메뉴 건너뛰기




Volumn 180, Issue 2, 2011, Pages 268-275

Active-site architecture of benzoxazinone-glucoside β-d-glucosidases in Triticeae

Author keywords

d Glucosidase; Benzoxazinone; Rye; Wheat

Indexed keywords

(2R) 2 O BETA D GLUCOPYRANOSYL 4 HYDROXY 2H 1,4 BENZOXAZIN 3(4H) ONE; (2R)-2-O-BETA-D-GLUCOPYRANOSYL-4-HYDROXY-2H-1,4-BENZOXAZIN-3(4H)-ONE; 2 O GLUCOPYRANOSYL 4 HYDROXY 7 METHOXY 1,4 BENZOXAZIN 3 ONE; 2,4 DIHYDROXY 7 METHOXY 1,4 BENZOXAZIN 3 ONE; 2,4-DIHYDROXY-7-METHOXY-1,4-BENZOXAZIN-3-ONE; 2-O-GLUCOPYRANOSYL-4-HYDROXY-7-METHOXY-1,4-BENZOXAZIN-3-ONE; BENZOXAZINE DERIVATIVE; BETA GLUCOSIDASE; COMPLEMENTARY DNA; GLUCOSIDE; VEGETABLE PROTEIN;

EID: 78650291221     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2010.09.001     Document Type: Article
Times cited : (16)

References (32)
  • 2
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat B., Davies G. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 1997, 7:637-644.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 3
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 1991, 280:309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 4
    • 0001463551 scopus 로고
    • Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a "retaining" glycosidase
    • Withers S.G., Warren R.A.J., Street I.P., Rupitz K., Kempton J.B., Aebersold R. Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a "retaining" glycosidase. J. Am. Chem. Soc. 1990, 112:5887-5889.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 5887-5889
    • Withers, S.G.1    Warren, R.A.J.2    Street, I.P.3    Rupitz, K.4    Kempton, J.B.5    Aebersold, R.6
  • 5
    • 35748962318 scopus 로고    scopus 로고
    • Molecular architecture of strictosidine glucosidase: the gateway to the biosynthesis of the monoterpenoid indole alkaloid family
    • Barleben L., Panjikar S., Ruppert M., Koepke J., Stockigt J. Molecular architecture of strictosidine glucosidase: the gateway to the biosynthesis of the monoterpenoid indole alkaloid family. Plant Cell 2007, 19:2886-2897.
    • (2007) Plant Cell , vol.19 , pp. 2886-2897
    • Barleben, L.1    Panjikar, S.2    Ruppert, M.3    Koepke, J.4    Stockigt, J.5
  • 6
    • 0035865504 scopus 로고    scopus 로고
    • Crystal structure of a monocotyledon (maize ZMGlu1) β-glucosidase and a model of its complex with p-nitrophenyl β-d-thioglucoside
    • Czjzek M., Cicek M., Zamboni V., Burmeister W.P., Bevan D.R., Henrissat B., Esen A. Crystal structure of a monocotyledon (maize ZMGlu1) β-glucosidase and a model of its complex with p-nitrophenyl β-d-thioglucoside. Biochem. J. 2001, 354:37-46.
    • (2001) Biochem. J. , vol.354 , pp. 37-46
    • Czjzek, M.1    Cicek, M.2    Zamboni, V.3    Burmeister, W.P.4    Bevan, D.R.5    Henrissat, B.6    Esen, A.7
  • 7
    • 0034610330 scopus 로고    scopus 로고
    • The mechanism of substrate (aglycone) specificity in β-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes
    • Czjzek M., Cicek M., Zamboni V., Bevan D.R., Henrissat B., Esen A. The mechanism of substrate (aglycone) specificity in β-glucosidases is revealed by crystal structures of mutant maize β-glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:13555-13560.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13555-13560
    • Czjzek, M.1    Cicek, M.2    Zamboni, V.3    Bevan, D.R.4    Henrissat, B.5    Esen, A.6
  • 8
    • 70349221692 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of Os3BGlu6, a rice β-glucosidase hydrolyzing hydrophobic glycosides and (1→3)- and (1→2)-linked disaccharides
    • Seshadri S., Akiyama T., Opassiri R., Kuaprasert B., Cairns J.K. Structural and enzymatic characterization of Os3BGlu6, a rice β-glucosidase hydrolyzing hydrophobic glycosides and (1→3)- and (1→2)-linked disaccharides. Plant Physiol. 2009, 151:47-58.
    • (2009) Plant Physiol. , vol.151 , pp. 47-58
    • Seshadri, S.1    Akiyama, T.2    Opassiri, R.3    Kuaprasert, B.4    Cairns, J.K.5
  • 10
    • 3843105862 scopus 로고    scopus 로고
    • Structural determinants of substrate specificity in family 1 β-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant β-glucosidase with strict specificity, in complex with its natural substrate
    • Verdoucq L., Moriniere J., Bevan D.R., Esen A., Vasella A., Henrissat B., Czjzek M. Structural determinants of substrate specificity in family 1 β-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant β-glucosidase with strict specificity, in complex with its natural substrate. J. Biol. Chem. 2004, 279:31796-31803.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31796-31803
    • Verdoucq, L.1    Moriniere, J.2    Bevan, D.R.3    Esen, A.4    Vasella, A.5    Henrissat, B.6    Czjzek, M.7
  • 11
    • 0029645413 scopus 로고
    • The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase
    • Barrett T., Suresh C.G., Tolley S.P., Dodson E.J., Hughes M.A. The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase. Structure 1995, 3:951-960.
    • (1995) Structure , vol.3 , pp. 951-960
    • Barrett, T.1    Suresh, C.G.2    Tolley, S.P.3    Dodson, E.J.4    Hughes, M.A.5
  • 12
    • 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 1997, 5:663-675.
    • (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
  • 14
    • 0034014079 scopus 로고    scopus 로고
    • Role of natural benzoxazinones in the survival strategy of plants
    • Sicker D., Frey M., Schulz M., Gierl A. Role of natural benzoxazinones in the survival strategy of plants. Int. Rev. Cytol. 2000, 198:319-346.
    • (2000) Int. Rev. Cytol. , vol.198 , pp. 319-346
    • Sicker, D.1    Frey, M.2    Schulz, M.3    Gierl, A.4
  • 15
    • 85032069874 scopus 로고
    • Hydroxamic acids (4-hydroxy-1,4-benzoxazin-3-ones), defence chemicals in the Gramineae
    • Niemeyer H. Hydroxamic acids (4-hydroxy-1,4-benzoxazin-3-ones), defence chemicals in the Gramineae. Phytochemistry 1988, 27:3349-3358.
    • (1988) Phytochemistry , vol.27 , pp. 3349-3358
    • Niemeyer, H.1
  • 16
    • 0038688699 scopus 로고    scopus 로고
    • Cloning of a plastidic rye (Secale cereale) β-glucosidase cDNA and its expression in Escherichia coli
    • Nikus J., Esen A., Jonsson L.M.V. Cloning of a plastidic rye (Secale cereale) β-glucosidase cDNA and its expression in Escherichia coli. Physiol. Plant. 2003, 118:337-345.
    • (2003) Physiol. Plant. , vol.118 , pp. 337-345
    • Nikus, J.1    Esen, A.2    Jonsson, L.M.V.3
  • 17
    • 0043092250 scopus 로고    scopus 로고
    • Mutational and structural analysis of aglycone specificity in maize and sorghum β-glucosidases
    • Verdoucq L., Czjzek M., Moriniere J., Bevan D.R., Esen A. Mutational and structural analysis of aglycone specificity in maize and sorghum β-glucosidases. J. Biol. Chem. 2003, 278:25055-25062.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25055-25062
    • Verdoucq, L.1    Czjzek, M.2    Moriniere, J.3    Bevan, D.R.4    Esen, A.5
  • 18
    • 0034056643 scopus 로고    scopus 로고
    • Purification and characterization of a hydroxamic acid glucoside β-glucosidase from wheat (Triticum aestivum L.) seedlings
    • Sue M., Ishihara A., Iwamura H. Purification and characterization of a hydroxamic acid glucoside β-glucosidase from wheat (Triticum aestivum L.) seedlings. Planta 2000, 210:432-438.
    • (2000) Planta , vol.210 , pp. 432-438
    • Sue, M.1    Ishihara, A.2    Iwamura, H.3
  • 21
    • 78650295947 scopus 로고
    • Joint CCP4 + ESF-EAMCB Newsletter on Protein Crystallography, Recent changes to the MOSFLM package for processing film and image plate data
    • A.G.W. Leslie, Joint CCP4 + ESF-EAMCB Newsletter on Protein Crystallography, No. 26. Recent changes to the MOSFLM package for processing film and image plate data (1992).
    • (1992) , vol.26
    • Leslie, A.G.W.1
  • 22
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Cryst. 1997, 30:1022-1025.
    • (1997) J. Appl. Cryst. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 25
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 1999, 125:156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 28
    • 0034640778 scopus 로고    scopus 로고
    • Purification and characterization of a β-glucosidase from rye (Secale cereale L.) seedlings
    • Sue M., Ishihara A., Iwamura H. Purification and characterization of a β-glucosidase from rye (Secale cereale L.) seedlings. Plant Sci. 2000, 155:67-74.
    • (2000) Plant Sci. , vol.155 , pp. 67-74
    • Sue, M.1    Ishihara, A.2    Iwamura, H.3
  • 29
    • 0001410590 scopus 로고
    • Identification of a covalent α-d-glucopyranosyl enzyme intermediate formed on a β-glucosidase
    • Withers S.G., Street I.P. Identification of a covalent α-d-glucopyranosyl enzyme intermediate formed on a β-glucosidase. J. Am. Chem. Soc. 1988, 110:8551-8553.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8551-8553
    • Withers, S.G.1    Street, I.P.2
  • 30
    • 0023940907 scopus 로고
    • 2-Deoxy-2-fluoro-d-glycosyl fluorides. A new class of specific mechanism-based glycosidase inhibitors
    • Withers S.G., Rupitz K., Street I.P. 2-Deoxy-2-fluoro-d-glycosyl fluorides. A new class of specific mechanism-based glycosidase inhibitors. J. Biol. Chem. 1988, 263:7929-7932.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7929-7932
    • Withers, S.G.1    Rupitz, K.2    Street, I.P.3
  • 31
    • 0034671719 scopus 로고    scopus 로고
    • High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base
    • Burmeister W.P., Cottaz S., Rollin P., Vasella A., Henrissat B. High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base. J. Biol. Chem. 2000, 275:39385-39393.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39385-39393
    • Burmeister, W.P.1    Cottaz, S.2    Rollin, P.3    Vasella, A.4    Henrissat, B.5
  • 32
    • 33646270203 scopus 로고    scopus 로고
    • Molecular basis of substrate specificity in family 1 glycoside hydrolases
    • Marana S.R. Molecular basis of substrate specificity in family 1 glycoside hydrolases. IUBMB Life 2006, 58:63-73.
    • (2006) IUBMB Life , vol.58 , pp. 63-73
    • Marana, S.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.