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Volumn 26, Issue 4, 2009, Pages 495-510

C1-/C2-aromatic-imino-glyco-conjugates: Experimental and computational studies of binding, inhibition and docking aspects towards glycosidases isolated from soybean and jack bean

Author keywords

C1 C2 aromatic imino glyco conjugates; Fluorescence quenching; Glycosidase inhibition; Glycosidases from soybean and jack bean; Pure mannosidase; Rigid docking

Indexed keywords

ALPHA MANNOSIDASE; GALACTOSE; GLYCOSIDASE; IMINE; IMINOSUGAR; LACTOSE; RIBOSE;

EID: 64149127789     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-008-9199-4     Document Type: Article
Times cited : (9)

References (36)
  • 1
    • 0037416196 scopus 로고    scopus 로고
    • A role for N-glycanase in the cytosolic turnover of glycoproteins
    • C. Hirsch D.I. Bolm H.L. Polegh 2003 A role for N-glycanase in the cytosolic turnover of glycoproteins EMBO J. 22 1036 1046
    • (2003) EMBO J. , vol.22 , pp. 1036-1046
    • Hirsch, C.1    Bolm, D.I.2    Polegh, H.L.3
  • 2
    • 26244466799 scopus 로고    scopus 로고
    • Characterization of schizosaccharo-myces pombe ER α-mannosidase: A reevaluation of the role of the enzyme on ER-associated degradation
    • F. Movsichoff O.A. Castro A. Parodi 2005 Characterization of schizosaccharo-myces pombe ER α-mannosidase: A reevaluation of the role of the enzyme on ER-associated degradation J. Mol. Biol. Cell 16 4714 4724
    • (2005) J. Mol. Biol. Cell , vol.16 , pp. 4714-4724
    • Movsichoff, F.1    Castro, O.A.2    Parodi, A.3
  • 3
    • 0034731340 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER)-associated degradation of misfolded n-linked glycoproteins is suppressed upon inhibition of ER mannosidase i
    • F. Tokunaga C. Brostrom T. Koide P. Arvan 2000 Endoplasmic reticulum (ER)-associated degradation of misfolded n-linked glycoproteins is suppressed upon inhibition of ER mannosidase I J. Biol. Chem. 275 40757 40764
    • (2000) J. Biol. Chem. , vol.275 , pp. 40757-40764
    • Tokunaga, F.1    Brostrom, C.2    Koide, T.3    Arvan, P.4
  • 4
    • 0021738039 scopus 로고
    • Novel glycosidase inhibitors, nojirimycin b and d-mannonic-δ-lactam isolation, structure determination and biological property
    • T. Niwa T. Tsuruoka H. Goi Y. Kodama J. Itoh S. Inouye Y. Yamada T. Niida M. Nobe Y. Ogawa 1984 Novel glycosidase inhibitors, nojirimycin b and d-mannonic-δ-lactam isolation, structure determination and biological property J. Antibiot. 37 1579 1586
    • (1984) J. Antibiot. , vol.37 , pp. 1579-1586
    • Niwa, T.1    Tsuruoka, T.2    Goi, H.3    Kodama, Y.4    Itoh, J.5    Inouye, S.6    Yamada, Y.7    Niida, T.8    Nobe, M.9    Ogawa, Y.10
  • 5
    • 0000094845 scopus 로고    scopus 로고
    • Anomer-selective inhibition of glycosidases using aminocyclopentanols
    • E. Leroy J.L. Reymond 1999 Anomer-selective inhibition of glycosidases using aminocyclopentanols Org. Lett. 1 775 777
    • (1999) Org. Lett. , vol.1 , pp. 775-777
    • Leroy, E.1    Reymond, J.L.2
  • 6
    • 0034719245 scopus 로고    scopus 로고
    • Synthesis and evaluation of aminocyclopentitol inhibitors of β-glucosidases
    • O. Boss E. Leroy A. Blaser J.L. Reymond 2000 Synthesis and evaluation of aminocyclopentitol inhibitors of β-glucosidases Org. Lett. 2 151 154
    • (2000) Org. Lett. , vol.2 , pp. 151-154
    • Boss, O.1    Leroy, E.2    Blaser, A.3    Reymond, J.L.4
  • 7
    • 0035805650 scopus 로고    scopus 로고
    • Syntheses via isoxazolines, part 25. Amino(hydroxymethyl)cyclo- pentanetriols, an emerging class of potent glycosidase inhibitors-Part I: Synthesis and evaluation of β-d-pyranoside analogues in the manno, gluco, galacto, and GlcNAc series
    • M. Kleban P. Hilgers J.N. Greul R.D. Kugler J. Li S. Picasso P. Vogel V. Jager 2001 Syntheses via isoxazolines, part 25. Amino(hydroxymethyl)cyclo- pentanetriols, an emerging class of potent glycosidase inhibitors-Part I: synthesis and evaluation of β-d-pyranoside analogues in the manno, gluco, galacto, and GlcNAc series ChemBioChem 2 365 368
    • (2001) ChemBioChem , vol.2 , pp. 365-368
    • Kleban, M.1    Hilgers, P.2    Greul, J.N.3    Kugler, R.D.4    Li, J.5    Picasso, S.6    Vogel, P.7    Jager, V.8
  • 8
    • 0035805652 scopus 로고    scopus 로고
    • Amino-(hydroxymethyl)cyclopentanetriols, an emerging class of potent glycosidase inhibitors-Part II: Synthesis, evaluation, and optimization of β-d-galactopyranoside analogues
    • J.N. Greul M. Kleban B. Schneider S. Picasso V. Jager 2001 Amino-(hydroxymethyl)cyclopentanetriols, an emerging class of potent glycosidase inhibitors-Part II: synthesis, evaluation, and optimization of β-d-galactopyranoside analogues ChemBioChem 2 368 370
    • (2001) ChemBioChem , vol.2 , pp. 368-370
    • Greul, J.N.1    Kleban, M.2    Schneider, B.3    Picasso, S.4    Jager, V.5
  • 9
    • 0035194309 scopus 로고    scopus 로고
    • Combinatorial library of five-membered iminocyclitol and the inhibitory activities against glyco-enzymes
    • C. Saotome C.H. Wong O. Kanie 2001 Combinatorial library of five-membered iminocyclitol and the inhibitory activities against glyco-enzymes Chem. Biol. 8 1061 1070
    • (2001) Chem. Biol. , vol.8 , pp. 1061-1070
    • Saotome, C.1    Wong, C.H.2    Kanie, O.3
  • 11
    • 0142119368 scopus 로고    scopus 로고
    • Rapid diversity-oriented synthesis in microtiter plates for in situ screening: Discovery of potent and selective α-fucosidase inhibitors
    • C.Y. Wu C.F. Chang J.S.Y. Chen C.H. Wong C.H. Lin 2003 Rapid diversity-oriented synthesis in microtiter plates for in situ screening: discovery of potent and selective α-fucosidase inhibitors Angew. Chem. Int. Ed. 42 4661 4664
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 4661-4664
    • Wu, C.Y.1    Chang, C.F.2    Chen, J.S.Y.3    Wong, C.H.4    Lin, C.H.5
  • 12
    • 30444438410 scopus 로고    scopus 로고
    • Novel five-membered iminocyclitol derivatives as selective and potent glycosidase inhibitors: New structures for antivirals and osteoarthritis
    • P.H. Liang W.C. Cheng Y.L. Lee H.P. Yu Y.T. Wu Y.L. Lin C.H. Wong 2006 Novel five-membered iminocyclitol derivatives as selective and potent glycosidase inhibitors: new structures for antivirals and osteoarthritis ChemBioChem 7 165 173
    • (2006) ChemBioChem , vol.7 , pp. 165-173
    • Liang, P.H.1    Cheng, W.C.2    Lee, Y.L.3    Yu, H.P.4    Wu, Y.T.5    Lin, Y.L.6    Wong, C.H.7
  • 13
    • 0037421266 scopus 로고    scopus 로고
    • First stereocontrolled synthesis and biological evaluation of 1,6-dideoxy-L-nojirimycin
    • A. Bordier P. Compain O.R. Martin K. Ikeda N. Asano 2003 First stereocontrolled synthesis and biological evaluation of 1,6-dideoxy-L- nojirimycin Tetrahedron 14 47 51
    • (2003) Tetrahedron , vol.14 , pp. 47-51
    • Bordier, A.1    Compain, P.2    Martin, O.R.3    Ikeda, K.4    Asano, N.5
  • 14
    • 33745594042 scopus 로고    scopus 로고
    • Synthesis and evaluation of glycosidase inhibitory activity of N-butyl 1-deoxy-d-gluco-homonojirimycin and N-butyl 1-deoxy-l-ido-homonojirimycin
    • S.D. Markad N.S. Karanjule T. Sharma S.G. Sabharwal D.D. Dhavale 2006 Synthesis and evaluation of glycosidase inhibitory activity of N-butyl 1-deoxy-d-gluco-homonojirimycin and N-butyl 1-deoxy-l-ido-homonojirimycin Bioorg. Med. Chem. 14 5535 5539
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 5535-5539
    • Markad, S.D.1    Karanjule, N.S.2    Sharma, T.3    Sabharwal, S.G.4    Dhavale, D.D.5
  • 15
    • 0000417547 scopus 로고
    • Total synthesis and chemical design of useful glycosidase inhibitors
    • K. Tatsuta 1984 Total synthesis and chemical design of useful glycosidase inhibitors Pure Appl. Chem. 68 1341 1346
    • (1984) Pure Appl. Chem. , vol.68 , pp. 1341-1346
    • Tatsuta, K.1
  • 17
    • 21744444754 scopus 로고    scopus 로고
    • Glycosidase inhibition by 1-glycosyl-4-phenyl triazoles
    • L.L. Rossi A. Basu 2005 Glycosidase inhibition by 1-glycosyl-4-phenyl triazoles Bioorg. Med. Chem. Lett. 15 3596 3599
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 3596-3599
    • Rossi, L.L.1    Basu, A.2
  • 18
    • 33747305857 scopus 로고    scopus 로고
    • Carbohydrate-based switch-on molecular sensor for Cu(II) in buffer: Absorption and fluorescence study of the selective recognition of Cu(II) ions by galactosyl derivatives in HEPES buffer
    • N.K. Singhal B. Ramanujam V. Mariappandar C.P. Rao 2006 Carbohydrate-based switch-on molecular sensor for Cu(II) in buffer: absorption and fluorescence study of the selective recognition of Cu(II) ions by galactosyl derivatives in HEPES buffer Org. Lett. 8 3525 3528
    • (2006) Org. Lett. , vol.8 , pp. 3525-3528
    • Singhal, N.K.1    Ramanujam, B.2    Mariappandar, V.3    Rao, C.P.4
  • 19
    • 34247616666 scopus 로고    scopus 로고
    • Experimental and computational studies of the recognition of amino acids by galactosyl-imine and -amine derivatives: An attempt to understand the lectin-carbohydrate interactions
    • R. Ahuja N.K. Singhal B. Ramanujam M. Ravikumar C.P. Rao 2007 Experimental and computational studies of the recognition of amino acids by galactosyl-imine and -amine derivatives: an attempt to understand the lectin-carbohydrate interactions J. Org. Chem. 72 3430 3442
    • (2007) J. Org. Chem. , vol.72 , pp. 3430-3442
    • Ahuja, R.1    Singhal, N.K.2    Ramanujam, B.3    Ravikumar, M.4    Rao, C.P.5
  • 20
    • 51249174308 scopus 로고
    • The nature of lectins from Dolichos lablab
    • N.S. Kumar D.R. Rao 1986 The nature of lectins from Dolichos lablab J. Biosci. 10 95 109
    • (1986) J. Biosci. , vol.10 , pp. 95-109
    • Kumar, N.S.1    Rao, D.R.2
  • 22
    • 0026505784 scopus 로고
    • Characterization of two galactosidases extracted from wheat germ with a hydroalcoholic solvent
    • M.D. Papet D. Delay M. Monsigny F. Delmotte 1992 Characterization of two galactosidases extracted from wheat germ with a hydroalcoholic solvent Biochimie 74 53 56
    • (1992) Biochimie , vol.74 , pp. 53-56
    • Papet, M.D.1    Delay, D.2    Monsigny, M.3    Delmotte, F.4
  • 23
    • 0014370674 scopus 로고
    • Purification and properties of α-d-mannosidase from jack-bean meal
    • S.M. Snaith G.A. Levvy 1968 Purification and properties of α-d-mannosidase from jack-bean meal Biochem. J. 110 663 670
    • (1968) Biochem. J. , vol.110 , pp. 663-670
    • Snaith, S.M.1    Levvy, G.A.2
  • 24
    • 0033135605 scopus 로고    scopus 로고
    • Structural and dynamic aspects of β-glycosidase from mesophilic and thermophilic bacteria by multitryptophanyl emission decay studies
    • E. Bismuto R. Nucci M. Rossi G. Irace 1999 Structural and dynamic aspects of β-glycosidase from mesophilic and thermophilic bacteria by multitryptophanyl emission decay studies Proteins 35 163 172
    • (1999) Proteins , vol.35 , pp. 163-172
    • Bismuto, E.1    Nucci, R.2    Rossi, M.3    Irace, G.4
  • 25
    • 0034647627 scopus 로고    scopus 로고
    • The role of tryptophan residues in substrate binding to catalytic domains A and B of xylanase C from Fibrobacter succinogenes S85
    • K.A. McAllister L. Marrone A.J. Clarke 2000 The role of tryptophan residues in substrate binding to catalytic domains A and B of xylanase C from Fibrobacter succinogenes S85 Biochim. Biophys. Acta. 1480 342 352
    • (2000) Biochim. Biophys. Acta. , vol.1480 , pp. 342-352
    • McAllister, K.A.1    Marrone, L.2    Clarke, A.J.3
  • 27
    • 34548672784 scopus 로고    scopus 로고
    • ParDOCK: An all atom energy based Monte Carlo docking protocol for protein-ligand complexes
    • A. Gupta A. Gandhimathi P. Sharma B. Jayaram 2007 ParDOCK: an all atom energy based Monte Carlo docking protocol for protein-ligand complexes Protein Pept. Lett. 14 632 646
    • (2007) Protein Pept. Lett. , vol.14 , pp. 632-646
    • Gupta, A.1    Gandhimathi, A.2    Sharma, P.3    Jayaram, B.4
  • 28
    • 0037827688 scopus 로고    scopus 로고
    • Crystal structure of rice α-galactosidase complexed with D-galactose
    • Z. Fujimoto S. Kaneko M. Momma H. Kobayashi H. Mizuno 2003 Crystal structure of rice α-galactosidase complexed with D-galactose J. Biol. Chem. 278 20313 20318
    • (2003) J. Biol. Chem. , vol.278 , pp. 20313-20318
    • Fujimoto, Z.1    Kaneko, S.2    Momma, M.3    Kobayashi, H.4    Mizuno, H.5
  • 29
    • 0034731519 scopus 로고    scopus 로고
    • Structural basis for catalysis and inhibition of N-glycan processing class I-α-1,2-mannosidases
    • F. Vallee K. Karaveg A. Herscovics K.W. Moremen P.L. Howell 2000 Structural basis for catalysis and inhibition of N-glycan processing class I-α-1,2-mannosidases J. Biol. Chem. 275 41287 41298
    • (2000) J. Biol. Chem. , vol.275 , pp. 41287-41298
    • Vallee, F.1    Karaveg, K.2    Herscovics, A.3    Moremen, K.W.4    Howell, P.L.5
  • 30
    • 0028211360 scopus 로고
    • Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase
    • W.W. Wakarchuk R.L. Campbell W.L. Sung J. Davoodi M. Yaguchi 1994 Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase Protein Sci. 3 467 475
    • (1994) Protein Sci. , vol.3 , pp. 467-475
    • Wakarchuk, W.W.1    Campbell, R.L.2    Sung, W.L.3    Davoodi, J.4    Yaguchi, M.5
  • 31
    • 0036124422 scopus 로고    scopus 로고
    • The 1.9 Å Structure of α-N-acetylgalactosaminidase: Molecular basis of glycosidase deficiency diseases
    • S.C. Garman L. Hannick A. Zhu D.N. Garboczi 2002 The 1.9 Å Structure of α-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases Structure 10 425 434
    • (2002) Structure , vol.10 , pp. 425-434
    • Garman, S.C.1    Hannick, L.2    Zhu, A.3    Garboczi, D.N.4
  • 32
    • 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
    • M. Czjzek M. Cicek V.R. Zamboni W.P. Burmeister D.R. Bevan B. Henrissat A. Esen 2001 Crystal structure of a monocotyledon (maize ZMGlu1) β-glucosidase and a model of its complex with p-nitrophenyl β-d-thioglucoside Biochem. J. 354 37 46
    • (2001) Biochem. J. , vol.354 , pp. 37-46
    • Czjzek, M.1    Cicek, M.2    Zamboni, V.R.3    Burmeister, W.P.4    Bevan, D.R.5    Henrissat, B.6    Esen, A.7
  • 33
    • 33646253657 scopus 로고    scopus 로고
    • Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose
    • M. Czjzek F. Alberto E. Jordi H. Bernard 2006 Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose Biochem. J. 395 457 462
    • (2006) Biochem. J. , vol.395 , pp. 457-462
    • Czjzek, M.1    Alberto, F.2    Jordi, E.3    Bernard, H.4
  • 34
    • 0028519285 scopus 로고
    • Crystal structure of trichosanthin-NADPH complex at 1.7 Å resolution reveals active-site architecture
    • Y. Wang J.P. Xiong Z.X. Xia 1994 Crystal structure of trichosanthin-NADPH complex at 1.7 Å resolution reveals active-site architecture Nat. Struct. Biol. 1 695 700
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 695-700
    • Wang, Y.1    Xiong, J.P.2    Xia, Z.X.3


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