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Volumn 83, Issue , 2012, Pages 15-24

Assessing functional diversity in the soybean β-substituted alanine synthase enzyme family

Author keywords

Substituted alanine synthase (BSAS); Cysteine degradation; Cysteine synthesis; Enzyme family; Glycine max; Leguminosae; Metabolism; Soybean

Indexed keywords

AMIDASE; BETA UREIDOPROPIONASE; BETA-UREIDOPROPIONASE; CYSTEINE; DRUG DERIVATIVE; ISOENZYME;

EID: 84867065288     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2012.08.003     Document Type: Article
Times cited : (17)

References (61)
  • 2
    • 75949120234 scopus 로고    scopus 로고
    • An O-acetylserine(thiol)lyase homolog with l-cysteine desulfhydrase activity regulates cysteine homeostasis in Arabidopsis
    • C. Álvarez, L. Calo, L.C. Romero, I. García, and C. Gotor An O-acetylserine(thiol)lyase homolog with l-cysteine desulfhydrase activity regulates cysteine homeostasis in Arabidopsis Plant Physiol. 152 2010 656 669
    • (2010) Plant Physiol. , vol.152 , pp. 656-669
    • Álvarez, C.1    Calo, L.2    Romero, L.C.3    García, I.4    Gotor, C.5
  • 3
    • 66149160358 scopus 로고    scopus 로고
    • Comprehensive analysis of the Brassica juncea root proteome in response to cadmium exposure by complementary proteomic approaches
    • S. Alvarez, B.M. Berla, J. Sheffield, R.E. Cahoon, J.M. Jez, and L.M. Hicks Comprehensive analysis of the Brassica juncea root proteome in response to cadmium exposure by complementary proteomic approaches Proteomics 9 2009 2419 2431
    • (2009) Proteomics , vol.9 , pp. 2419-2431
    • Alvarez, S.1    Berla, B.M.2    Sheffield, J.3    Cahoon, R.E.4    Jez, J.M.5    Hicks, L.M.6
  • 4
    • 84867048709 scopus 로고    scopus 로고
    • Methionine metabolism in plants
    • J.M. Jez, American Society of Agronomy Inc.; Crop Science Society of America Inc.; Soil Science Society of America Inc. Madison
    • R. Amir, and Y. Hacham Methionine metabolism in plants J.M. Jez, Sulfur: A Missing Link between Soils, Crops, and Nutrition 2008 American Society of Agronomy Inc.; Crop Science Society of America Inc.; Soil Science Society of America Inc. Madison 251 279
    • (2008) Sulfur: A Missing Link between Soils, Crops, and Nutrition , pp. 251-279
    • Amir, R.1    Hacham, Y.2
  • 5
    • 77950350310 scopus 로고    scopus 로고
    • Arabidopsis S-sulfocysteine synthase activity is essential for chloroplast function and long-day light-dependent redox control
    • M.A. Bermúdez, M.A. Páez-Ochoa, C. Gotor, and L.C. Romero Arabidopsis S-sulfocysteine synthase activity is essential for chloroplast function and long-day light-dependent redox control Plant Cell 22 2010 403 416
    • (2010) Plant Cell , vol.22 , pp. 403-416
    • Bermúdez, M.A.1    Páez-Ochoa, M.A.2    Gotor, C.3    Romero, L.C.4
  • 6
    • 33644685874 scopus 로고    scopus 로고
    • Molecular basis of cysteine biosynthesis in plants: Structural and functional analysis of O-acetylserine sulfhydrylase from Arabdiopsis thaliana
    • E.R. Bonner, R.E. Cahoon, S.M. Knapke, and J.M. Jez Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of O-acetylserine sulfhydrylase from Arabdiopsis thaliana J. Biol. Chem. 280 2005 38803 38813
    • (2005) J. Biol. Chem. , vol.280 , pp. 38803-38813
    • Bonner, E.R.1    Cahoon, R.E.2    Knapke, S.M.3    Jez, J.M.4
  • 7
    • 0141682285 scopus 로고    scopus 로고
    • Sulfur assimilation in soybean: Molecular cloning and characterization of O-acetylserine(thiol)lyase (cysteine synthase)
    • D. Chronis, and H.B. Krishnan Sulfur assimilation in soybean: molecular cloning and characterization of O-acetylserine(thiol)lyase (cysteine synthase) Crop Sci. 43 2003 1819 1827
    • (2003) Crop Sci. , vol.43 , pp. 1819-1827
    • Chronis, D.1    Krishnan, H.B.2
  • 8
    • 0742267793 scopus 로고    scopus 로고
    • Sulfur assimilartion in soybean (Glycine max [L.] Merr.): Molecular cloning and characterization of a cytosolic isoform of serine acetyltransferase
    • D. Chronis, and H.B. Krishnan Sulfur assimilartion in soybean (Glycine max [L.] Merr.): molecular cloning and characterization of a cytosolic isoform of serine acetyltransferase Planta 218 2004 417 426
    • (2004) Planta , vol.218 , pp. 417-426
    • Chronis, D.1    Krishnan, H.B.2
  • 9
    • 0026637901 scopus 로고
    • Purification and characterization of O-acetylserine(thiol) lyase from spinach chloroplasts
    • M. Droux, J. Martins, P. Sajus, and R. Douce Purification and characterization of O-acetylserine(thiol) lyase from spinach chloroplasts Arch. Biochem. Biophys. 295 1992 379 390
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 379-390
    • Droux, M.1    Martins, J.2    Sajus, P.3    Douce, R.4
  • 10
    • 0032125745 scopus 로고    scopus 로고
    • Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants - Structural and kinetic properties of the free and bound enzymes
    • M. Droux, M.L. Ruffet, R. Douce, and D. Job Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants - structural and kinetic properties of the free and bound enzymes Eur. J. Biochem. 255 1998 235 245
    • (1998) Eur. J. Biochem. , vol.255 , pp. 235-245
    • Droux, M.1    Ruffet, M.L.2    Douce, R.3    Job, D.4
  • 11
    • 0001738523 scopus 로고
    • Stage of development descriptions for soybeans, Glycine max (L.) Merrill
    • W.R. Fehr, C.E. Caviness, D.T. Burmood, and J.S. Pennington Stage of development descriptions for soybeans, Glycine max (L.) Merrill Crop Sci. 11 1971 929 930
    • (1971) Crop Sci. , vol.11 , pp. 929-930
    • Fehr, W.R.1    Caviness, C.E.2    Burmood, D.T.3    Pennington, J.S.4
  • 12
    • 33947545688 scopus 로고    scopus 로고
    • Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex
    • J.A. Francois, S. Kumaran, and J.M. Jez Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex Plant Cell 18 2006 3647 3655
    • (2006) Plant Cell , vol.18 , pp. 3647-3655
    • Francois, J.A.1    Kumaran, S.2    Jez, J.M.3
  • 13
    • 78649526445 scopus 로고    scopus 로고
    • Mitochondrial beta-cyanoalanine synthase is essential for root hair formation in Arabidopsis thaliana
    • I. García, J.M. Castellano, B. Vioque, R. Solano, C. Gotor, and L.C. Romero Mitochondrial beta-cyanoalanine synthase is essential for root hair formation in Arabidopsis thaliana Plant Cell 22 2010 3268 3279
    • (2010) Plant Cell , vol.22 , pp. 3268-3279
    • García, I.1    Castellano, J.M.2    Vioque, B.3    Solano, R.4    Gotor, C.5    Romero, L.C.6
  • 14
    • 0010237258 scopus 로고
    • A role for ethylene in the metabolism of cyanide by higher plants
    • J.S. Goudey, L.T. Forrest, and M.S. Spencer A role for ethylene in the metabolism of cyanide by higher plants Plant Physiol. 89 1989 1306 1310
    • (1989) Plant Physiol. , vol.89 , pp. 1306-1310
    • Goudey, J.S.1    Forrest, L.T.2    Spencer, M.S.3
  • 15
    • 46649097789 scopus 로고    scopus 로고
    • Structure and expression of MdFBCP1, encoding an F-box-containing protein 1, during Fuji apple (Malus domestica Borkh.) fruit ripening
    • S.E. Han, Y.S. Seo, S. Heo, D. Kim, S.K. Sung, and W.T. Kim Structure and expression of MdFBCP1, encoding an F-box-containing protein 1, during Fuji apple (Malus domestica Borkh.) fruit ripening Plant Cell Rep. 27 2008 1291 1301
    • (2008) Plant Cell Rep. , vol.27 , pp. 1291-1301
    • Han, S.E.1    Seo, Y.S.2    Heo, S.3    Kim, D.4    Sung, S.K.5    Kim, W.T.6
  • 16
    • 0033927405 scopus 로고    scopus 로고
    • Beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis
    • Y. Hatzfeld, A. Maruyama, A. Schmidt, M. Noji, K. Ishizawa, and K. Saito Beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis Plant Physiol. 123 2000 1163 1171
    • (2000) Plant Physiol. , vol.123 , pp. 1163-1171
    • Hatzfeld, Y.1    Maruyama, A.2    Schmidt, A.3    Noji, M.4    Ishizawa, K.5    Saito, K.6
  • 17
    • 43549120312 scopus 로고    scopus 로고
    • Analysis of the arabidopsis O-acetylserine(thiol)lyase gene family demonstrates compartment-specific differences in the regulation of cysteine synthesis
    • C. Heeg, C. Kruse, R. Jost, M. Gutensohn, T. Ruppert, M. Wirtz, and R. Hell Analysis of the arabidopsis O-acetylserine(thiol)lyase gene family demonstrates compartment-specific differences in the regulation of cysteine synthesis Plant Cell 20 2008 168 185
    • (2008) Plant Cell , vol.20 , pp. 168-185
    • Heeg, C.1    Kruse, C.2    Jost, R.3    Gutensohn, M.4    Ruppert, T.5    Wirtz, M.6    Hell, R.7
  • 18
    • 0032915394 scopus 로고    scopus 로고
    • Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine(thiol)lyase) from Arabidopsis thaliana
    • H. Heese, J. Lipke, T. Altmann, and R. Höfgen Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine(thiol)lyase) from Arabidopsis thaliana Amino Acids 16 1999 113 131
    • (1999) Amino Acids , vol.16 , pp. 113-131
    • Heese, H.1    Lipke, J.2    Altmann, T.3    Höfgen, R.4
  • 19
    • 0035313606 scopus 로고    scopus 로고
    • Plant concepts for mineral acquisition and allocation
    • R. Hell, and H. Hillebrand Plant concepts for mineral acquisition and allocation Curr. Opin. Biotechnol. 12 2001 161 168
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 161-168
    • Hell, R.1    Hillebrand, H.2
  • 20
    • 38249032944 scopus 로고
    • Purification and properties of β-cyano-l-alanine synthase from Spinacia oleracea
    • F. Ikegami, K. Takayama, C. Tajima, and I. Murakoshi Purification and properties of β-cyano-l-alanine synthase from Spinacia oleracea Phytochemistry 27 1988 2011 2016
    • (1988) Phytochemistry , vol.27 , pp. 2011-2016
    • Ikegami, F.1    Takayama, K.2    Tajima, C.3    Murakoshi, I.4
  • 21
    • 38249031429 scopus 로고
    • Purification and properties of β-cyano-l-alanine synthase from Lathyrus latifolius
    • F. Ikegami, K. Takayama, and I. Murakoshi Purification and properties of β-cyano-l-alanine synthase from Lathyrus latifolius Phytochemistry 27 1988 3385 3389
    • (1988) Phytochemistry , vol.27 , pp. 3385-3389
    • Ikegami, F.1    Takayama, K.2    Murakoshi, I.3
  • 22
    • 0029804132 scopus 로고    scopus 로고
    • Enzymatic synthesis of two isoxazolylalanine isomers by cysteine synthases in Lathyrus species
    • F. Ikegami, M. Kamiya, Y.H. Kuo, F. Lambein, and I. Murakoshi Enzymatic synthesis of two isoxazolylalanine isomers by cysteine synthases in Lathyrus species Biol. Pharm. Bull. 19 1996 1214 1215
    • (1996) Biol. Pharm. Bull. , vol.19 , pp. 1214-1215
    • Ikegami, F.1    Kamiya, M.2    Kuo, Y.H.3    Lambein, F.4    Murakoshi, I.5
  • 23
    • 0034622527 scopus 로고    scopus 로고
    • Genomic and functional characterization of the oas gene family encoding O-acetylserine (thiol) lyases, enzymes catalyzing the final step in cysteine biosynthesis in Arabidopsis thaliana
    • R. Jost, O. Berkowitz, M. Wirtz, L. Hopkins, M.J. Hawkesford, and R. Hell Genomic and functional characterization of the oas gene family encoding O-acetylserine (thiol) lyases, enzymes catalyzing the final step in cysteine biosynthesis in Arabidopsis thaliana Gene 253 2000 237 247
    • (2000) Gene , vol.253 , pp. 237-247
    • Jost, R.1    Berkowitz, O.2    Wirtz, M.3    Hopkins, L.4    Hawkesford, M.J.5    Hell, R.6
  • 24
    • 0036405469 scopus 로고    scopus 로고
    • Detection of intermediates in reactions catalyzed by PLP-dependent enzymes: O-acetylserine sulfhydrylase and serine-glyoxalate aminotransferase
    • W.E. Karsten, and P.F. Cook Detection of intermediates in reactions catalyzed by PLP-dependent enzymes: O-acetylserine sulfhydrylase and serine-glyoxalate aminotransferase Methods Enzymol. 354 2002 223 237
    • (2002) Methods Enzymol. , vol.354 , pp. 223-237
    • Karsten, W.E.1    Cook, P.F.2
  • 25
    • 84855217567 scopus 로고    scopus 로고
    • Transgenic soybean plants overexpressing O-acetylserine sulfhydrylase accumulate enhanced levels of cysteine and Bowman-Birk protease inhibitor in seeds
    • W.S. Kim, D. Chronis, M. Jurgens, A.C. Schroeder, S.W. Hyun, J.M. Jez, and H.B. Krishnan Transgenic soybean plants overexpressing O-acetylserine sulfhydrylase accumulate enhanced levels of cysteine and Bowman-Birk protease inhibitor in seeds Planta 235 2012 13 23
    • (2012) Planta , vol.235 , pp. 13-23
    • Kim, W.S.1    Chronis, D.2    Jurgens, M.3    Schroeder, A.C.4    Hyun, S.W.5    Jez, J.M.6    Krishnan, H.B.7
  • 26
    • 33745615124 scopus 로고    scopus 로고
    • Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity
    • N.M. Koropatkin, H.B. Pakrasi, and T.J. Smith Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity Proc. Natl. Acad. Sci. USA 103 2006 9820 9825
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9820-9825
    • Koropatkin, N.M.1    Pakrasi, H.B.2    Smith, T.J.3
  • 27
    • 0014670046 scopus 로고
    • Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium
    • N.M. Kredich, M.A. Becker, and G.M. Tomkins Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium J. Biol. Chem. 244 1969 2428 2439
    • (1969) J. Biol. Chem. , vol.244 , pp. 2428-2439
    • Kredich, N.M.1    Becker, M.A.2    Tomkins, G.M.3
  • 28
    • 14844342726 scopus 로고    scopus 로고
    • Engineering soybean for enhanced sulfur amino acid content
    • H.B. Krishnan Engineering soybean for enhanced sulfur amino acid content Crop Sci. 45 2005 454 461
    • (2005) Crop Sci. , vol.45 , pp. 454-461
    • Krishnan, H.B.1
  • 29
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • V. Kruft, H. Eubel, L. Jänsch, W. Werhahn, and H. Braun Proteomic approach to identify novel mitochondrial proteins in Arabidopsis Plant Physiol. 127 2001 1694 1710
    • (2001) Plant Physiol. , vol.127 , pp. 1694-1710
    • Kruft, V.1    Eubel, H.2    Jänsch, L.3    Werhahn, W.4    Braun, H.5
  • 30
    • 34248217612 scopus 로고    scopus 로고
    • Thermodynamics of the interaction between O-acetylserine sulfhydrylase and the C-terminus of serine acetyltransferase
    • S. Kumaran, and J.M. Jez Thermodynamics of the interaction between O-acetylserine sulfhydrylase and the C-terminus of serine acetyltransferase Biochemistry 46 2007 5586 5594
    • (2007) Biochemistry , vol.46 , pp. 5586-5594
    • Kumaran, S.1    Jez, J.M.2
  • 31
    • 65649133057 scopus 로고    scopus 로고
    • Assembly of the cysteine synthase complex and the regulatory role of protein-protein interactions
    • S. Kumaran, H. Yi, H.B. Krishnan, and J.M. Jez Assembly of the cysteine synthase complex and the regulatory role of protein-protein interactions J. Biol. Chem. 284 2009 10268 10275
    • (2009) J. Biol. Chem. , vol.284 , pp. 10268-10275
    • Kumaran, S.1    Yi, H.2    Krishnan, H.B.3    Jez, J.M.4
  • 32
    • 62349118389 scopus 로고    scopus 로고
    • Heterologous expression analyses of rice OsCAS in Arabidopsis and in yeast provide evidence for its roles in cyanide detoxification rather than in cysteine synthesis in vivo
    • K.W. Lai, C.P. Yau, Y.C. Tse, L. Jian, and W.K. Yip Heterologous expression analyses of rice OsCAS in Arabidopsis and in yeast provide evidence for its roles in cyanide detoxification rather than in cysteine synthesis in vivo J. Exp. Bot. 60 2009 993 1008
    • (2009) J. Exp. Bot. , vol.60 , pp. 993-1008
    • Lai, K.W.1    Yau, C.P.2    Tse, Y.C.3    Jian, L.4    Yip, W.K.5
  • 34
    • 56049121498 scopus 로고    scopus 로고
    • Recent advances in understanding plant response to sulfur-deficiency
    • M. Lewandowska, and A. Sirko Recent advances in understanding plant response to sulfur-deficiency Acta Biochim. Pol. 55 2008 457 471
    • (2008) Acta Biochim. Pol. , vol.55 , pp. 457-471
    • Lewandowska, M.1    Sirko, A.2
  • 35
    • 50649089207 scopus 로고    scopus 로고
    • RNA-seq: An assessment of technical reproducibility and comparison with gene expression arrays
    • J.C. Maroni, C.E. Mason, S.M. Mane, M. Stephens, and Y. Gilad RNA-seq: an assessment of technical reproducibility and comparison with gene expression arrays Genome Res. 18 2008 1509 1517
    • (2008) Genome Res. , vol.18 , pp. 1509-1517
    • Maroni, J.C.1    Mason, C.E.2    Mane, S.M.3    Stephens, M.4    Gilad, Y.5
  • 36
    • 0034807334 scopus 로고    scopus 로고
    • Beta-cyanoalanine synthase and cysteine synthase from potato: Molecular cloning, biochemical characterization, and spatial and hormonal regulation
    • A. Maruyama, K. Saito, and K. Ishizawa Beta-cyanoalanine synthase and cysteine synthase from potato: molecular cloning, biochemical characterization, and spatial and hormonal regulation Plant Mol. Biol. 46 2001 749 760
    • (2001) Plant Mol. Biol. , vol.46 , pp. 749-760
    • Maruyama, A.1    Saito, K.2    Ishizawa, K.3
  • 37
    • 0027787895 scopus 로고
    • Evidence for identity of beta-pyrazolealanine synthase with cysteine synthase in watermelon: Formation of beta-pyrazole-alanine by cloned cysteine synthase in vitro and in vivo
    • M. Noji, I. Murakosh, and K. Saito Evidence for identity of beta-pyrazolealanine synthase with cysteine synthase in watermelon: formation of beta-pyrazole-alanine by cloned cysteine synthase in vitro and in vivo Biochem. Biophys. Res. Commun. 197 1993 1111 1117
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 1111-1117
    • Noji, M.1    Murakosh, I.2    Saito, K.3
  • 38
    • 33646867610 scopus 로고    scopus 로고
    • Soybean ATP sulfurylase, a homodimeric enzyme involved in sulfur assimilation, is abundantly expressed in roots and induced by cold treatment
    • P. Phartiyal, W.S. Kim, R.E. Cahoon, J.M. Jez, and H.B. Krishnan Soybean ATP sulfurylase, a homodimeric enzyme involved in sulfur assimilation, is abundantly expressed in roots and induced by cold treatment Arch. Biochem. Biophys. 450 2006 20 29
    • (2006) Arch. Biochem. Biophys. , vol.450 , pp. 20-29
    • Phartiyal, P.1    Kim, W.S.2    Cahoon, R.E.3    Jez, J.M.4    Krishnan, H.B.5
  • 39
    • 37549006750 scopus 로고    scopus 로고
    • The role of 5′-adenylylsulfate reductase in the sulfur assimilation pathway of soybean: Molecular cloning, kinetic characterization, and gene expression
    • P. Phartiyal, W.S. Kim, R.E. Cahoon, J.M. Jez, and H.N. Krishnan The role of 5′-adenylylsulfate reductase in the sulfur assimilation pathway of soybean: molecular cloning, kinetic characterization, and gene expression Phytochemistry 69 2008 356 364
    • (2008) Phytochemistry , vol.69 , pp. 356-364
    • Phartiyal, P.1    Kim, W.S.2    Cahoon, R.E.3    Jez, J.M.4    Krishnan, H.N.5
  • 40
    • 20444414185 scopus 로고    scopus 로고
    • Impact of elevated H(2)S on metabolite levels, activity of enzymes and expression of genes involved in cysteine metabolism
    • A. Riemenschneider, V. Nikiforova, R. Hoefgen, L.J. De Kok, and J. Papenbrock Impact of elevated H(2)S on metabolite levels, activity of enzymes and expression of genes involved in cysteine metabolism Plant Physiol. Biochem. 43 2005 473 483
    • (2005) Plant Physiol. Biochem. , vol.43 , pp. 473-483
    • Riemenschneider, A.1    Nikiforova, V.2    Hoefgen, R.3    De Kok, L.J.4    Papenbrock, J.5
  • 43
    • 79955571171 scopus 로고    scopus 로고
    • Sulfur assimilation in photosynthetic organisms: Molecular functions and regulations of transporters and assimilatory enzymes
    • H. Takahashi, S. Kopriva, M. Giordano, K. Saito, and R. Hell Sulfur assimilation in photosynthetic organisms: molecular functions and regulations of transporters and assimilatory enzymes Annu. Rev. Plant Biol. 62 2011 157 184
    • (2011) Annu. Rev. Plant Biol. , vol.62 , pp. 157-184
    • Takahashi, H.1    Kopriva, S.2    Giordano, M.3    Saito, K.4    Hell, R.5
  • 44
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • K. Tamura, D. Peterson, N. Peterson, G. Stecher, M. Nei, and S. Kumar MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods Mol. Biol. Evol. 28 2011 2731 2739
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 45
    • 0000672312 scopus 로고
    • Effect of 2,4-dichlorophenoxyacetic acid on endogenous cyanide, beta-cyanoalanine synthase activity, and ethylene evolution in seedlings of soybean and barley
    • F.L. Tittle, J.S. Goudey, and M.S. Spencer Effect of 2,4- dichlorophenoxyacetic acid on endogenous cyanide, beta-cyanoalanine synthase activity, and ethylene evolution in seedlings of soybean and barley Plant Physiol. 94 1990 1143 1148
    • (1990) Plant Physiol. , vol.94 , pp. 1143-1148
    • Tittle, F.L.1    Goudey, J.S.2    Spencer, M.S.3
  • 46
    • 0031669094 scopus 로고    scopus 로고
    • Separation, subcellular location and influence of sulphur nutrition on isoforms of cysteine synthase in spinach
    • A.G.S. Warrilow, and M.J. Hawkesford Separation, subcellular location and influence of sulphur nutrition on isoforms of cysteine synthase in spinach J. Exp. Bot. 49 1998 1625 1636
    • (1998) J. Exp. Bot. , vol.49 , pp. 1625-1636
    • Warrilow, A.G.S.1    Hawkesford, M.J.2
  • 47
    • 0034121969 scopus 로고    scopus 로고
    • Cysteine synthase (O-acetylserine (thiol) lyase) substrate specificities classify the mitochondrial isoform as a cyanoalanine synthase
    • A.G.S. Warrilow, and M.J. Hawkesford Cysteine synthase (O-acetylserine (thiol) lyase) substrate specificities classify the mitochondrial isoform as a cyanoalanine synthase J. Exp. Bot. 51 2000 985 993
    • (2000) J. Exp. Bot. , vol.51 , pp. 985-993
    • Warrilow, A.G.S.1    Hawkesford, M.J.2
  • 48
    • 40749148526 scopus 로고    scopus 로고
    • Physiological roles of the β-substituted alanine synthase gene family in Arabidopsis
    • M. Watanabe, M. Kusano, A. Oikawa, A. Fukushima, M. Noji, and K. Saito Physiological roles of the β-substituted alanine synthase gene family in Arabidopsis Plant Physiol. 146 2008 310 320
    • (2008) Plant Physiol. , vol.146 , pp. 310-320
    • Watanabe, M.1    Kusano, M.2    Oikawa, A.3    Fukushima, A.4    Noji, M.5    Saito, K.6
  • 49
    • 57749102702 scopus 로고    scopus 로고
    • Comparative genomics and reverse genetics analysis reveal indispensable functions of the serine acetyltransferase gene family in Arabidopsis
    • M. Watanabe, K. Mochida, T. Kato, S. Tabata, N. Yoshimoto, M. Noji, and K. Saito Comparative genomics and reverse genetics analysis reveal indispensable functions of the serine acetyltransferase gene family in Arabidopsis Plant Cell 20 2008 2484 2496
    • (2008) Plant Cell , vol.20 , pp. 2484-2496
    • Watanabe, M.1    Mochida, K.2    Kato, T.3    Tabata, S.4    Yoshimoto, N.5    Noji, M.6    Saito, K.7
  • 50
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2 - A multiple sequence alignment editor and analysis workbench
    • A.M. Waterhouse, J.B. Procter, D.M.A. Martin, M. Clamp, and G.J. Barton Jalview Version 2 - a multiple sequence alignment editor and analysis workbench Bioinformatics 25 2009 1189 1191
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.A.3    Clamp, M.4    Barton, G.J.5
  • 52
    • 4344713150 scopus 로고    scopus 로고
    • O-acetylserine (thiol) lyase: An enigmatic enzyme of plant cysteine biosynthesis revisited in Arabidopsis thaliana
    • M. Wirtz, M. Droux, and R. Hell O-acetylserine (thiol) lyase: an enigmatic enzyme of plant cysteine biosynthesis revisited in Arabidopsis thaliana J. Exp. Bot. 55 2004 1785 1798
    • (2004) J. Exp. Bot. , vol.55 , pp. 1785-1798
    • Wirtz, M.1    Droux, M.2    Hell, R.3
  • 53
    • 78649997901 scopus 로고    scopus 로고
    • Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include N-terminal acetylation
    • M. Wirtz, C. Heeg, A.A. Samami, T. Ruppert, and R. Hell Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include N-terminal acetylation Amino Acids 39 2010 1077 1086
    • (2010) Amino Acids , vol.39 , pp. 1077-1086
    • Wirtz, M.1    Heeg, C.2    Samami, A.A.3    Ruppert, T.4    Hell, R.5
  • 54
    • 0000271226 scopus 로고
    • Subcellular and developmental distribution of beta-cyanoalanine synthase in barley leaves
    • E.S. Wurtele, B.L. Nikolau, and E.E. Conn Subcellular and developmental distribution of beta-cyanoalanine synthase in barley leaves Plant Physiol. 78 1985 285 290
    • (1985) Plant Physiol. , vol.78 , pp. 285-290
    • Wurtele, E.S.1    Nikolau, B.L.2    Conn, E.E.3
  • 55
    • 0034074441 scopus 로고    scopus 로고
    • Three Arabidopsis genes encoding proteins with differential activities for cysteine synthase and beta-cyanoalanine synthase
    • Y. Yamaguchi, T. Nakamura, T. Kusano, and H. Sano Three Arabidopsis genes encoding proteins with differential activities for cysteine synthase and beta-cyanoalanine synthase Plant Cell Physiol. 41 2000 465 476
    • (2000) Plant Cell Physiol. , vol.41 , pp. 465-476
    • Yamaguchi, Y.1    Nakamura, T.2    Kusano, T.3    Sano, H.4
  • 56
    • 77950261020 scopus 로고    scopus 로고
    • Sensing sulfur conditions: Simple to complex protein regulatory mechanisms in plant thiol metabolism
    • H. Yi, A. Galant, G.E. Ravilious, M.L. Preuss, and J.M. Jez Sensing sulfur conditions: simple to complex protein regulatory mechanisms in plant thiol metabolism Mol. Plant 3 2010 269 279
    • (2010) Mol. Plant , vol.3 , pp. 269-279
    • Yi, H.1    Galant, A.2    Ravilious, G.E.3    Preuss, M.L.4    Jez, J.M.5
  • 57
    • 84864483247 scopus 로고    scopus 로고
    • Structure of soybean β-cyanoalanine synthase and the molecular basis for cyanide detoxification in plants
    • H. Yi, M. Juergens, and J.M. Jez Structure of soybean β-cyanoalanine synthase and the molecular basis for cyanide detoxification in plants Plant Cell 24 2012 2696 2706
    • (2012) Plant Cell , vol.24 , pp. 2696-2706
    • Yi, H.1    Juergens, M.2    Jez, J.M.3
  • 59
    • 0001237406 scopus 로고
    • Cyanide metabolism in relation to ethylene production in plant tissues
    • W.K. Yip, and S.F. Yang Cyanide metabolism in relation to ethylene production in plant tissues Plant Physiol. 88 1988 473 476
    • (1988) Plant Physiol. , vol.88 , pp. 473-476
    • Yip, W.K.1    Yang, S.F.2
  • 60
    • 57349119513 scopus 로고    scopus 로고
    • Cloning and functional characterization of an O-acetylserine(thiol)lyase- encoding gene in wild soybean (Glycine soja)
    • C. Zhang, Q. Meng, J. Gai, and D. Yu Cloning and functional characterization of an O-acetylserine(thiol)lyase-encoding gene in wild soybean (Glycine soja) Mol. Biol. Rep. 35 2008 527 534
    • (2008) Mol. Biol. Rep. , vol.35 , pp. 527-534
    • Zhang, C.1    Meng, Q.2    Gai, J.3    Yu, D.4
  • 61
    • 58549118423 scopus 로고    scopus 로고
    • Characterization of O-acetylserine(thiol)lyase-encoding genes reveals their distinct but cooperative expression in cysteine synthesis of soybean [Glycine max (L.) Merr.]
    • C. Zhang, Q. Meng, M. Zhang, F. Huang, J. Gai, and D. Yu Characterization of O-acetylserine(thiol)lyase-encoding genes reveals their distinct but cooperative expression in cysteine synthesis of soybean [Glycine max (L.) Merr.] Plant Mol. Biol. Rep. 26 2008 277 291.
    • (2008) Plant Mol. Biol. Rep. , vol.26 , pp. 277-291
    • Zhang, C.1    Meng, Q.2    Zhang, M.3    Huang, F.4    Gai, J.5    Yu, D.6


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