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Volumn 50, Issue 25, 2011, Pages 5693-5703

Mutational effects on transglycosylating activity of family 18 chitinases and construction of a hypertransglycosylating mutant

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC RESIDUES; CATALYTIC CYCLES; CHITINASES; MUTATIONAL EFFECTS; NATURAL SUBSTRATES; SERRATIA MARCESCENS; SITE DIRECTED MUTAGENESIS; SUBSITES; SUGAR ACCEPTORS; TRANS GLYCOSYLATION ACTIVITY; TRANSGLYCOSYLATION;

EID: 79959457508     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2002532     Document Type: Article
Times cited : (81)

References (64)
  • 1
    • 63849127101 scopus 로고    scopus 로고
    • Prebiotic oligosaccharides change the concentrations of short-chain fatty acids and the microbial population of mouse bowel
    • Pan, X. D., Chen, F. Q., Wu, T. X., Tang, H. G., and Zhao, Z. Y. (2009) Prebiotic oligosaccharides change the concentrations of short-chain fatty acids and the microbial population of mouse bowel J. Zhejiang Univ. Sci. B10, 258-263
    • (2009) J. Zhejiang Univ. Sci. , vol.10 , pp. 258-263
    • Pan, X.D.1    Chen, F.Q.2    Wu, T.X.3    Tang, H.G.4    Zhao, Z.Y.5
  • 2
    • 0036982053 scopus 로고    scopus 로고
    • Chitosan oligosaccharides, dp 2-8, have prebiotic effect on the Bifidobacterium bifidium and Lactobacillus sp
    • Lee, H. W., Park, Y. S., Jung, J. S., and Shin, W. S. (2002) Chitosan oligosaccharides, dp 2-8, have prebiotic effect on the Bifidobacterium bifidium and Lactobacillus sp Anaerobe 8, 319-324
    • (2002) Anaerobe , vol.8 , pp. 319-324
    • Lee, H.W.1    Park, Y.S.2    Jung, J.S.3    Shin, W.S.4
  • 3
    • 0000568294 scopus 로고
    • Effects of chitosan, pectic acid, lysozyme, and Chitinase on the growth of several phytopathogens
    • Hirano, S. and Nagao, N. (1989) Effects of chitosan, pectic acid, lysozyme, and Chitinase on the growth of several phytopathogens Agric. Biol. Chem. 53, 3065-3066
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 3065-3066
    • Hirano, S.1    Nagao, N.2
  • 4
    • 2942668626 scopus 로고    scopus 로고
    • Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation
    • DOI 10.1126/science.1095336
    • Zhu, Z., Zheng, T., Homer, R. J., Kim, Y. K., Chen, N. Y., Cohn, L., Hamid, Q., and Elias, J. A. (2004) Acidic mammalian Chitinase in asthmatic Th2 Inflammation and IL-13 pathway activation Science 304, 1678-1682 (Pubitemid 38765861)
    • (2004) Science , vol.304 , Issue.5677 , pp. 1678-1682
    • Zhu, Z.1    Zheng, T.2    Homer, R.J.3    Kim, Y.-K.4    Chen, N.Y.5    Cohn, L.6    Hamid, Q.7    Elias, J.A.8
  • 5
    • 68649097772 scopus 로고    scopus 로고
    • Inhibitory effects of chitooligosaccharides on tumor growth and metastasis
    • Shen, K.-T., Chen, M.-H., Chan, H.-Y., Jeng, J.-H., and Wang, Y.-J. (2009) Inhibitory effects of chitooligosaccharides on tumor growth and metastasis Food Chem. Toxicol. 47, 1864-1871
    • (2009) Food Chem. Toxicol. , vol.47 , pp. 1864-1871
    • Shen, K.-T.1    Chen, M.-H.2    Chan, H.-Y.3    Jeng, J.-H.4    Wang, Y.-J.5
  • 6
    • 33747846583 scopus 로고    scopus 로고
    • Chitin and chitosan: Properties and applications
    • DOI 10.1016/j.progpolymsci.2006.06.001, PII S0079670006000530
    • Rinaudo, M. (2006) Chitin and chitosan: Properties and applications Prog. Polym. Sci. 31, 603-632 (Pubitemid 44287019)
    • (2006) Progress in Polymer Science (Oxford) , vol.31 , Issue.7 , pp. 603-632
    • Rinaudo, M.1
  • 7
    • 13544269349 scopus 로고    scopus 로고
    • Depolymerized products of chitosan as potent inhibitors of tumor-induced angiogenesis
    • DOI 10.1016/j.bbagen.2004.11.009
    • Prashanth, K. V. H. and Tharanathan, R. N. (2005) Depolymerized products of chitosan as potent inhibitors of tumor-induced angiogenesis Biochim. Biophys. Acta 1722, 22-29 (Pubitemid 40222401)
    • (2005) Biochimica et Biophysica Acta - General Subjects , vol.1722 , Issue.1 , pp. 22-29
    • Harish, P.K.V.1    Tharanathan, R.N.2
  • 8
    • 4544301221 scopus 로고    scopus 로고
    • Acidic mammalian chitinase - A potential target for asthma therapy
    • DOI 10.1016/j.tips.2004.08.002, PII S0165614704002251
    • Donnelly, L. E. and Barnes, P. J. (2004) Acidic mammalian Chitinase-a potential target for asthma therapy Trends Pharmacol. Sci. 25, 509-511 (Pubitemid 39233562)
    • (2004) Trends in Pharmacological Sciences , vol.25 , Issue.10 , pp. 509-511
    • Donnelly, L.E.1    Barnes, P.J.2
  • 9
    • 0001007252 scopus 로고    scopus 로고
    • Comparison of the ability of partially n-acetylated chitosans and chitooligosaccharides to elicit resistance reactions in wheat leaves
    • Vander, P., Varum, K. M., Domard, A., El Gueddari, N. E., and Moerschbacher, B. M. (1998) Comparison of the ability of partially N-acetylated chitosans and chitooligosaccharides to elicit resistance reactions in wheat leaves Plant Physiol. 118, 1353-1359 (Pubitemid 128653069)
    • (1998) Plant Physiology , vol.118 , Issue.4 , pp. 1353-1359
    • Vander, P.1    Vaain, K.M.2    Domard, A.3    El Gueddari, N.E.4    Moerschbacher, B.M.5
  • 10
    • 0036343045 scopus 로고    scopus 로고
    • Elicitor activity of cerebroside, a sphingolipid elicitor, in cell suspension cultures of rice
    • Umemura, K., Ogawa, N., Koga, J., Iwata, M., and Usami, H. (2002) Elicitor activity of cerebroside, a sphingolipid elicitor, in cell suspension cultures of rice Plant Cell Physiol. 43, 778-784 (Pubitemid 34877892)
    • (2002) Plant and Cell Physiology , vol.43 , Issue.7 , pp. 778-784
    • Umemura, K.1    Ogawa, N.2    Koga, J.3    Iwata, M.4    Usami, H.5
  • 11
    • 58149142985 scopus 로고    scopus 로고
    • Partially acetylated chitosan oligo- and polymers induce an oxidative burst in suspension cultured cells of the gymnosperm Araucaria angustifolia
    • dos Santos, A. L. W., El Gueddari, N. E., Trombotto, S., and Moerschbacher, B. M. (2008) Partially acetylated chitosan oligo- and polymers induce an oxidative burst in suspension cultured cells of the gymnosperm Araucaria angustifolia Biomacromolecules 9, 3411-3415
    • (2008) Biomacromolecules , vol.9 , pp. 3411-3415
    • Dos Santos, A.L.W.1    El Gueddari, N.E.2    Trombotto, S.3    Moerschbacher, B.M.4
  • 12
    • 0024331914 scopus 로고
    • 1989) Transglycosylation and transfer-reaction activities of endo-alpha-N-acetyl-D-galactosaminidase from Diplococcus(Streptococcus) pneumoniae
    • Bardales, R. M. and Bhavanandan, V. P. (1989) 1989) Transglycosylation and transfer-reaction activities of endo-alpha-N-acetyl-D-galactosaminidase from Diplococcus(Streptococcus) pneumoniae J. Biol. Chem. 264, 3-19897
    • (1989) J. Biol. Chem. , vol.264 , pp. 3-19897
    • Bardales, R.M.1    Bhavanandan, V.P.2
  • 13
    • 0014408503 scopus 로고
    • Lysozyme-catalyzed hydrolysis and transglycosylation reactions of bacterial cell wall oligosaccharides
    • Chipman, D. M., Pollock, J. J., and Sharon, N. (1968) Lysozyme-catalyzed hydrolysis and transglycosylation reactions of bacterial cell wall oligosaccharides J. Biol. Chem. 243, 487-496
    • (1968) J. Biol. Chem. , vol.243 , pp. 487-496
    • Chipman, D.M.1    Pollock, J.J.2    Sharon, N.3
  • 14
    • 0031392412 scopus 로고    scopus 로고
    • Transglycosylation activity of α-D-galactosidase from Trichoderma reesei. An investigation of the active site
    • DOI 10.1016/S0008-6215(97)00229-2, PII S0008621597002292
    • Eneyskaya, E. V., Golubev, A. M., Kachurin, A. M., Savel'ev, A. N., and Neustroev, K. N. (1997) Transglycosylation activity of alpha-D-galactosidase from Trichoderma reesei-An investigation of the active site Carbohydr. Res. 305, 83-91 (Pubitemid 28252843)
    • (1997) Carbohydrate Research , vol.305 , Issue.1 , pp. 83-91
    • Eneyskaya, E.V.1    Golubev, A.M.2    Kachurin, A.M.3    Savel'ev, A.N.4    Neustroev, K.N.5
  • 15
    • 36849015794 scopus 로고    scopus 로고
    • Identification of the catalytic acid-base residue of arthrobacter endo-β-N-acetylglucosaminidase by chemical rescue of an inactive mutant
    • DOI 10.1093/jb/mvm124
    • Fujita, K., Sato, R., Toma, K., Kitahara, K., Suganuma, T., Yamamoto, K., and Takegawa, K. (2007) Identification of the catalytic acid-base residue of Arthrobacter endo-beta-N-acetylglucosaminidase by chemical rescue of an inactive mutant J. Biochem. 142, 301-306 (Pubitemid 350221832)
    • (2007) Journal of Biochemistry , vol.142 , Issue.3 , pp. 301-306
    • Fujita, K.1    Sato, R.2    Toma, K.3    Kitahara, K.4    Suganuma, T.5    Yamamoto, K.6    Takegawa, K.7
  • 16
    • 41949130819 scopus 로고    scopus 로고
    • Mutants of Mucor hiemalis Endo-β-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities
    • Umekawa, M., Huang, W., Li, B., Fujita, K., Ashida, H., Wang, L.-X., and Yamamoto, K. (2008) Mutants of Mucor hiemalis Endo-β-N- acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities J. Biol. Chem. 283, 4469-4479
    • (2008) J. Biol. Chem. , vol.283 , pp. 4469-4479
    • Umekawa, M.1    Huang, W.2    Li, B.3    Fujita, K.4    Ashida, H.5    Wang, L.-X.6    Yamamoto, K.7
  • 17
    • 0032882011 scopus 로고    scopus 로고
    • Mutagenesis of glycosidases
    • DOI 10.1146/annurev.biochem.68.1.487
    • Ly, H. D. and Withers, S. G. (1999) Mutagenesis of glycosidases Annu. Rev. Biochem. 68, 487-522 (Pubitemid 29449201)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 487-522
    • Ly, H.D.1    Withers, S.G.2
  • 18
    • 0034631781 scopus 로고    scopus 로고
    • Glycosyl fluorides in enzymatic reactions
    • DOI 10.1016/S0008-6215(00)00041-0, PII S0008621500000410
    • Williams, S. J. and Withers, S. G. (2000) Glycosyl fluorides in enzymatic reactions Carbohydr. Res. 327, 27-46 (Pubitemid 30624997)
    • (2000) Carbohydrate Research , vol.327 , Issue.1-2 , pp. 27-46
    • Williams, S.J.1    Withers, S.G.2
  • 20
    • 9744227158 scopus 로고    scopus 로고
    • Differential recognition of animal type β4-galactosylated and -fucosylated chito-oligosaccharides by two family 18 chitinases from Trichoderma harzianum
    • DOI 10.1093/glycob/cwh121
    • Boer, H., Munck, N., Natunen, J., Wohlfahrt, G., Söderlund, H., Renkonen, O., and Koivula, A. (2004) Differential recognition of animal type beta 4-galactosylated and alpha 3-fucosylated chito-oligosaccharides by two family 18 chitinases from Trichoderma harzianum Glycobiology 14, 1303-1313 (Pubitemid 39585363)
    • (2004) Glycobiology , vol.14 , Issue.12 , pp. 1303-1313
    • Boer, H.1    Munck, N.2    Natunen, J.3    Wohlfahrt, G.4    Soderlund, H.5    Renkonen, O.6    Koivula, A.7
  • 22
    • 0035957051 scopus 로고    scopus 로고
    • Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis
    • DOI 10.1021/bi001537s
    • Fukamizo, T., Sasaki, C., Schelp, E., Bortone, K., and Robertus, J. D. (2001) Kinetic properties of Chitinase-1 from the fungal pathogen Coccidioides immitis Biochemistry 40, 2448-2454 (Pubitemid 32171718)
    • (2001) Biochemistry , vol.40 , Issue.8 , pp. 2448-2454
    • Fukamizo, T.1    Sasaki, C.2    Schelp, E.3    Bortone, K.4    Robertus, J.D.5
  • 23
    • 76849112035 scopus 로고    scopus 로고
    • Transglycosylation reaction catalyzed by a class v Chitinase from cycad, Cycas revoluta: A study involving site-directed mutagenesis, HPLC, and real-time ESI-MS
    • Taira, T., Fujiwara, M., Dennhart, N., Hayashi, H., Onaga, S., Ohnuma, T., Letzel, T., Sakuda, S., and Fukamizo, T. (2010) Transglycosylation reaction catalyzed by a class V Chitinase from cycad, Cycas revoluta: A study involving site-directed mutagenesis, HPLC, and real-time ESI-MS Biochim. Biophys. Acta 1804, 668-675
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 668-675
    • Taira, T.1    Fujiwara, M.2    Dennhart, N.3    Hayashi, H.4    Onaga, S.5    Ohnuma, T.6    Letzel, T.7    Sakuda, S.8    Fukamizo, T.9
  • 25
    • 33846641660 scopus 로고    scopus 로고
    • Antifungal activity of oligochitosan against Phytophthora capsici and other plant pathogenic fungi in vitro
    • Xu, J. G., Zhao, X. M., Han, X. W., and Du, Y. G. (2007) Antifungal activity of oligochitosan against Phytophthora capsici and other plant pathogenic fungi in vitro Pestic. Biochem. Physiol. 87, 220-228
    • (2007) Pestic. Biochem. Physiol. , vol.87 , pp. 220-228
    • Xu, J.G.1    Zhao, X.M.2    Han, X.W.3    Du, Y.G.4
  • 26
    • 0035216323 scopus 로고    scopus 로고
    • Antimicrobial effect of chitooligosaccharides produced by bioreactor
    • Jeon, Y. J., Park, P. J., and Kim, S. K. (2001) Antimicrobial effect of chitooligosaccharides produced by bioreactor Carbohydr. Polym. 44, 71-76
    • (2001) Carbohydr. Polym. , vol.44 , pp. 71-76
    • Jeon, Y.J.1    Park, P.J.2    Kim, S.K.3
  • 27
    • 59349093746 scopus 로고    scopus 로고
    • Chitosan oligosaccharides attenuate hydrogen peroxide-induced stress injury in human umbilical vein endothelial cells
    • Liu, H. T., Li, W. M., Xu, G., Li, X. Y., Bai, X. F., Wei, P., Yu, C., and Du, Y. G. (2009) Chitosan oligosaccharides attenuate hydrogen peroxide-induced stress injury in human umbilical vein endothelial cells Pharmacol. Res. 59, 167-175
    • (2009) Pharmacol. Res. , vol.59 , pp. 167-175
    • Liu, H.T.1    Li, W.M.2    Xu, G.3    Li, X.Y.4    Bai, X.F.5    Wei, P.6    Yu, C.7    Du, Y.G.8
  • 28
    • 40849083691 scopus 로고    scopus 로고
    • Anti-angiogenic activities of chitooligosaccharides
    • Wu, H. G., Yao, Z., Bal, X. F., Du, Y. G., and Lin, B. C. (2008) Anti-angiogenic activities of chitooligosaccharides Carbohydr. Polym. 73, 105-110
    • (2008) Carbohydr. Polym. , vol.73 , pp. 105-110
    • Wu, H.G.1    Yao, Z.2    Bal, X.F.3    Du, Y.G.4    Lin, B.C.5
  • 29
    • 46649119277 scopus 로고    scopus 로고
    • Chitin oligosaccharides inhibit oxidative stress in live cells
    • Ngo, D. N., Kim, M. M., and Kim, S. K. (2008) Chitin oligosaccharides inhibit oxidative stress in live cells Carbohydr. Polym. 74, 228-234
    • (2008) Carbohydr. Polym. , vol.74 , pp. 228-234
    • Ngo, D.N.1    Kim, M.M.2    Kim, S.K.3
  • 30
    • 77952965887 scopus 로고    scopus 로고
    • Production of chitooligosaccharides and their potential applications in medicine
    • Aam, B. B., Heggset, E. B., Norberg, A. L., Sørlie, M., Vårum, K. M., and Eijsink, V. G. H. (2010) Production of chitooligosaccharides and their potential applications in medicine Mar. Drugs 8, 1482-1517
    • (2010) Mar. Drugs , vol.8 , pp. 1482-1517
    • Aam, B.B.1    Heggset, E.B.2    Norberg, A.L.3    Sørlie, M.4    Vårum, K.M.5    Eijsink, V.G.H.6
  • 31
    • 0036186885 scopus 로고    scopus 로고
    • Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis
    • DOI 10.1046/j.0014-2956.2001.02721.x
    • Bokma, E., Rozeboom, H. J., Sibbald, M., Dijkstra, B. W., and Beintema, J. J. (2002) Expression and characterization of active site mutants of hevamine, a Chitinase from the rubber tree Hevea brasiliensis Eur. J. Biochem. 269, 893-901 (Pubitemid 34175409)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.3 , pp. 893-901
    • Bokma, E.1    Rozeboom, H.J.2    Sibbald, M.3    Dijkstra, B.W.4    Beintema, J.J.5
  • 32
    • 1642521614 scopus 로고    scopus 로고
    • Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase
    • DOI 10.1046/j.1432-1033.2003.03923.x
    • Synstad, B., Gåseidnes, S., Van Aalten, D. M. F., Vriend, G., Nielsen, J. E., and Eijsink, V. G. H. (2004) Mutational and computational analysis of the role of conserved residues in the active site of a family 18 Chitinase FEBS J. 271, 253-262 (Pubitemid 38130453)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.2 , pp. 253-262
    • Synstad, B.1    Gaseidnes, S.2    Van Aalten, D.M.F.3    Vriend, G.4    Nielsen, J.E.5    Eijsink, V.G.H.6
  • 34
    • 31444442746 scopus 로고    scopus 로고
    • Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation
    • DOI 10.1271/bbb.70.243
    • Aronson, N. N., Jr., Halloran, B. A., Alexeyev, M. F., Zhou, X., Wang, Y., Meehan, E. J., and Chen, L. (2006) Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens Chitinase A enhances transglycosylation Biosci. Biotechnol. Biochem. 70, 243-251 (Pubitemid 43150983)
    • (2006) Bioscience, Biotechnology and Biochemistry , vol.70 , Issue.1 , pp. 243-251
    • Aronson Jr., N.N.1    Halloran, B.A.2    Alexeyev, M.F.3    Zhou, X.E.4    Wang, Y.5    Meehan, E.J.6    Chen, L.7
  • 36
    • 0035949643 scopus 로고    scopus 로고
    • High resolution structural analyses of mutant Chitinase A complexes with substrates provide new insight into the mechanism of catalysis
    • DOI 10.1021/bi010505h
    • Papanikolau, Y., Prag, G., Tavlas, G., Vorgias, C. E., Oppenheim, A. B., and Petratos, K. (2001) High resolution structural analyses of mutant Chitinase A complexes with substrates provide new insight into the mechanism of catalysis Biochemistry 40, 11338-11343 (Pubitemid 32911276)
    • (2001) Biochemistry , vol.40 , Issue.38 , pp. 11338-11343
    • Papanikolau, Y.1    Prag, G.2    Tavlas, G.3    Vorgias, C.E.4    Oppenheim, A.B.5    Petratos, K.6
  • 38
    • 77952145858 scopus 로고    scopus 로고
    • The roles of three Serratia marcescens chitinases in chitin conversion are reflected in different thermodynamic signatures of allosamidin binding
    • Baban, J., Fjeld, S., Sakuda, S., Eijsink, V. G. H., and Sørlie, M. (2010) The roles of three Serratia marcescens chitinases in chitin conversion are reflected in different thermodynamic signatures of allosamidin binding J. Phys. Chem. B 114, 6144-6149
    • (2010) J. Phys. Chem. B , vol.114 , pp. 6144-6149
    • Baban, J.1    Fjeld, S.2    Sakuda, S.3    Eijsink, V.G.H.4    Sørlie, M.5
  • 41
    • 70249145779 scopus 로고    scopus 로고
    • Toward understanding of carbohydrate binding and substrate specificity of a glycosyl hydrolase 18 family (GH-18) Chitinase from Trichoderma harzianum
    • Lienemann, M., Boer, H., Paananen, A., Cottaz, S., and Koivula, A. (2009) Toward understanding of carbohydrate binding and substrate specificity of a glycosyl hydrolase 18 family (GH-18) Chitinase from Trichoderma harzianum Glycobiology 19, 1116-1126
    • (2009) Glycobiology , vol.19 , pp. 1116-1126
    • Lienemann, M.1    Boer, H.2    Paananen, A.3    Cottaz, S.4    Koivula, A.5
  • 42
    • 78249285272 scopus 로고    scopus 로고
    • Determination of substrate binding energies in individual subsites of a family 18 Chitinase
    • Norberg, A. L., Karlsen, V., Hoell, I. A., Bakke, I., Eijsink, V. G. H., and Sørlie, M. (2010) Determination of substrate binding energies in individual subsites of a family 18 Chitinase FEBS Lett. 584, 4581-4585
    • (2010) FEBS Lett. , vol.584 , pp. 4581-4585
    • Norberg, A.L.1    Karlsen, V.2    Hoell, I.A.3    Bakke, I.4    Eijsink, V.G.H.5    Sørlie, M.6
  • 43
    • 12944260514 scopus 로고
    • Atomic features of protein-carbohydrate interactions
    • Vyas, N. K. (1991) Atomic features of protein-carbohydrate interactions Curr. Opin. Struct. Biol. 1, 732-740 (Pubitemid 121002420)
    • (1991) Current Opinion in Structural Biology , vol.1 , Issue.5 , pp. 732-740
    • Vyas, N.K.1
  • 44
    • 0344825227 scopus 로고    scopus 로고
    • Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitin
    • DOI 10.1042/BJ20030419
    • Watanabe, T., Ariga, Y., Sato, U., Toratani, T., Hashimoto, M., Nikiaidou, N., Kezuka, Y., Nonaka, T., and Sugiyama, J. (2003) Aromatic residues within the substrate-binding cleft of Bacillus circulans Chitinase A1 are essential for hydrolysis of crystalline chitin Biochem. J. 376, 237-244 (Pubitemid 37487219)
    • (2003) Biochemical Journal , vol.376 , Issue.1 , pp. 237-244
    • Watanabe, T.1    Ariga, Y.2    Sato, U.3    Toratani, T.4    Hashimoto, M.5    Nikaidou, N.6    Kezuka, Y.7    Nonaka, T.8    Sugiyama, J.9
  • 45
    • 68949127197 scopus 로고    scopus 로고
    • Mutation of Trp137 to glutamate completely removes transglycosyl activity associated with Aspergillus fumigatus AfChiB1
    • Lü, Y., Yang, H., Hu, H., Wang, Y., Rao, Z., and Jin, C. (2008) Mutation of Trp137 to glutamate completely removes transglycosyl activity associated with Aspergillus fumigatus AfChiB1 Glycoconj. J. 26, 525-534
    • (2008) Glycoconj. J. , vol.26 , pp. 525-534
    • Lü, Y.1    Yang, H.2    Hu, H.3    Wang, Y.4    Rao, Z.5    Jin, C.6
  • 46
    • 0028815373 scopus 로고
    • Chitinase B from Serratia marcescens BJL200 is exported to the periplasm without processing
    • Brurberg, M. B., Eijsink, V. G. H., Haandrikman, A. J., Venema, G., and Nes, I. F. (1995) Chitinase B from Serratia marcescens BJL200 is exported to the periplasm without processing Microbiology 141, 123-131
    • (1995) Microbiology , vol.141 , pp. 123-131
    • Brurberg, M.B.1    Eijsink, V.G.H.2    Haandrikman, A.J.3    Venema, G.4    Nes, I.F.5
  • 47
    • 0027973484 scopus 로고
    • Characterization of a chitinase gene (chiA) from Serratia marcescens BJL200 and one-step purification of the gene product
    • DOI 10.1016/0378-1097(94)00462-5
    • Brurberg, M. B., Eijsink, V. G. H., and Nes, I. F. (1994) Characterization of a Chitinase gene (chiA) from Serratia marcescens BJL200 and one-step purification of the gene product FEMS Microbiol. Lett. 124, 399-404 (Pubitemid 24369107)
    • (1994) FEMS Microbiology Letters , vol.124 , Issue.3 , pp. 399-404
    • Brurberg, M.B.1    Eijsink, V.G.H.2    Nes, I.F.3
  • 49
    • 33847421735 scopus 로고    scopus 로고
    • Natural substrate assay for chitinases using high-performance liquid chromatography: A comparison with existing assays
    • DOI 10.1016/j.ab.2006.12.044, PII S0003269707000036
    • Krokeide, I.-M., Synstad, B., Gåseidnes, S., Horn, S. J., Eijsink, V. G. H., and Sørlie, M. (2007) Natural substrate assay for chitinases using high-performance liquid chromatography: A comparison with existing assays Anal. Biochem. 363, 128-134 (Pubitemid 46348973)
    • (2007) Analytical Biochemistry , vol.363 , Issue.1 , pp. 128-134
    • Krokeide, I.-M.1    Synstad, B.2    Gaseidnes, S.3    Horn, S.J.4    Eijsink, V.G.H.5    Sorlie, M.6
  • 50
    • 41549104699 scopus 로고    scopus 로고
    • Expression and Characterization of Endochitinase C from Serratia marcescens BJL200 and Its Purification by a One-step General Purification Method
    • Synstad, B., Vaaje-Kolstad, G., Cederkvist, H. F., Saua, S. F., Horn, S. J., Eijsink, V. G. H., and Sørlie, M. (2008) Expression and Characterization of Endochitinase C from Serratia marcescens BJL200 and Its Purification by a One-step General Purification Method Biosci. Biotechnol. Biochem. 72, 1-9
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 1-9
    • Synstad, B.1    Vaaje-Kolstad, G.2    Cederkvist, H.F.3    Saua, S.F.4    Horn, S.J.5    Eijsink, V.G.H.6    Sørlie, M.7
  • 51
    • 70350233222 scopus 로고    scopus 로고
    • Substrate binding modes and anomer selectivity of Chitinase A from Vibrio harveyi
    • not supplied.
    • Suginta, W., Pantoom, S., and Prinz, H. Substrate binding modes and anomer selectivity of Chitinase A from Vibrio harveyi. J. Chem. Biol 2009, not supplied.
    • (2009) J. Chem. Biol
    • Suginta, W.1    Pantoom, S.2    Prinz, H.3
  • 52
    • 0242667918 scopus 로고    scopus 로고
    • Glycosynthase Activity of Bacillus licheniformis 1,3-1,4-β-Glucanase Mutants: Specificity, Kinetics, and Mechanism
    • DOI 10.1021/bi030131n
    • Faijes, M., Pérez, X., Pérez, O., and Planas, A. (2003) Glycosynthase activity of Bacillus licheniformis 1,3-1,4-β-glucanase mutants: Specificity, kinetics, and mechanism Biochemistry 42, 13304-13318 (Pubitemid 37420683)
    • (2003) Biochemistry , vol.42 , Issue.45 , pp. 13304-13318
    • Faijes, M.1    Perez, X.2    Perez, O.3    Planas, A.4
  • 53
    • 79958159163 scopus 로고    scopus 로고
    • QM/MM Modeling of substrate-assisted catalysis in family 18 chitinases: Conformational changes and the role of Asp142 in catalysis in ChiB
    • 10.1021/bi101362g
    • Jitonnom, J., Lee, V. S., Nimmanpipug, P., Rowlands, H. A., and Mulholland, A. J. (2011) QM/MM Modeling of substrate-assisted catalysis in family 18 chitinases: Conformational changes and the role of Asp142 in catalysis in ChiB Biochemistry 10.1021/bi101362g
    • (2011) Biochemistry
    • Jitonnom, J.1    Lee, V.S.2    Nimmanpipug, P.3    Rowlands, H.A.4    Mulholland, A.J.5
  • 54
    • 67449088829 scopus 로고    scopus 로고
    • Aromatic residues in the catalytic center of Chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency
    • Zakariassen, H., Aam, B. B., Horn, S. J., Vårum, K. M., Sørlie, M., and Eijsink, V. G. H. (2009) Aromatic residues in the catalytic center of Chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency J. Biol. Chem. 284, 10610-10617
    • (2009) J. Biol. Chem. , vol.284 , pp. 10610-10617
    • Zakariassen, H.1    Aam, B.B.2    Horn, S.J.3    Vårum, K.M.4    Sørlie, M.5    Eijsink, V.G.H.6
  • 55
    • 77950866694 scopus 로고    scopus 로고
    • Signatures of activation parameters reveal substrate-dependent rate determining steps in polysaccharide turnover by a family 18 Chitinase
    • Zakariassen, H., Eijsink, V. G. H., and Sorlie, M. (2010) Signatures of activation parameters reveal substrate-dependent rate determining steps in polysaccharide turnover by a family 18 Chitinase Carbohydr. Polym. 81, 14-20
    • (2010) Carbohydr. Polym. , vol.81 , pp. 14-20
    • Zakariassen, H.1    Eijsink, V.G.H.2    Sorlie, M.3
  • 56
    • 33645090163 scopus 로고    scopus 로고
    • Three-dimensional crystal structure and enzymatic characterization of β-Mannanase Man5A from Blue Mussel Mytilus edulis
    • Larsson, A. M., Anderson, L., Xu, B., Muñoz, I. G., Usón, I., Janson, J.-C., Stålbrand, H., and Ståhlberg, J. (2006) Three-dimensional crystal structure and enzymatic characterization of β-Mannanase Man5A from Blue Mussel Mytilus edulis J. Mol. Biol. 357, 1500-1510
    • (2006) J. Mol. Biol. , vol.357 , pp. 1500-1510
    • Larsson, A.M.1    Anderson, L.2    Xu, B.3    Muñoz, I.G.4    Usón, I.5    Janson, J.-C.6    Stålbrand, H.7    Ståhlberg, J.8
  • 60
    • 0348050009 scopus 로고    scopus 로고
    • Oligosaccharide synthesis by glycosynthases
    • DOI 10.1016/j.tibtech.2003.10.008
    • Perugino, G., Trincone, A., Rossi, M., and Moracci, M. (2004) Oligosaccharide synthesis by glycosynthases Trends Biotechnol. 22, 31-37 (Pubitemid 38030318)
    • (2004) Trends in Biotechnology , vol.22 , Issue.1 , pp. 31-37
    • Perugino, G.1    Trincone, A.2    Rossi, M.3    Moracci, M.4
  • 61
    • 42149186349 scopus 로고    scopus 로고
    • Teaching old enzymes new tricks: Engineering and evolution of glycosidases and glycosyl transferases for improved glycoside synthesis
    • DOI 10.1139/O07-149
    • Shaikh, F. A. and Withers, S. G. (2008) Teaching old enzymes new tricks: engineering and evolution of glycosdiases and glycosyl transferase for improved glycoside synthesis Biochem. Cell Biol. 86, 169-177 (Pubitemid 351536497)
    • (2008) Biochemistry and Cell Biology , vol.86 , Issue.2 , pp. 169-177
    • Shaikh, F.A.1    Withers, S.G.2
  • 62
    • 0037321566 scopus 로고    scopus 로고
    • De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase a and its complex with the inhibitor allosamidin
    • DOI 10.1107/S0907444902021923
    • Papanikolau, Y., Tavlas, G., Vorgias, C. E., and Petratos, K. (2003) De novo purification scheme and crystallization conditions yield high-resolution structures of Chitinase A and its complex with the inhibitor allosamidin Acta Crystallogr. 59, 400-403 (Pubitemid 36224875)
    • (2003) Acta Crystallographica Section D: Biological Crystallography , vol.59 , Issue.2 , pp. 400-403
    • Papanikolau, Y.1    Tavlas, G.2    Vorgias, C.E.3    Petratos, K.4
  • 63
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases [1]
    • Davies, G. J., Wilson, K. S., and Henrissat, B. (1997) Nomenclature for sugar-binding subsites in glycosyl hydrolases Biochem. J. 321, 557-559 (Pubitemid 27056509)
    • (1997) Biochemical Journal , vol.321 , Issue.2 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 64
    • 0019869086 scopus 로고
    • Substrate-binding site of endo-1,4-β-xylanase of the yeast Cryptococcus albidus
    • Biely, P., Kratky, Z., and Vrsanska, M. (1981) Substrate-binding site of endo-b-1,4-xylanase of the yeast Cryptococcus albidus Eur. J. Biochem. 119, 559-564 (Pubitemid 12204091)
    • (1981) European Journal of Biochemistry , vol.119 , Issue.3 , pp. 559-564
    • Biely, P.1    Kratky, Z.2    Vrsanska, M.3


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