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Volumn 17, Issue 3, 1999, Pages 414-420

Functional expression and characterization of the myrosinase MYR1 from Brassica napus in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

2 DEOXY 2 FLUOROGLUCOTROPAEOLIN; 4 HYDROXYBENZYLGLUCOSINOLATE; ASCORBIC ACID; CASTANOSPERMINE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITOR; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYMIC HYDROLYSIS; FUNGAL GROWTH; HETEROLOGOUS PRODUCT; PH; PROTEIN EXPRESSION; RECOMBINANT ENZYME; THIOGLUCOSIDASE; WESTERN BLOTTING;

EID: 0033486155     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1158     Document Type: Article
Times cited : (45)

References (24)
  • 2
    • 0002829778 scopus 로고
    • Immunogold-EM localization of myrosinase in Brassicaceae
    • Thangstad O. P., Evjen K., Bones A. Immunogold-EM localization of myrosinase in Brassicaceae. Protoplasma. 161:1991;85-93.
    • (1991) Protoplasma , vol.161 , pp. 85-93
    • Thangstad, O.P.1    Evjen, K.2    Bones, A.3
  • 3
    • 0000197605 scopus 로고
    • Biological effects of glucosinolates
    • H. G. Cutler. Washington: Am. Chem. Soc. Symp.
    • Chew F. S. Biological effects of glucosinolates. Cutler H. G. Biologically Active Natural Products. 1988;155-181 Am. Chem. Soc. Symp. Washington.
    • (1988) Biologically Active Natural Products , pp. 155-181
    • Chew, F.S.1
  • 4
    • 0000295679 scopus 로고    scopus 로고
    • The myrosinase-glucosinolate system, its organisation and biochemistry
    • Bones A. M., Rossiter J. T. The myrosinase-glucosinolate system, its organisation and biochemistry. Physiol. Plant. 97:1996;194-208.
    • (1996) Physiol. Plant. , vol.97 , pp. 194-208
    • Bones, A.M.1    Rossiter, J.T.2
  • 5
    • 0028362240 scopus 로고
    • Molecular characterization of two cloned nitrilases from Arabidopsis thaliana: Key enzymes in biosynthesis of the plant hormone indole-3-acetic acid
    • Bartling D., Seedorf M., Schmidt R. C., Weiler E. W. Molecular characterization of two cloned nitrilases from Arabidopsis thaliana: Key enzymes in biosynthesis of the plant hormone indole-3-acetic acid. Proc. Nat. Acad. Sci. USA. 91:1994;6021-6025.
    • (1994) Proc. Nat. Acad. Sci. USA , vol.91 , pp. 6021-6025
    • Bartling, D.1    Seedorf, M.2    Schmidt, R.C.3    Weiler, E.W.4
  • 8
    • 0027333312 scopus 로고
    • The thioglucoside glucohydrolase (myrosinase) gene family in Brassicaceae
    • Thangstad O. P., Winge P., Husebye H., Bones A. The thioglucoside glucohydrolase (myrosinase) gene family in Brassicaceae. Plant Mol. Biol. 23:1993;511-524.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 511-524
    • Thangstad, O.P.1    Winge, P.2    Husebye, H.3    Bones, A.4
  • 9
    • 84989724112 scopus 로고
    • Purification, characterization and partial amino acid sequencing of β-thioglucosidase from Brassica napus L
    • Bones A. M., Slupphaug G. Purification, characterization and partial amino acid sequencing of β-thioglucosidase from Brassica napus L. Plant Physiol. 134:1989;722-729.
    • (1989) Plant Physiol. , vol.134 , pp. 722-729
    • Bones, A.M.1    Slupphaug, G.2
  • 10
    • 84890441310 scopus 로고
    • Enzymic properties of purified myrosinase from Lepidium sativum seedlings
    • Durham P. L., Poulton J. E. Enzymic properties of purified myrosinase from Lepidium sativum seedlings. Z. Naturforsch. 45:1990;173-178.
    • (1990) Z. Naturforsch. , vol.45 , pp. 173-178
    • Durham, P.L.1    Poulton, J.E.2
  • 11
    • 0025359610 scopus 로고
    • An improved method for the purification of myrosinase and its physicochemical characterization
    • Pessina A., Thomas R. M., Palmieri S., Luisi P. L. An improved method for the purification of myrosinase and its physicochemical characterization. Arch. Biochem. Biophys. 280:1990;383-389.
    • (1990) Arch. Biochem. Biophys. , vol.280 , pp. 383-389
    • Pessina, A.1    Thomas, R.M.2    Palmieri, S.3    Luisi, P.L.4
  • 12
    • 0001222897 scopus 로고
    • Sequence of a cDNA clone encoding the enzyme myrosinase and expression of myrosinase in different tissues of Brassica napus
    • Falk A., Xue J., Lenman M., Rask L. Sequence of a cDNA clone encoding the enzyme myrosinase and expression of myrosinase in different tissues of Brassica napus. Plant Sci. 83:1992;181-186.
    • (1992) Plant Sci. , vol.83 , pp. 181-186
    • Falk, A.1    Xue, J.2    Lenman, M.3    Rask, L.4
  • 13
    • 0029257401 scopus 로고
    • Characterization of a new myrosinase in Brassica napus
    • Falk A., Ek B., Rask L. Characterization of a new myrosinase in Brassica napus. Plant Mol. Biol. 27:1995;863-874.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 863-874
    • Falk, A.1    Ek, B.2    Rask, L.3
  • 14
    • 0026477042 scopus 로고
    • The glucosinolate-degrading enzyme myrosinase in Brassicaceae is encoded by a gene family
    • Xue J., Lenman M., Falk A., Rask L. The glucosinolate-degrading enzyme myrosinase in Brassicaceae is encoded by a gene family. Plant Mol. Biol. 18:1992;387-398.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 387-398
    • Xue, J.1    Lenman, M.2    Falk, A.3    Rask, L.4
  • 15
    • 0001083002 scopus 로고
    • Getting started with yeast
    • F. Sherman, G. R. Fink, & J. R Hicks. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Sherman F. Getting started with yeast. Sherman F., Fink G. R., Hicks J. R. Methods in Yeast Genetics. 1983;3-21 Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1983) Methods in Yeast Genetics , pp. 3-21
    • Sherman, F.1
  • 16
  • 17
    • 79959321909 scopus 로고    scopus 로고
    • Preparation of protein extracts from yeast
    • F. M. Ausubel. New York: Wiley
    • Dunn B., Wobbe C. R. Preparation of protein extracts from yeast. Ausubel F. M. Current Protocols in Molecular Biology. 1997;13.13.4-13.13.5 Wiley, New York.
    • (1997) Current Protocols in Molecular Biology , pp. 13134-13135
    • Dunn, B.1    Wobbe, C.R.2
  • 18
    • 0000856498 scopus 로고
    • Two nuclear mutations that block mitochondria protein import in yeast
    • Yaffe M. P., Schatz G. Two nuclear mutations that block mitochondria protein import in yeast. Proc. Nat. Acad. Sci. USA. 81:1984;4819-4823.
    • (1984) Proc. Nat. Acad. Sci. USA , vol.81 , pp. 4819-4823
    • Yaffe, M.P.1    Schatz, G.2
  • 19
    • 0022539027 scopus 로고
    • Peptide and protein molecular weight determination by electrophoresis using a high molarity Tris buffer system without urea
    • Fling S. P., Gregerson D. S. Peptide and protein molecular weight determination by electrophoresis using a high molarity Tris buffer system without urea. Anal. Biochem. 155:1986;83-88.
    • (1986) Anal. Biochem. , vol.155 , pp. 83-88
    • Fling, S.P.1    Gregerson, D.S.2
  • 20
    • 0040034407 scopus 로고
    • The decomposition products of sinalbin and their degradation pathways
    • Kawakishi S., Namiki M., Watanabe H., Muramatsu K. The decomposition products of sinalbin and their degradation pathways. Agric. Biol. Chem. 31:1967;823-830.
    • (1967) Agric. Biol. Chem. , vol.31 , pp. 823-830
    • Kawakishi, S.1    Namiki, M.2    Watanabe, H.3    Muramatsu, K.4
  • 21
    • 0029954123 scopus 로고    scopus 로고
    • Mechanism-based inhibition and stereochemistry of glucosinolate hydrolysis by myrosinase
    • Cottaz S., Henrissat B., Driguez H. Mechanism-based inhibition and stereochemistry of glucosinolate hydrolysis by myrosinase. Biochemistry. 35:1996;15256-15259.
    • (1996) Biochemistry , vol.35 , pp. 15256-15259
    • Cottaz, S.1    Henrissat, B.2    Driguez, H.3
  • 22
    • 84989718516 scopus 로고
    • Development and characteristics of myrosinase in Brassica napus during early seedling growth
    • James D. C., Rossiter J. T. Development and characteristics of myrosinase in Brassica napus during early seedling growth. Physiol. Plant. 82:1991;163-170.
    • (1991) Physiol. Plant , vol.82 , pp. 163-170
    • James, D.C.1    Rossiter, J.T.2
  • 23
    • 0001873443 scopus 로고
    • Effect of castanospermine and related polyhydroxyalkaloids on purified myrosinase from Lepidium sativum seedlings
    • Durham P. L., Poulton J. E. Effect of castanospermine and related polyhydroxyalkaloids on purified myrosinase from Lepidium sativum seedlings. Plant Physiol. 90:1989;48-52.
    • (1989) Plant Physiol. , vol.90 , pp. 48-52
    • Durham, P.L.1    Poulton, J.E.2
  • 24
    • 0031570331 scopus 로고    scopus 로고
    • The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase
    • Burmeister W. P., Cottaz S., Driguez H., Iori R., Palmieri S., Henrissat B. The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase. Structure. 5:1997;663-675.
    • (1997) Structure , vol.5 , pp. 663-675
    • Burmeister, W.P.1    Cottaz, S.2    Driguez, H.3    Iori, R.4    Palmieri, S.5    Henrissat, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.