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Volumn 365, Issue 2, 2007, Pages 165-173

Determination of steady-state kinetic parameters for a xylanase-catalyzed hydrolysis of neutral underivatized xylooligosaccharides by mass spectrometry

Author keywords

Electrospray ionization mass spectrometry; Enzyme kinetics; Substrate specificity; Xylanase; Xylooligosaccharide

Indexed keywords

CATALYSIS; ELECTROSPRAY IONIZATION; ENZYME KINETICS; HYDROLYSIS; KINETIC PARAMETERS; MASS SPECTROMETERS; OLIGOSACCHARIDES; SUBSTRATES;

EID: 34247889870     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.03.034     Document Type: Article
Times cited : (7)

References (51)
  • 1
    • 12444323074 scopus 로고    scopus 로고
    • Mass spectrometric approaches for the dynamic processes in the condensed phase
    • Fabris D. Mass spectrometric approaches for the dynamic processes in the condensed phase. Mass Spectrom. Rev. 24 (2005) 30-54
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 30-54
    • Fabris, D.1
  • 2
    • 0024438708 scopus 로고
    • Electrospray ionization mass spectrometry for large biomolecules
    • Fenn J.B., Mann M., Meng C.K., Wong S.F., and Whitehouse G.M. Electrospray ionization mass spectrometry for large biomolecules. Science 246 (1989) 64-70
    • (1989) Science , vol.246 , pp. 64-70
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, G.M.5
  • 3
    • 33845183392 scopus 로고
    • Real-time reaction monitoring by continuous introduction ion-spray tandem mass spectrometry
    • Lee E.D., Mück W., Henion J.D., and Covey T.R. Real-time reaction monitoring by continuous introduction ion-spray tandem mass spectrometry. J. Am. Chem. Soc. 111 (1989) 4600-4604
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 4600-4604
    • Lee, E.D.1    Mück, W.2    Henion, J.D.3    Covey, T.R.4
  • 4
    • 0029083577 scopus 로고
    • Kinetic monitoring of enzymatic reactions in real time by quantitative high-performance liquid chromatography-mass spectrometry
    • Hsieh F.Y.L., Tong X., Wachs T., Ganem B., and Henion J.D. Kinetic monitoring of enzymatic reactions in real time by quantitative high-performance liquid chromatography-mass spectrometry. Anal. Biochem. 229 (1995) 20-25
    • (1995) Anal. Biochem. , vol.229 , pp. 20-25
    • Hsieh, F.Y.L.1    Tong, X.2    Wachs, T.3    Ganem, B.4    Henion, J.D.5
  • 5
    • 0034644390 scopus 로고    scopus 로고
    • Steady-state kinetics of ricin A-chain reaction with the sarcin-ricin loop and with HIV-1 Ψ-RNA hairpins evaluated by direct infusion electrospray ionization mass spectrometry
    • Fabris D.J. Steady-state kinetics of ricin A-chain reaction with the sarcin-ricin loop and with HIV-1 Ψ-RNA hairpins evaluated by direct infusion electrospray ionization mass spectrometry. J. Am. Chem. Soc. 122 (2000) 8779-8780
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8779-8780
    • Fabris, D.J.1
  • 7
    • 0343071628 scopus 로고
    • Observation of noncovalent enzyme-substrate and enzyme-product complexes by ion-spray mass spectrometry
    • Ganem B., Li Y.-T., and Henion J.D. Observation of noncovalent enzyme-substrate and enzyme-product complexes by ion-spray mass spectrometry. J. Am. Chem. Soc. 113 (1991) 7818-7819
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7818-7819
    • Ganem, B.1    Li, Y.-T.2    Henion, J.D.3
  • 8
    • 18144368508 scopus 로고    scopus 로고
    • Kinetic measurements and mechanism determination of Stf0 sulfotransferase using mass spectrometry
    • Pi N., Hoang M.B., Gao H., Mougous J.D., Bertozzi C.R., and Leary J.A. Kinetic measurements and mechanism determination of Stf0 sulfotransferase using mass spectrometry. Anal. Biochem. 341 (2005) 94-104
    • (2005) Anal. Biochem. , vol.341 , pp. 94-104
    • Pi, N.1    Hoang, M.B.2    Gao, H.3    Mougous, J.D.4    Bertozzi, C.R.5    Leary, J.A.6
  • 9
    • 0030979205 scopus 로고    scopus 로고
    • Beyond enzyme kinetics: Direct determination of mechanisms by stopped-flow mass spectrometry
    • Northropp D.B., and Simpson F.B. Beyond enzyme kinetics: Direct determination of mechanisms by stopped-flow mass spectrometry. Bioorg. Med. Chem. 5 (1997) 641-644
    • (1997) Bioorg. Med. Chem. , vol.5 , pp. 641-644
    • Northropp, D.B.1    Simpson, F.B.2
  • 10
    • 0034115994 scopus 로고    scopus 로고
    • Stopped-flow-electrospray ionization mass spectrometry: A new method for studying chemical reaction kinetics in solution
    • Kolakowski B.M., Simmons D.A., and Konermann L. Stopped-flow-electrospray ionization mass spectrometry: A new method for studying chemical reaction kinetics in solution. Rapid Commun. Mass Spectrom. 14 (2000) 772-776
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 772-776
    • Kolakowski, B.M.1    Simmons, D.A.2    Konermann, L.3
  • 11
    • 0032568560 scopus 로고    scopus 로고
    • Pre-steady state kinetic analysis of an enzymatic reaction monitored by time-resolved electrospray ionization mass spectrometry
    • Zechel D.L., Konermann L., Withers S.G., and Douglass D.J. Pre-steady state kinetic analysis of an enzymatic reaction monitored by time-resolved electrospray ionization mass spectrometry. Biochemistry 37 (1998) 7664-7669
    • (1998) Biochemistry , vol.37 , pp. 7664-7669
    • Zechel, D.L.1    Konermann, L.2    Withers, S.G.3    Douglass, D.J.4
  • 12
    • 2342452560 scopus 로고    scopus 로고
    • Mechanistic studies on enzymatic reactions by electrospray ionization MS using a capillary mixer with adjustable reaction chamber volume for time-resolved measurements
    • Wilson D.J., and Konermann L. Mechanistic studies on enzymatic reactions by electrospray ionization MS using a capillary mixer with adjustable reaction chamber volume for time-resolved measurements. Anal. Chem. 76 (2004) 2537-2543
    • (2004) Anal. Chem. , vol.76 , pp. 2537-2543
    • Wilson, D.J.1    Konermann, L.2
  • 13
    • 22144444949 scopus 로고    scopus 로고
    • Probing the role of tightly bound phosphoenolpyruvate in Escherichia coli 3-deoxy-d-manno-octulosonate 8-phosphate synthase catalysis using quantitative time-resolved electrospray ionization mass spectrometry in the millisecond time range
    • Li Z., Sau A., Furdui C.M., and Anderson K.S. Probing the role of tightly bound phosphoenolpyruvate in Escherichia coli 3-deoxy-d-manno-octulosonate 8-phosphate synthase catalysis using quantitative time-resolved electrospray ionization mass spectrometry in the millisecond time range. Anal. Biochem. 343 (2005) 35-47
    • (2005) Anal. Biochem. , vol.343 , pp. 35-47
    • Li, Z.1    Sau, A.2    Furdui, C.M.3    Anderson, K.S.4
  • 14
    • 0042021429 scopus 로고    scopus 로고
    • A snapshot of enzyme catalysis using electrospray ionization mass spectrometry
    • Li Z., Sau A.K., Shen S., Whitehouse C., Baasov T., and Anderson K.S. A snapshot of enzyme catalysis using electrospray ionization mass spectrometry. J. Am. Chem. Soc. 125 (2003) 9938-9939
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9938-9939
    • Li, Z.1    Sau, A.K.2    Shen, S.3    Whitehouse, C.4    Baasov, T.5    Anderson, K.S.6
  • 15
    • 0030659720 scopus 로고    scopus 로고
    • Detection and identification of transient enzyme intermediates using rapid mixing, pulsed-flow electrospray mass spectrometry
    • Paiva A.A., Tilton Jr. R.F., Crooks G.P., Huang L.Q., and Anderson K.S. Detection and identification of transient enzyme intermediates using rapid mixing, pulsed-flow electrospray mass spectrometry. Biochemistry 36 (1997) 15472-15476
    • (1997) Biochemistry , vol.36 , pp. 15472-15476
    • Paiva, A.A.1    Tilton Jr., R.F.2    Crooks, G.P.3    Huang, L.Q.4    Anderson, K.S.5
  • 16
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg white lysozyme proceeds via a covalent intermediate
    • Vocadlo D.J., Davies G.J., Laine R., and Withers S.G. Catalysis by hen egg white lysozyme proceeds via a covalent intermediate. Nature 412 (2001) 835-838
    • (2001) Nature , vol.412 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 17
    • 0037027321 scopus 로고    scopus 로고
    • Kinetic analysis of NodST sulfotransferase using an electrospray ionization mass spectrometry assay
    • Pi N., Armstrong J.I., Bertozzi C.R., and Leary J.A. Kinetic analysis of NodST sulfotransferase using an electrospray ionization mass spectrometry assay. Biochemistry 41 (2002) 13283-13288
    • (2002) Biochemistry , vol.41 , pp. 13283-13288
    • Pi, N.1    Armstrong, J.I.2    Bertozzi, C.R.3    Leary, J.A.4
  • 18
    • 0842310465 scopus 로고    scopus 로고
    • Determination of enzyme/substrate specificity constants using a multiple substrate ESI-MS assay
    • Pi N., and Leary J.A. Determination of enzyme/substrate specificity constants using a multiple substrate ESI-MS assay. J. Am. Soc. Mass Spectrom. 15 (2004) 233-243
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 233-243
    • Pi, N.1    Leary, J.A.2
  • 19
    • 1842611596 scopus 로고    scopus 로고
    • Observation of a hybrid random ping-pong mechanism of catalysis for NodST: A mass spectrometry approach
    • Pi N., Yu Y., Mougous J.D., and Leary J.A. Observation of a hybrid random ping-pong mechanism of catalysis for NodST: A mass spectrometry approach. Protein Sci. 13 (2004) 903-912
    • (2004) Protein Sci. , vol.13 , pp. 903-912
    • Pi, N.1    Yu, Y.2    Mougous, J.D.3    Leary, J.A.4
  • 20
    • 2542498098 scopus 로고    scopus 로고
    • Kinetic measurements of phosphoglucomutase by direct analysis of glucose-1-phosphate and glucose-6-phosphate using ion/molecule reactions and Fourier transform ion cyclotron resonance mass spectrometry
    • Gao H., and Leary J.A. Kinetic measurements of phosphoglucomutase by direct analysis of glucose-1-phosphate and glucose-6-phosphate using ion/molecule reactions and Fourier transform ion cyclotron resonance mass spectrometry. Anal. Biochem. 329 (2004) 269-275
    • (2004) Anal. Biochem. , vol.329 , pp. 269-275
    • Gao, H.1    Leary, J.A.2
  • 21
    • 11844301222 scopus 로고    scopus 로고
    • Kinetic measurements of phosphoglucose isomerase and phosphomannose isomerase by direct analysis of phosphorylated aldose-ketose isomers using tandem mass spectrometry
    • Gao H., Chen Y., and Leary J.A. Kinetic measurements of phosphoglucose isomerase and phosphomannose isomerase by direct analysis of phosphorylated aldose-ketose isomers using tandem mass spectrometry. Intl. J. Mass Spectrom. Ion Proc. 240 (2005) 291-299
    • (2005) Intl. J. Mass Spectrom. Ion Proc. , vol.240 , pp. 291-299
    • Gao, H.1    Chen, Y.2    Leary, J.A.3
  • 22
    • 1642353442 scopus 로고    scopus 로고
    • Kinetic and substrate binding analysis of phosphorylase β via electrospray ionization mass spectrometry: A model for chemical proteomics of sugar phosphorylases
    • Zea C.J., and Pohl N.L. Kinetic and substrate binding analysis of phosphorylase β via electrospray ionization mass spectrometry: A model for chemical proteomics of sugar phosphorylases. Anal. Biochem. 327 (2004) 107-113
    • (2004) Anal. Biochem. , vol.327 , pp. 107-113
    • Zea, C.J.1    Pohl, N.L.2
  • 23
    • 0035799359 scopus 로고    scopus 로고
    • Analysis of enzyme kinetics using electrospray ionization mass spectrometry and multiple reaction monitoring: Fucosyltransferase
    • Norris A.J., Whitelegge J.P., Faull K.F., and Toyokuni T. Analysis of enzyme kinetics using electrospray ionization mass spectrometry and multiple reaction monitoring: Fucosyltransferase. Biochemistry 40 (2001) 3774-3779
    • (2001) Biochemistry , vol.40 , pp. 3774-3779
    • Norris, A.J.1    Whitelegge, J.P.2    Faull, K.F.3    Toyokuni, T.4
  • 24
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families, and extromephilic xylanases
    • Collins T., Gerday C., and Feller G. Xylanases, xylanase families, and extromephilic xylanases. FEMS Microb. Rev. 29 (2005) 3-23
    • (2005) FEMS Microb. Rev. , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 25
    • 0029937320 scopus 로고    scopus 로고
    • Biochemistry and genetics of microbial xylanases
    • Jeffries T.W. Biochemistry and genetics of microbial xylanases. Curr. Opin. Biotechnol. 7 (1996) 337-342
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 337-342
    • Jeffries, T.W.1
  • 26
    • 0030830456 scopus 로고    scopus 로고
    • Mechanism of catalysis by retaining β-glycosidases
    • White A., and Rose D.R. Mechanism of catalysis by retaining β-glycosidases. Curr. Opin. Struct. Biol. 7 (1997) 645-651
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 645-651
    • White, A.1    Rose, D.R.2
  • 27
    • 0028338985 scopus 로고
    • Crystallographic studies on endo-1,4-β-xylanase II from Trichoderma reesei: Two conformational states in the active site
    • Törrönen A., Harkki A., and Rouvinen J. Crystallographic studies on endo-1,4-β-xylanase II from Trichoderma reesei: Two conformational states in the active site. EMBO J. 13 (1994) 2493-2501
    • (1994) EMBO J. , vol.13 , pp. 2493-2501
    • Törrönen, A.1    Harkki, A.2    Rouvinen, J.3
  • 28
    • 0028911057 scopus 로고
    • Structural comparison of two major endo-1,4-β-xylanases from Trichoderma reesei
    • Törrönen A., and Rouvinen J. Structural comparison of two major endo-1,4-β-xylanases from Trichoderma reesei. Biochemistry 34 (1995) 847-856
    • (1995) Biochemistry , vol.34 , pp. 847-856
    • Törrönen, A.1    Rouvinen, J.2
  • 29
    • 0029739757 scopus 로고    scopus 로고
    • Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-xylanase II from Trichoderma reesei
    • Havukainen R., Törrönen A., Laitinen T., and Rouvinen J. Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-xylanase II from Trichoderma reesei. Biochemistry 35 (1996) 9617-9624
    • (1996) Biochemistry , vol.35 , pp. 9617-9624
    • Havukainen, R.1    Törrönen, A.2    Laitinen, T.3    Rouvinen, J.4
  • 30
    • 0040003315 scopus 로고    scopus 로고
    • Structural and functional properties of low molecular weight endo-1,4-β-xylanases
    • Törrönen A., and Rouvinen J. Structural and functional properties of low molecular weight endo-1,4-β-xylanases. J. Biotechnol. 75 (1997) 137-149
    • (1997) J. Biotechnol. , vol.75 , pp. 137-149
    • Törrönen, A.1    Rouvinen, J.2
  • 31
    • 3242663327 scopus 로고    scopus 로고
    • Characterization of mutant xylanases using Fourier transform ion cyclotron resonance mass spectrometry: Stabilizing contributions of disulfide bridges and N-terminal extensions
    • Jänis J., Turunen O., Leisola M., Derrick P.J., Rouvinen J., and Vainiotalo P. Characterization of mutant xylanases using Fourier transform ion cyclotron resonance mass spectrometry: Stabilizing contributions of disulfide bridges and N-terminal extensions. Biochemistry 43 (2004) 9556-9566
    • (2004) Biochemistry , vol.43 , pp. 9556-9566
    • Jänis, J.1    Turunen, O.2    Leisola, M.3    Derrick, P.J.4    Rouvinen, J.5    Vainiotalo, P.6
  • 32
    • 34247843067 scopus 로고    scopus 로고
    • S. Uotila, A. Hassinen, G. Joucla, K. Visuri, Solubility studies on the crystals of xylanase pI 9, in: Proceedings of the Recent Advances in Macromolecular Crystallization, 1999, San Diego, pp. 21-22.
  • 33
    • 0000060598 scopus 로고    scopus 로고
    • Monitoring reaction kinetics in solution by continuous-flow methods: The effects of convection and molecular diffusion under laminar flow conditions
    • Konermann L. Monitoring reaction kinetics in solution by continuous-flow methods: The effects of convection and molecular diffusion under laminar flow conditions. J. Phys. Chem. A 103 (1999) 7210-7216
    • (1999) J. Phys. Chem. A , vol.103 , pp. 7210-7216
    • Konermann, L.1
  • 34
    • 0035500232 scopus 로고    scopus 로고
    • A strategy for the determination of enzyme kinetics using electrospray ionization with an ion trap mass spectrometer
    • Ge X., Sirich T.L., Beyer M.K., Desaire H., and Leary J.A. A strategy for the determination of enzyme kinetics using electrospray ionization with an ion trap mass spectrometer. Anal. Chem. 73 (2001) 5078-5082
    • (2001) Anal. Chem. , vol.73 , pp. 5078-5082
    • Ge, X.1    Sirich, T.L.2    Beyer, M.K.3    Desaire, H.4    Leary, J.A.5
  • 35
    • 2942594230 scopus 로고    scopus 로고
    • Engineering the thermostability of Trichoderma reesei endo-1,4-β-xylanase II by combination of disulphide bridges
    • Xiong H., Fenel F., Leisola M., and Turunen O. Engineering the thermostability of Trichoderma reesei endo-1,4-β-xylanase II by combination of disulphide bridges. Extremophiles 8 (2004) 393-400
    • (2004) Extremophiles , vol.8 , pp. 393-400
    • Xiong, H.1    Fenel, F.2    Leisola, M.3    Turunen, O.4
  • 36
    • 0035916376 scopus 로고    scopus 로고
    • Simultaneous catalysis and product separation by cross-linked enzyme crystals
    • Leisola M., Jokela J., Finell J., and Pastinen O. Simultaneous catalysis and product separation by cross-linked enzyme crystals. Biotechnol. Bioeng. 72 (2001) 501-505
    • (2001) Biotechnol. Bioeng. , vol.72 , pp. 501-505
    • Leisola, M.1    Jokela, J.2    Finell, J.3    Pastinen, O.4
  • 37
    • 0027536224 scopus 로고
    • Mode of action of three endo-β-1,4-xylanases of Streptomyces lividans
    • Biely P., Kluepfel D., Morosoli R., and Shareck F. Mode of action of three endo-β-1,4-xylanases of Streptomyces lividans. Biochim. Biophys. Acta. 1162 (1993) 246-254
    • (1993) Biochim. Biophys. Acta. , vol.1162 , pp. 246-254
    • Biely, P.1    Kluepfel, D.2    Morosoli, R.3    Shareck, F.4
  • 38
    • 0026540828 scopus 로고
    • Action pattern of xylo-oligosaccharide hydrolysis by Schizophyllum commune xylanase A
    • Bray M.R., and Clarke A.J. Action pattern of xylo-oligosaccharide hydrolysis by Schizophyllum commune xylanase A. Eur. J. Biochem. 204 (1992) 191-196
    • (1992) Eur. J. Biochem. , vol.204 , pp. 191-196
    • Bray, M.R.1    Clarke, A.J.2
  • 39
    • 0028332196 scopus 로고
    • Enzymatic specificities and modes of action of the two catalytic domains of the XynC xylanase from Fibrobacter succinogenes S85
    • Zhu H., Paradis F.W., Krell P.J., Phillips J.P., and Forsberg C.W. Enzymatic specificities and modes of action of the two catalytic domains of the XynC xylanase from Fibrobacter succinogenes S85. J. Bacteriol. 176 (1994) 3885-3894
    • (1994) J. Bacteriol. , vol.176 , pp. 3885-3894
    • Zhu, H.1    Paradis, F.W.2    Krell, P.J.3    Phillips, J.P.4    Forsberg, C.W.5
  • 40
    • 0001307590 scopus 로고
    • Xylanase of Bacillus pumilus
    • Okada H., and Shinmyo A. Xylanase of Bacillus pumilus. Methods Enzymol. 160 (1988) 632-637
    • (1988) Methods Enzymol. , vol.160 , pp. 632-637
    • Okada, H.1    Shinmyo, A.2
  • 42
    • 0031028023 scopus 로고    scopus 로고
    • The β-d-xylosidase of Trichoderma reesei is a multifunctional β-d-xylan xylohydrolase
    • Herrmann M.C., Vršanska M., Jurickova M., Hirsch J., Biely P., and Kubicek C.P. The β-d-xylosidase of Trichoderma reesei is a multifunctional β-d-xylan xylohydrolase. Biochem. J. 321 (1997) 375-381
    • (1997) Biochem. J. , vol.321 , pp. 375-381
    • Herrmann, M.C.1    Vršanska, M.2    Jurickova, M.3    Hirsch, J.4    Biely, P.5    Kubicek, C.P.6
  • 43
    • 0036092233 scopus 로고    scopus 로고
    • Total hydrolysis of xylotetraose and xylobiose by soluble and cross-linked crystalline xylanase II from Trichoderma reesei
    • Finell J., Jokela J., Leisola M., and Riekkola M.-L. Total hydrolysis of xylotetraose and xylobiose by soluble and cross-linked crystalline xylanase II from Trichoderma reesei. Biocatal. Biotranform. 20 (2002) 281-290
    • (2002) Biocatal. Biotranform. , vol.20 , pp. 281-290
    • Finell, J.1    Jokela, J.2    Leisola, M.3    Riekkola, M.-L.4
  • 44
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies G.J., Wilson K.S., and Henrissat B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J. 321 (1997) 557-559
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 46
    • 0028211360 scopus 로고
    • Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase
    • Wakarchuk W.W., Campbell R.L., Sung W.L., Davoodi J., and Yaguchi M. Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase. Protein Sci. 3 (1994) 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
  • 47
    • 0028072135 scopus 로고
    • Stereochemistry of the hydrolysis of glycosidic linkage by endo-β-1,4-xylanases of Trichoderma reesei
    • Biely P., Kremnicky L., Alföldi J., and Tenkanen M. Stereochemistry of the hydrolysis of glycosidic linkage by endo-β-1,4-xylanases of Trichoderma reesei. FEBS Lett. 356 (1994) 137-140
    • (1994) FEBS Lett. , vol.356 , pp. 137-140
    • Biely, P.1    Kremnicky, L.2    Alföldi, J.3    Tenkanen, M.4
  • 51
    • 0035954371 scopus 로고    scopus 로고
    • Influence of the aglycone region of the substrate binding cleft of Pseudomonas xylanase 10A on catalysis
    • Armand S., Andrews S.R., Charnock S.J., and Gilbert H.J. Influence of the aglycone region of the substrate binding cleft of Pseudomonas xylanase 10A on catalysis. Biochemistry 40 (2001) 7404-7409
    • (2001) Biochemistry , vol.40 , pp. 7404-7409
    • Armand, S.1    Andrews, S.R.2    Charnock, S.J.3    Gilbert, H.J.4


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