메뉴 건너뛰기




Volumn 5, Issue 11, 1996, Pages 2311-2318

Probing the role of tryptophan residues in a cellulose-binding domain by chemical modification

Author keywords

absorbance spectroscopy; cellulose binding; fluorescence spectroscopy; N bromosuccinimide; NMR

Indexed keywords

CELLULOSE; GLUCAN GLUCOSIDASE; N BROMOSUCCINIMIDE; TRYPTOPHAN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 0029849212     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560051117     Document Type: Article
Times cited : (54)

References (34)
  • 1
    • 0028031522 scopus 로고
    • Quantitation of tryptophan and tyrosine residues in proteins by fourth-derivative spectroscopy
    • Bray MR, Carriere AD, Clarke AJ. 1994. Quantitation of tryptophan and tyrosine residues in proteins by fourth-derivative spectroscopy. Anal Biochem 221:278-284.
    • (1994) Anal Biochem , vol.221 , pp. 278-284
    • Bray, M.R.1    Carriere, A.D.2    Clarke, A.J.3
  • 2
    • 0028084395 scopus 로고
    • Identification of a glutamate residue at the active site of xylanase A from Schizophyllum commune
    • Bray MR, Clarke AJ. 1994. Identification of a glutamate residue at the active site of xylanase A from Schizophyllum commune. Eur J Biochem 219:821-827.
    • (1994) Eur J Biochem , vol.219 , pp. 821-827
    • Bray, M.R.1    Clarke, A.J.2
  • 3
    • 0028939962 scopus 로고
    • Identification of an essential tyrosyl residue in the binding site of Schizophyllum commune xylanase A
    • Bray MR, Clarke AJ. 1995. Identification of an essential tyrosyl residue in the binding site of Schizophyllum commune xylanase A. Biochemistry 34:2006-2014.
    • (1995) Biochemistry , vol.34 , pp. 2006-2014
    • Bray, M.R.1    Clarke, A.J.2
  • 4
    • 0029965579 scopus 로고    scopus 로고
    • Binding of the cellulose-binding domain of exoglucanase Cex from Cellulomonas fimi to insoluble cellulose is entropically driven
    • Forthcoming
    • Creagh AL, Ong E, Jervis E, Kilburn DG, Haynes CA. 1996. Binding of the cellulose-binding domain of exoglucanase Cex from Cellulomonas fimi to insoluble cellulose is entropically driven. Proc Natl Acad Sci USA. Forthcoming.
    • (1996) Proc Natl Acad Sci USA
    • Creagh, A.L.1    Ong, E.2    Jervis, E.3    Kilburn, D.G.4    Haynes, C.A.5
  • 5
    • 0028364450 scopus 로고
    • The cellulose-binding domain of endoglucanase A (CenA) from Cellulomonas fimi: Evidence for the involvement of tryptophan residues in binding
    • Din N, Forsythe IJ, Burtnick LD, Gilkes NR, Miller RC Jr, Warren RAJ, Kilburn DG. 1994. The cellulose-binding domain of endoglucanase A (CenA) from Cellulomonas fimi: Evidence for the involvement of tryptophan residues in binding. Mol Microbiol 11:747-755.
    • (1994) Mol Microbiol , vol.11 , pp. 747-755
    • Din, N.1    Forsythe, I.J.2    Burtnick, L.D.3    Gilkes, N.R.4    Miller Jr., R.C.5    Warren, R.A.J.6    Kilburn, D.G.7
  • 6
    • 0015214379 scopus 로고
    • Changes in conformation of insolubilized trypsin and chymotrypsin, followed by fluorescence
    • Gabel D, Steinberg IZ, Katchalski E. 1971. Changes in conformation of insolubilized trypsin and chymotrypsin, followed by fluorescence. Biochemistry 10:4661-4669.
    • (1971) Biochemistry , vol.10 , pp. 4661-4669
    • Gabel, D.1    Steinberg, I.Z.2    Katchalski, E.3
  • 8
    • 0029072063 scopus 로고
    • pTugA and pTugAS: Vectors for high-level expression of cloned genes in Escherichia coli
    • Graham RW, Greenwood JM, Warren RAJ, Kilburn DG, Trimbur DE. 1995. pTugA and pTugAS: Vectors for high-level expression of cloned genes in Escherichia coli. Gene 158:51-54.
    • (1995) Gene , vol.158 , pp. 51-54
    • Graham, R.W.1    Greenwood, J.M.2    Warren, R.A.J.3    Kilburn, D.G.4    Trimbur, D.E.5
  • 9
    • 0345410714 scopus 로고
    • Oxidation studies of indoles and the tertiary structure of proteins
    • Green NM, Witkop B. 1964. Oxidation studies of indoles and the tertiary structure of proteins. Trans NY Acad Sci 26:659-669.
    • (1964) Trans NY Acad Sci , vol.26 , pp. 659-669
    • Green, N.M.1    Witkop, B.2
  • 10
    • 0014687881 scopus 로고
    • Fluorescence study of interactions between valyl-tRNA synthetase and valyl-specific tRNAs from Escherichia coli
    • Hélène C, Brun F, Yaniv M. 1969. Fluorescence study of interactions between valyl-tRNA synthetase and valyl-specific tRNAs from Escherichia coli. Biochem Biophys Res Commun 37:393-398.
    • (1969) Biochem Biophys Res Commun , vol.37 , pp. 393-398
    • Hélène, C.1    Brun, F.2    Yaniv, M.3
  • 11
    • 0026021698 scopus 로고
    • Chemical modification and NMR studies on a mushroom lectin Ischnoderma resinosun agglutinin (IRA)
    • Kawagishi H, Mori H. 1991. Chemical modification and NMR studies on a mushroom lectin Ischnoderma resinosun agglutinin (IRA). Biochim Biophys Acta 1076:179-186.
    • (1991) Biochim Biophys Acta , vol.1076 , pp. 179-186
    • Kawagishi, H.1    Mori, H.2
  • 12
    • 0028116179 scopus 로고
    • A stable isotope-aided NMR study of the active site of an endoglucanase from a strain of Bacillus
    • Kawarminami S, Ozaki K, Sumitomo N, Hayashi Y, Ito S, Shimada I, Arata Y. 1994. A stable isotope-aided NMR study of the active site of an endoglucanase from a strain of Bacillus. J Biol Chem 269:28752-28756.
    • (1994) J Biol Chem , vol.269 , pp. 28752-28756
    • Kawarminami, S.1    Ozaki, K.2    Sumitomo, N.3    Hayashi, Y.4    Ito, S.5    Shimada, I.6    Arata, Y.7
  • 13
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay LE, Keifer P, Saarinen T. 1992. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114:10663-10665.
    • (1992) J Am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 14
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallog 24:946-950.
    • (1991) J Appl Crystallog , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 15
    • 0024962351 scopus 로고
    • Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
    • Kraulis PJ, Clore GM, Nilges M, Jones TA, Petterson G, Knowles J, Gronenborn AM. 1989. Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry 28:7241-7257.
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, P.J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Petterson, G.5    Knowles, J.6    Gronenborn, A.M.7
  • 16
    • 0000272446 scopus 로고
    • Intrinsic fluorescence of proteins
    • Cundall RB, Dale RE, eds. Time-resolved fluorescence spectroscopy in biochemistry and biology
    • Longworth JW. 1983. Intrinsic fluorescence of proteins. In: Cundall RB, Dale RE, eds. Time-resolved fluorescence spectroscopy in biochemistry and biology. NATO Advanced Science Institute Series, Series A. Life Sciences Vol 69 pp 651-725.
    • (1983) NATO Advanced Science Institute Series, Series A. Life Sciences , vol.69 , pp. 651-725
    • Longworth, J.W.1
  • 18
    • 0040835880 scopus 로고
    • Identification of two tryptophan residues in endoglucanase III from Trichoderma reesei essential for cellulose binding and catalytic activity
    • Saddler JN, Penner MH, eds. Enzymatic degradation of insoluble carbohydrates. Washington, DC: American Chemical Society
    • Macarron R, Henrissat B, Van Beeuman J, Dominguez JM, Claeyssens M. 1995. Identification of two tryptophan residues in endoglucanase III from Trichoderma reesei essential for cellulose binding and catalytic activity. In: Saddler JN, Penner MH, eds. Enzymatic degradation of insoluble carbohydrates. ACS Symposium Series No. 618. Washington, DC: American Chemical Society. pp 164-173.
    • (1995) ACS Symposium Series No. 618 , pp. 164-173
    • Macarron, R.1    Henrissat, B.2    Van Beeuman, J.3    Dominguez, J.M.4    Claeyssens, M.5
  • 19
    • 0017098299 scopus 로고
    • 1-acetoxytryptophan-62 in the oxidation of tryptophan-62 of hen egg-white lysozyme by N-bromosuccinimide in acetate buffer
    • 1-acetoxytryptophan-62 in the oxidation of tryptophan-62 of hen egg-white lysozyme by N-bromosuccinimide in acetate buffer. Biochemistry 15:3438-3445.
    • (1976) Biochemistry , vol.15 , pp. 3438-3445
    • Norton, R.S.1    Allerhand, A.2
  • 20
    • 0026011001 scopus 로고
    • Enzyme immobilization using a cellulose-binding domain: Properties of a β-glucosidase fusion protein
    • Ong E, Gilkes NR, Miller RC Jr, Warren RAJ, Kilburn DG. 1991. Enzyme immobilization using a cellulose-binding domain: Properties of a β-glucosidase fusion protein. Enzyme Microb Technol 13:59-65.
    • (1991) Enzyme Microb Technol , vol.13 , pp. 59-65
    • Ong, E.1    Gilkes, N.R.2    Miller Jr., R.C.3    Warren, R.A.J.4    Kilburn, D.G.5
  • 21
    • 0027909736 scopus 로고
    • Ccx) domain of an exoglucanase from Cellulomonas fimi: Production in Escherichia coli and characterization of the polypeptide
    • Ccx) domain of an exoglucanase from Cellulomonas fimi: Production in Escherichia coli and characterization of the polypeptide. Bio-Tech Bioeng 42:401-409.
    • (1993) BioTech Bioeng , vol.42 , pp. 401-409
    • Ong, E.1    Gilkes, N.R.2    Miller Jr., R.C.3    Warren, R.A.J.4    Kilburn, D.G.5
  • 22
    • 0024355972 scopus 로고
    • Enzyme immobilization using the cellulose-binding domain of a Cellulomonas fimi exoglucanase
    • Ong E, Gilkes NR, Warren RAJ, Miller RC Jr, Kilburn DG. 1989. Enzyme immobilization using the cellulose-binding domain of a Cellulomonas fimi exoglucanase. Bio/Technology 7:604-607.
    • (1989) Bio/Technology , vol.7 , pp. 604-607
    • Ong, E.1    Gilkes, N.R.2    Warren, R.A.J.3    Miller Jr., R.C.4    Kilburn, D.G.5
  • 23
    • 0011984733 scopus 로고
    • The use of N-bromosuccinimide and N-bromoacetamide for the selective cleavage of c-tryptophyl peptide bonds in model peptides and glucagon
    • Patchornik A, Lawson WB, Gross EP, Witkop B. 1960. The use of N-bromosuccinimide and N-bromoacetamide for the selective cleavage of c-tryptophyl peptide bonds in model peptides and glucagon. J Am Chem Soc 82:5923-5926.
    • (1960) J Am Chem Soc , vol.82 , pp. 5923-5926
    • Patchornik, A.1    Lawson, W.B.2    Gross, E.P.3    Witkop, B.4
  • 24
    • 0027386771 scopus 로고
    • The role of conserved tryptophan residues in the interaction of a bacterial cellulose binding domain with its ligand
    • Poole DB, Hazlewood GP, Huskisson NS, Virden R, Gilbert HJ. 1993. The role of conserved tryptophan residues in the interaction of a bacterial cellulose binding domain with its ligand. FEMS Microbiol Lett 106:77-84.
    • (1993) FEMS Microbiol Lett , vol.106 , pp. 77-84
    • Poole, D.B.1    Hazlewood, G.P.2    Huskisson, N.S.3    Virden, R.4    Gilbert, H.J.5
  • 26
    • 0027941934 scopus 로고
    • Proton NMR studies of the structural and dynamical effect of chemical modification of a single aromatic side-chain in a snake cardiotoxin
    • Roumestand C, Gilquin B, Trémeau O, Gatineau E, Mouawad L, Méney A, Toma F. 1994. Proton NMR studies of the structural and dynamical effect of chemical modification of a single aromatic side-chain in a snake cardiotoxin. J Mol Biol 243:719-735.
    • (1994) J Mol Biol , vol.243 , pp. 719-735
    • Roumestand, C.1    Gilquin, B.2    Trémeau, O.3    Gatineau, E.4    Mouawad, L.5    Méney, A.6    Toma, F.7
  • 28
    • 77956994950 scopus 로고
    • Determination of the tryptophan content of proteins with N-bromosuccinimide
    • Spande TF, Witkop B. 1967. Determination of the tryptophan content of proteins with N-bromosuccinimide. Methods Enzymol 11:498-506.
    • (1967) Methods Enzymol , vol.11 , pp. 498-506
    • Spande, T.F.1    Witkop, B.2
  • 29
    • 0003010122 scopus 로고
    • Influence of acarbose and maltose on the reactivity of individual tryptophanyl residues in glucoamylase from Aspergillus niger
    • Svensson B, Clarke AJ, Svendsen I. 1986. Influence of acarbose and maltose on the reactivity of individual tryptophanyl residues in glucoamylase from Aspergillus niger. Carlsberg Res Commun 51:61-73.
    • (1986) Carlsberg Res Commun , vol.51 , pp. 61-73
    • Svensson, B.1    Clarke, A.J.2    Svendsen, I.3
  • 30
    • 0001594653 scopus 로고
    • Cellulose-binding domains: Classification and properties
    • Saddler JN, Penner MH, eds. Enzymatic degradation of insoluble carbohydrates. Washington, DC: American Chemical Society
    • Tomme P, Warren RAJ, Miller RC Jr, Gilkes NR. 1995. Cellulose-binding domains: Classification and properties. In: Saddler JN, Penner MH, eds. Enzymatic degradation of insoluble carbohydrates. ACS Symposium Series No. 618. Washington, DC: American Chemical Society. pp 142-163.
    • (1995) ACS Symposium Series No. 618 , vol.618 , pp. 142-163
    • Tomme, P.1    Warren, R.A.J.2    Miller Jr., R.C.3    Gilkes, N.R.4
  • 31
    • 12944260514 scopus 로고
    • Atomic features of protein-carbohydrate interactions
    • Vyas NK. 1991. Atomic features of protein-carbohydrate interactions Curr Opinion Struct Biol 1:732-740.
    • (1991) Curr Opinion Struct Biol , vol.1 , pp. 732-740
    • Vyas, N.K.1
  • 32
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart DS, Sykes BD, Richards FM. 1991. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 222:311-333.
    • (1991) J Mol Biol , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 34
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domains of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domains of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR 4:845-858.
    • (1994) J Biomol NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.