractionation of a cell-free system from Chlorella into two activities necessary for the reduction of adenosine 3′-phosphate to acid-volatile radioactivity. Plant Physiol. 47:1971;300-305.
    • (1971) Plant Physiol. , vol.47 , pp. 300-305
    • Hodson, R.C.1    Schiff, J.A.2
  • 10
    • 0003269875 scopus 로고
    • Studies of sulfate utilization by algae: 10. Nutritional and enzymatic characterisation of Chlorella mutants impaired for sulfate utilization
    • Hodson R.C., Schiff J.A. Studies of sulfate utilization by algae: 10. Nutritional and enzymatic characterisation of Chlorella mutants impaired for sulfate utilization. Plant Physiol. 47:1971;306-311.
    • (1971) Plant Physiol. , vol.47 , pp. 306-311
    • Hodson, R.C.1    Schiff, J.A.2
  • 11
    • 0015269556 scopus 로고
    • On the mechanism of photosynthetic sulfate reduction. An APS sulfotransferase from Chlorella
    • Schmidt A. On the mechanism of photosynthetic sulfate reduction. An APS sulfotransferase from Chlorella. Arch. Mikrobiol. 84:1972;77-86.
    • (1972) Arch. Mikrobiol. , vol.84 , pp. 77-86
    • Schmidt, A.1
  • 12
    • 0010562627 scopus 로고
    • Studies of sulfate utilization by algae, 13. Adenosine 5′-phosphosulfate (APS) as an intermediate in the conversion of adenosine 3′5′-phosphosulfate (PAPS) to acid-volatile radioactivity
    • Goldschmidt E.E., Tang M.L., Schiff J.A. Studies of sulfate utilization by algae, 13. Adenosine 5′-phosphosulfate (APS) as an intermediate in the conversion of adenosine 3′5′-phosphosulfate (PAPS) to acid-volatile radioactivity. Plant Sci. Lett. 4:1975;293-299.
    • (1975) Plant Sci. Lett. , vol.4 , pp. 293-299
    • Goldschmidt, E.E.1    Tang, M.L.2    Schiff, J.A.3
  • 13
    • 0001388439 scopus 로고
    • A sulfotransferase from spinach leaves using adenosine-5′-phosphosulfate
    • Schmidt A. A sulfotransferase from spinach leaves using adenosine-5′-phosphosulfate. Planta. 124:1975;267-275.
    • (1975) Planta , vol.124 , pp. 267-275
    • Schmidt, A.1
  • 14
    • 0010556305 scopus 로고
    • Distribution of APS sulfotransferase activity among higher plants
    • Schmidt A. Distribution of APS sulfotransferase activity among higher plants. Plant Sci. Lett. 5:1975;407-415.
    • (1975) Plant Sci. Lett. , vol.5 , pp. 407-415
    • Schmidt, A.1
  • 15
    • 0000925164 scopus 로고
    • The adenosine-5′-phosphosulfate sulfotransferase from spinach (Spinacia oleracea L.). Stabilization, partial purification and properties
    • Schmidt A. The adenosine-5′-phosphosulfate sulfotransferase from spinach (Spinacia oleracea L.). Stabilization, partial purification and properties. Planta. 130:1976;257-263.
    • (1976) Planta , vol.130 , pp. 257-263
    • Schmidt, A.1
  • 17
    • 0030023180 scopus 로고    scopus 로고
    • Adenosine 5′-phosphosulfate sulfotransferase from the marine macroalga Porphyra yezoensis Ueda (Rhodophyta); Stabilization, purification, and properties
    • Kanno N., Nagahisa E., Sato M., Sato Y. Adenosine 5′-phosphosulfate sulfotransferase from the marine macroalga Porphyra yezoensis Ueda (Rhodophyta); stabilization, purification, and properties. Planta. 198:1996;440-446.
    • (1996) Planta , vol.198 , pp. 440-446
    • Kanno, N.1    Nagahisa, E.2    Sato, M.3    Sato, Y.4
  • 18
    • 0026096770 scopus 로고
    • Purification and properties of adenosine 5′-phosphosulphate sulphotransferase from Euglena
    • Li J., Schiff J.A. Purification and properties of adenosine 5′-phosphosulphate sulphotransferase from Euglena. Biochem. J. 274:1991;355-360.
    • (1991) Biochem. J. , vol.274 , pp. 355-360
    • Li, J.1    Schiff, J.A.2
  • 19
    • 4243518356 scopus 로고
    • Adenosine 5′-phosphosulfate sulfotransferase: Enzyme-bound intermediates
    • Li J., Schiff J.A. Adenosine 5′-phosphosulfate sulfotransferase: Enzyme-bound intermediates. Plant Cell Physiol. 33:1992;63-72.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 63-72
    • Li, J.1    Schiff, J.A.2
  • 20
    • 0015866062 scopus 로고
    • Sulfate reduction in a cell-free system of Chlorella. The ferredoxin-dependent reduction of a protein-bound intermediate by thiosulfonate reductase
    • Schmidt A. Sulfate reduction in a cell-free system of Chlorella. The ferredoxin-dependent reduction of a protein-bound intermediate by thiosulfonate reductase. Arch. Mikrobiol. 93:1973;29-52.
    • (1973) Arch. Mikrobiol. , vol.93 , pp. 29-52
    • Schmidt, A.1
  • 21
    • 0000527976 scopus 로고
    • Biosynthesis of cysteine
    • F.C. Neidhardt, J.L. Ingraham, K.B. Low, B. Magasanik, M. Schaechter, & H.E. Umbarger. Washington, DC, USA: American Society for Microbiology
    • Kredich N.M. Biosynthesis of cysteine. Neidhardt F.C., Ingraham J.L., Low K.B., Magasanik B., Schaechter M., Umbarger H.E. Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. 1987;419-428 American Society for Microbiology, Washington, DC, USA.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 419-428
    • Kredich, N.M.1
  • 22
    • 0026640677 scopus 로고
    • Physiological analysis of mutants of Saccharomyces cerevisiae impaired in sulphate assimilation
    • Thomas D., Barbey R., Henry D., Surdin-Kerjan Y. Physiological analysis of mutants of Saccharomyces cerevisiae impaired in sulphate assimilation. J. Gen. Microbiol. 138:1992;2021-2028.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2021-2028
    • Thomas, D.1    Barbey, R.2    Henry, D.3    Surdin-Kerjan, Y.4
  • 23
    • 0000468111 scopus 로고
    • Ferredoxin-sulfite reductase from spinach
    • Aketagawa J., Tamura G. Ferredoxin-sulfite reductase from spinach. Agric. Biol. Chem. 44:1980;2371-2378.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 2371-2378
    • Aketagawa, J.1    Tamura, G.2
  • 24
    • 0030592165 scopus 로고    scopus 로고
    • A cDNA clone from Arabidopsis thaliana encoding plastidic ferredoxin: Sulfite reductase
    • Bruhl A., Haverkamp T., Gisselmann G., Schwenn J.D. A cDNA clone from Arabidopsis thaliana encoding plastidic ferredoxin: sulfite reductase. Biochim. Biophys. Acta. 1295:1996;119-124.
    • (1996) Biochim. Biophys. Acta , vol.1295 , pp. 119-124
    • Bruhl, A.1    Haverkamp, T.2    Gisselmann, G.3    Schwenn, J.D.4
  • 25
    • 84961469286 scopus 로고
    • Sulphate assimilation in higher plants: A thioredoxin-dependent PAPS-reductase from spinach leaves
    • Schwenn J.D. Sulphate assimilation in higher plants: A thioredoxin-dependent PAPS-reductase from spinach leaves. Z. Naturforsch. 44c:1989;504-508.
    • (1989) Z. Naturforsch. , vol.44 , pp. 504-508
    • Schwenn, J.D.1
  • 26
    • 0010595016 scopus 로고
    • Function of thioredoxin in the reduction of adenosine 3′-phosphate 5′-phosphosulfate in Escherichia coli
    • P. Gadal. Paris, France: CNRS
    • Tsang M.L. Function of thioredoxin in the reduction of adenosine 3′-phosphate 5′-phosphosulfate in Escherichia coli. Gadal P. Thioredoxins: Structure and Functions. 1983;21-24 CNRS, Paris, France.
    • (1983) Thioredoxins: Structure and Functions , pp. 21-24
    • Tsang, M.L.1
  • 27
    • 84995069579 scopus 로고
    • Homologies in the structural genes encoding for sulphate reducing enzymes from higher plants and prokaryotes
    • Gisselmann G., Niehaus A., Schwenn J.D. Homologies in the structural genes encoding for sulphate reducing enzymes from higher plants and prokaryotes. Bot. Acta. 105:1992;213-218.
    • (1992) Bot. Acta , vol.105 , pp. 213-218
    • Gisselmann, G.1    Niehaus, A.2    Schwenn, J.D.3
  • 28
    • 0028836545 scopus 로고
    • Heterologous expression of genes in bacterial, fungal, animal, and plant cells
    • Frommer W.B., Ninnemann O. Heterologous expression of genes in bacterial, fungal, animal, and plant cells. Annu. Rev. Plant Physiol. Plant Mol. Biol. 46:1995;419-444.
    • (1995) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.46 , pp. 419-444
    • Frommer, W.B.1    Ninnemann, O.2
  • 29
    • 0025924684 scopus 로고
    • Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli
    • Krone F.A., Westphal G., Schwenn J.D. Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli. Mol. Gen. Genet. 225:1991;314-319.
    • (1991) Mol. Gen. Genet. , vol.225 , pp. 314-319
    • Krone, F.A.1    Westphal, G.2    Schwenn, J.D.3
  • 30
    • 0014365872 scopus 로고
    • Positive control of sulphate reduction in Escherichia coli. Isolation, characterization and mapping of cysteineless mutants of E. coli K12
    • Jones-Mortimer M.C. Positive control of sulphate reduction in Escherichia coli. Isolation, characterization and mapping of cysteineless mutants of E. coli K12. Biochem. J. 110:1968;589-595.
    • (1968) Biochem. J. , vol.110 , pp. 589-595
    • Jones-Mortimer, M.C.1
  • 31
    • 0026022605 scopus 로고
    • λYES - A multifunctional cDNA expression vector for the isolation of genes by complementation of yeast and Escherichia coli mutations
    • Elledge S.J., Mulligan J.T., Ramer S.W., Spottswood M., Davis R.W. λYES - a multifunctional cDNA expression vector for the isolation of genes by complementation of yeast and Escherichia coli mutations. Proc. Natl. Acad. Sci. U.S.A. 88:1991;1731-1735.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 1731-1735
    • Elledge, S.J.1    Mulligan, J.T.2    Ramer, S.W.3    Spottswood, M.4    Davis, R.W.5
  • 32
    • 0029830772 scopus 로고    scopus 로고
    • Three members of a novel small gene family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin domain and 'APS reductase' activity
    • Gutierrez-Marcos J.F., Roberts M.A., Campbell E.I., Wray J.L. Three members of a novel small gene family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin domain and 'APS reductase' activity. Proc. Natl. Acad. Sci. U.S.A. 93:1996;13377-13382.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13377-13382
    • Gutierrez-Marcos, J.F.1    Roberts, M.A.2    Campbell, E.I.3    Wray, J.L.4
  • 33
    • 0023080760 scopus 로고
    • PAPS reductase from Escherichia coli: Characterization of the enzyme as probe for thioredoxins
    • Schwenn J.D., Schriek U. PAPS reductase from Escherichia coli: Characterization of the enzyme as probe for thioredoxins. Z. Naturforsch. 42c:1987;93-102.
    • (1987) Z. Naturforsch. , vol.42 , pp. 93-102
    • Schwenn, J.D.1    Schriek, U.2
  • 34
    • 0029841432 scopus 로고    scopus 로고
    • Sulfate reduction in higher plants - Molecular evidence for a novel 5′-adenylylsulfate reductase
    • Setya A., Murillo M., Leustek T. Sulfate reduction in higher plants - molecular evidence for a novel 5′-adenylylsulfate reductase. Proc. Natl. Acad. Sci. U.S.A. 93:1996;13383-13388.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13383-13388
    • Setya, A.1    Murillo, M.2    Leustek, T.3
  • 35
    • 0025135468 scopus 로고
    • A conserved cleavage-site motif in chloroplast transit peptides
    • Gavel Y., von Heijne G. A conserved cleavage-site motif in chloroplast transit peptides. FEBS Lett. 261:1990;455-458.
    • (1990) FEBS Lett. , vol.261 , pp. 455-458
    • Gavel, Y.1    Von Heijne, G.2
  • 37
    • 0027959156 scopus 로고
    • Protein disulfide isomerase-building bridges in protein-folding
    • Freedman R.B., Hirst T.R., Tuite M.F. Protein disulfide isomerase-building bridges in protein-folding. Trends Biochem. Sci. 19:1994;331-336.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 38
    • 0022495947 scopus 로고
    • Further characterization and amino acid sequence of m-type thioredoxins from spinach chloroplasts
    • Maeda K., Tsugita A., Dalzoppo D., Vilbois F., Schurmann P. Further characterization and amino acid sequence of m-type thioredoxins from spinach chloroplasts. Eur. J. Biochem. 154:1986;197-203.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 197-203
    • Maeda, K.1    Tsugita, A.2    Dalzoppo, D.3    Vilbois, F.4    Schurmann, P.5
  • 41
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264:1989;13963-13966.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 42
    • 0001148764 scopus 로고
    • Sulfur metabolism B. Adenosine 5′-phosphosulfate sulphotransferase
    • Lea P.J. London: Academic Press
    • Brunold C., Suter M. Sulfur metabolism B. Adenosine 5′-phosphosulfate sulphotransferase. Lea P.J. Methods in Plant Biochemistry: Enzymes of Primary Metabolism. 3:1990;339-343 Academic Press, London.
    • (1990) Methods in Plant Biochemistry: Enzymes of Primary Metabolism , vol.3 , pp. 339-343
    • Brunold, C.1    Suter, M.2
  • 43
    • 0010632279 scopus 로고
    • Evidence for the participation of both stromal and membrane enzymes
    • Schwenn J.D., Depka B., Hennies H.H. Evidence for the participation of both stromal and membrane enzymes. Plant Cell Physiol. 17:1976;165-176.
    • (1976) Plant Cell Physiol. , vol.17 , pp. 165-176
    • Schwenn, J.D.1    Depka, B.2    Hennies, H.H.3
  • 44
    • 85003994243 scopus 로고
    • Effect of high and low sulfate concentrations on adenosine 5′-phosphosulfate sulfotransferase activity from Lemna minor
    • Brunold C., Suter M., Lavanchy P. Effect of high and low sulfate concentrations on adenosine 5′-phosphosulfate sulfotransferase activity from Lemna minor. Physiol. Plant. 70:1987;168-174.
    • (1987) Physiol. Plant. , vol.70 , pp. 168-174
    • Brunold, C.1    Suter, M.2    Lavanchy, P.3
  • 45
    • 0027973967 scopus 로고
    • APS-sulfotransferase activity is identical to higher plant APS-kinase (EC 2.7.1.25)
    • Schiffmann S., Schwenn J.D. APS-sulfotransferase activity is identical to higher plant APS-kinase (EC 2.7.1.25). FEBS Lett. 355:1994;229-232.
    • (1994) FEBS Lett. , vol.355 , pp. 229-232
    • Schiffmann, S.1    Schwenn, J.D.2
  • 46
    • 0010596421 scopus 로고
    • A kinetic investigation of the APS kinase from Chlamydomonas reinhardtii CW15
    • Schwenn J.D., Jender H.G. A kinetic investigation of the APS kinase from Chlamydomonas reinhardtii CW15. Phytochemistry. 20:1981;601-604.
    • (1981) Phytochemistry , vol.20 , pp. 601-604
    • Schwenn, J.D.1    Jender, H.G.2
  • 47
    • 0028849610 scopus 로고
    • Reaction mechanism of thioredoxin: 3′-phosphoadenylylsulfate reductase investigated by site-directed mutagenesis
    • Berendt U., Haverkamp T., Prior A., Schwenn J.D. Reaction mechanism of thioredoxin: 3′-phosphoadenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 233:1995;347-356.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 347-356
    • Berendt, U.1    Haverkamp, T.2    Prior, A.3    Schwenn, J.D.4
  • 48
    • 34250131767 scopus 로고
    • Hydrogen peroxide scavenging systems within pea chloroplasts. A quantitative study
    • Gilham D.J., Dodge A.D. Hydrogen peroxide scavenging systems within pea chloroplasts. A quantitative study. Planta. 167:1986;246-251.
    • (1986) Planta , vol.167 , pp. 246-251
    • Gilham, D.J.1    Dodge, A.D.2
  • 49
    • 0010638644 scopus 로고
    • Glutathione-insulin transhydrogenase of human liver
    • Tomizawa H.H., Varandani P.T. Glutathione-insulin transhydrogenase of human liver. J. Biol. Chem. 240:1965;3191-3194.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3191-3194
    • Tomizawa, H.H.1    Varandani, P.T.2
  • 50
    • 0029175508 scopus 로고
    • Ferredoxin: Thioredoxin system
    • Schurmann P. Ferredoxin: thioredoxin system. Methods Enzymol. 252:1995;274-283.
    • (1995) Methods Enzymol. , vol.252 , pp. 274-283
    • Schurmann, P.1
  • 51
    • 0000570970 scopus 로고
    • Carbon dioxide assimilation in oxygenic and anoxygenic photosynthesis
    • Buchanan B.B. Carbon dioxide assimilation in oxygenic and anoxygenic photosynthesis. Photosynth. Res. 33:1992;147-162.
    • (1992) Photosynth. Res. , vol.33 , pp. 147-162
    • Buchanan, B.B.1
  • 52
    • 0039399893 scopus 로고
    • Biochemistry of the sulfur cycle
    • D.M. Greenberg. New York: Academic Press
    • Siegel L.M. Biochemistry of the sulfur cycle. Greenberg D.M. Metabolism of Sulfur Compounds. 1975;217-286 Academic Press, New York.
    • (1975) Metabolism of Sulfur Compounds , pp. 217-286
    • Siegel, L.M.1
  • 53
    • 0000713965 scopus 로고
    • Partial purification and characterization of a 3′-phosphoadenosine 5′-phosphosulfate: Desulfoglucosinolate sulfotransferase from cress (Lepidium sativum)
    • Glendening T.M., Poulson J.E. Partial purification and characterization of a 3′-phosphoadenosine 5′-phosphosulfate: desulfoglucosinolate sulfotransferase from cress (Lepidium sativum). Plant Physiol. 94:1990;811-818.
    • (1990) Plant Physiol. , vol.94 , pp. 811-818
    • Glendening, T.M.1    Poulson, J.E.2
  • 54
    • 0010562631 scopus 로고
    • Partial purification and some properties of flavonol 7-sulfotransferase from Flaveria bidentis
    • Varin L., Ibrahim R.K. Partial purification and some properties of flavonol 7-sulfotransferase from Flaveria bidentis. Plant Physiol. 95:1991;1254-1258.
    • (1991) Plant Physiol. , vol.95 , pp. 1254-1258
    • Varin, L.1    Ibrahim, R.K.2
  • 55
    • 0026569391 scopus 로고
    • Novel flavonol 3-sulfotransferase-purification, kinetic properties and partial amino acid sequence
    • Varin L., Ibrahim R.K. Novel flavonol 3-sulfotransferase-purification, kinetic properties and partial amino acid sequence. J. Biol. Chem. 267:1992;1858-1863.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1858-1863
    • Varin, L.1    Ibrahim, R.K.2
  • 57
    • 0017154294 scopus 로고
    • Properties of enzyme fraction A from Chlorella and copurification of 3′(2′),5′-bisphosphonucleoside 3′(2′)-phosphohydrolase, adenosine 5′-phosphosulfate sulfohydrolase and adenosine-5′-phosphosulfate cyclase activities
    • Tsang M.L., Schiff J.A. Properties of enzyme fraction A from Chlorella and copurification of 3′(2′),5′-bisphosphonucleoside 3′(2′)-phosphohydrolase, adenosine 5′-phosphosulfate sulfohydrolase and adenosine-5′-phosphosulfate cyclase activities. Eur. J. Biochem. 65:1976;113-121.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 113-121
    • Tsang, M.L.1    Schiff, J.A.2
  • 58
    • 0028858093 scopus 로고
    • 2+-sensitive 3′(2′),5′-diphosphonucleoside 3′(2′)-phosphohydrolase and complements yeast met22 and Escherichia coli cysQ mutations
    • 2+-sensitive 3′(2′),5′-diphosphonucleoside 3′(2′)-phosphohydrolase and complements yeast met22 and Escherichia coli cysQ mutations. J. Biol. Chem. 270:1995;29105-29110.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29105-29110
    • Peng, Z.1    Verma, D.P.S.2
  • 59
    • 0030099036 scopus 로고    scopus 로고
    • The SAL1 gene of Arabidopsis, encoding an enzyme with 3′(2′),5′-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities, increases salt tolerance in yeast
    • Quintero F.J., Garciadeblas B., Rodriguez-Navarro A. The SAL1 gene of Arabidopsis, encoding an enzyme with 3′(2′),5′-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities, increases salt tolerance in yeast. Plant Cell. 8:1996;529-537.
    • (1996) Plant Cell , vol.8 , pp. 529-537
    • Quintero, F.J.1    Garciadeblas, B.2    Rodriguez-Navarro, A.3
  • 60
    • 0028912113 scopus 로고
    • A salt-sensitive 3′(2′),5′-bisphosphate nucleotidase involve in sulfate activation
    • Murguia J.R., Belles J.M., Serrano R. A salt-sensitive 3′(2′),5′-bisphosphate nucleotidase involve in sulfate activation. Science. 267:1995;232-234.
    • (1995) Science , vol.267 , pp. 232-234
    • Murguia, J.R.1    Belles, J.M.2    Serrano, R.3
  • 62
    • 0028466132 scopus 로고
    • Cloning of a cDNA encoding ATP sulfurylase from Arabidopsis thaliana by functional expression in Saccharomyces cerevisiae
    • Leustek T., Murillo M., Cervantes M. Cloning of a cDNA encoding ATP sulfurylase from Arabidopsis thaliana by functional expression in Saccharomyces cerevisiae. Plant Physiol. 105:1994;897-902.
    • (1994) Plant Physiol. , vol.105 , pp. 897-902
    • Leustek, T.1    Murillo, M.2    Cervantes, M.3
  • 63
    • 0028885653 scopus 로고
    • ATP sulfurylase from Arabidopsis thaliana and Escherichia coli are functionally equivalent but structurally and kinetically divergent. Nucleotide sequence of two ATP sulfurylase cDNAs from Arabidopsis thaliana and analysis of a recombinant enzyme
    • Murillo M., Leustek T. ATP sulfurylase from Arabidopsis thaliana and Escherichia coli are functionally equivalent but structurally and kinetically divergent. Nucleotide sequence of two ATP sulfurylase cDNAs from Arabidopsis thaliana and analysis of a recombinant enzyme. Arch. Biochem. Biophys. 323:1995;195-204.
    • (1995) Arch. Biochem. Biophys. , vol.323 , pp. 195-204
    • Murillo, M.1    Leustek, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.