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Volumn 26, Issue 5, 2009, Pages 525-534

Mutation of Trp137 to glutamate completely removes transglycosyl activity associated with the Aspergillus fumigatus AfChiB1

Author keywords

Aspergillus fumigatus; Chitinase; Mutation; Transglycosylation

Indexed keywords

GLUTAMIC ACID; HYDROLASE; NUCLEOPHILE; CHITINASE; FUNGAL PROTEIN;

EID: 68949127197     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-008-9203-z     Document Type: Article
Times cited : (27)

References (29)
  • 1
    • 0028316274 scopus 로고
    • Stereochemical course of the hydrolysis reaction catalyzed by chitinases a1 and d from bacillus circulans WL-12
    • DOI 10.1016/0014-5793(94)80314-5
    • S. Armand H. Tomita A. Heyraud C. Gey T. Watanabe B. Henrissat 1994 Stereochemical course of the hydrolysis reaction catalyzed by chitinases A1 and D from Bacillus circulans WL-12 FEBS Lett. 343 177 180 8168626 10.1016/0014-5793(94)80314-5 1:CAS:528:DyaK2cXlsFajs74%3D (Pubitemid 24126671)
    • (1994) FEBS Letters , vol.343 , Issue.2 , pp. 177-180
    • Armanda, S.1    Tomita, H.2    Heyraud, A.3    Gey, C.4    Watanabe, T.5    Henrissat, B.6
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 942051 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
    • M. Bradford 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem 72 248 254 942051 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 4
    • 0029884662 scopus 로고    scopus 로고
    • Comparative studies of chitinases A and B from Serratia marcescens
    • 10.1099/13500872-142-7-1581 1:CAS:528:DyaK28Xks1yit7w%3D
    • M.B. Brurberg I.F. Nes V.G.H. Eijsink 1996 Comparative studies of chitinases A and B from Serratia marcescens Microbiol. 142 1581 1589 10.1099/13500872-142-7-1581 1:CAS:528:DyaK28Xks1yit7w%3D
    • (1996) Microbiol. , vol.142 , pp. 1581-1589
    • Brurberg, M.B.1    Nes, I.F.2    Eijsink, V.G.H.3
  • 5
    • 0031781440 scopus 로고    scopus 로고
    • Inducible chitinolytic system of Aspergillus fumigatus
    • 10.1099/00221287-144-6-1575
    • G.M. Escort V.M. Hearn D.J. Adams 1998 Inducible chitinolytic system of Aspergillus fumigatus Microbiol. 144 1575 1585 10.1099/00221287-144-6-1575
    • (1998) Microbiol. , vol.144 , pp. 1575-1585
    • Escort, G.M.1    Hearn, V.M.2    Adams, D.J.3
  • 6
    • 0026709204 scopus 로고
    • What's new in chitinase research?
    • 10.1007/BF02124285 1:CAS:528:DyaK38XlvVKqtL0%3D
    • J. Flach P.E. Pilet P. Jolles 1992 What's new in chitinase research? Experientia Basel 48 701 716 10.1007/BF02124285 1:CAS:528:DyaK38XlvVKqtL0%3D
    • (1992) Experientia Basel , vol.48 , pp. 701-716
    • Flach, J.1    Pilet, P.E.2    Jolles, P.3
  • 7
    • 0000759564 scopus 로고
    • Physiology of microbial degradation of chitin and chitosan
    • 10.1007/BF00058835 1:CAS:528:DyaK3MXkt1Gmurg%3D
    • G.W. Gooday 1990 Physiology of microbial degradation of chitin and chitosan Biodegradation 1 177 190 10.1007/BF00058835 1:CAS:528: DyaK3MXkt1Gmurg%3D
    • (1990) Biodegradation , vol.1 , pp. 177-190
    • Gooday, G.W.1
  • 8
    • 0001773321 scopus 로고    scopus 로고
    • The ever-widening diversity of chitinase
    • G.W. Gooday 1997 The ever-widening diversity of chitinase Carbohydrates Eur. 19 18 22
    • (1997) Carbohydrates Eur. , vol.19 , pp. 18-22
    • Gooday, G.W.1
  • 9
    • 0028880647 scopus 로고
    • Identification and preliminary characterization of a chitinase gene in the Autographa californica nuclear polyhedrosis virus genome
    • 7571437 10.1006/viro.1995.1525 1:CAS:528:DyaK2MXosFWgtL4%3D
    • R.E. Hawtin K. Arnold M.D. Ayres P.M.D. Zanotto S.C. Howard G.W. Gooday L.H. Chappell P.A. Kitts L.A. King R.D. Possee 1995 Identification and preliminary characterization of a chitinase gene in the Autographa californica nuclear polyhedrosis virus genome Virology 212 673 685 7571437 10.1006/viro.1995.1525 1:CAS:528:DyaK2MXosFWgtL4%3D
    • (1995) Virology , vol.212 , pp. 673-685
    • Hawtin, R.E.1    Arnold, K.2    Ayres, M.D.3    Zanotto, P.M.D.4    Howard, S.C.5    Gooday, G.W.6    Chappell, L.H.7    Kitts, P.A.8    King, L.A.9    Possee, R.D.10
  • 10
    • 16644391319 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of a native chitinase from the fungal pathogen Aspergillus fumigatus YJ-4O7
    • DOI 10.1107/S0907444904005190
    • H. Hu G. Wang H. Yang J. Zhou L. Mo K. Yang C. Jin C. Jin Z. Rao 2004 Crystallization and preliminary crystallographic analysis of a native chitinase from the fungal pathogen Aspergillus fumigatus YJ-407 Acta Crystallogr. D Biol. Crystallogr. 60 Pt 5 939 940 15103145 10.1107/S0907444904005190 (Pubitemid 41184795)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.5 , pp. 939-940
    • Hu, H.1    Wang, G.2    Yang, H.3    Zhou, J.4    Mo, L.5    Yang, K.6    Jin, C.7    Jin, C.8    Rao, Z.9
  • 11
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • 1:CAS:528:DyaE38XjtFKgsA%3D%3D
    • T. Imoto K. Yagishita 1971 A simple activity measurement of lysozyme Agric. Biol. Chem. 35 1154 1156 1:CAS:528:DyaE38XjtFKgsA%3D%3D
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 12
    • 0026002418 scopus 로고
    • Chitinase is required for cell separation during growth of Saccharomyces cerevisiae. J
    • 1:CAS:528:DyaK38XisV2ltLs%3D
    • M.J. Kuranda P.W. Robbins 1991 Chitinase is required for cell separation during growth of Saccharomyces cerevisiae. J Biol. Chem. 266 19758 19767 1:CAS:528:DyaK38XisV2ltLs%3D
    • (1991) Biol. Chem. , vol.266 , pp. 19758-19767
    • Kuranda, M.J.1    Robbins, P.W.2
  • 13
    • 0000122560 scopus 로고
    • Properties and transglycosylation reaction of a chitinase from Nocardia orientalis. Agric
    • 1:CAS:528:DyaL1MXls12qt7o%3D
    • F. Nanjo I. Sakai M. Ishikawa K. Isobe T. Usui 1989 Properties and transglycosylation reaction of a chitinase from Nocardia orientalis. Agric Biol. Chem. 53 2189 2195 1:CAS:528:DyaL1MXls12qt7o%3D
    • (1989) Biol. Chem. , vol.53 , pp. 2189-2195
    • Nanjo, F.1    Sakai, I.2    Ishikawa, M.3    Isobe, K.4    Usui, T.5
  • 14
    • 0037490208 scopus 로고    scopus 로고
    • Crystal structures of allosamidin derivatives in complex with human macrophage chitinase
    • DOI 10.1074/jbc.M300362200
    • F.V. Rao D.R. Houston R.G. Boot J.M.F.G. Aerts S. Sakuda D.M.F. van Aalten 2003 Crystal structures of allosamidin derivatives in complex with human macrophage chitinase J. Biol. Chem. 278 20110 20116 12639956 10.1074/jbc.M300362200 1:CAS:528:DC%2BD3sXktVaqu74%3D (Pubitemid 36799205)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.22 , pp. 20110-20116
    • Rao, F.V.1    Houston, D.R.2    Boot, R.G.3    Aerts, J.M.F.G.4    Sakuda, S.5    Van Aalten, D.M.F.6
  • 15
    • 12344317078 scopus 로고    scopus 로고
    • Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases
    • DOI 10.1016/j.chembiol.2004.10.013, PII S1074552104003308
    • F.C. Rao D.R. Houston R.G. Boot J.M.F.G. Aerts M. Hodkinson D.J. Adams K. Shimi S. Omura D.M.F. van Aalten 2005 Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinase Chem. Biol. 12 65 76 15664516 10.1016/j.chembiol.2004.10.013 1:CAS:528:DC%2BD2MXmtlKmsA%3D%3D (Pubitemid 40118327)
    • (2005) Chemistry and Biology , vol.12 , Issue.1 , pp. 65-76
    • Rao, F.V.1    Houston, D.R.2    Boot, R.G.3    Aerts, J.M.F.G.4    Hodkinson, M.5    Adams, D.J.6    Shiomi, K.7    Omura, S.8    Van Aalten, D.M.F.9
  • 16
    • 0028911536 scopus 로고
    • Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins
    • 7836450 10.1074/jbc.270.44.26252 1:CAS:528:DyaK2MXjsV2ksbk%3D
    • G.H. Renkema R.G. Boot A.O. Muijsers W.E. Donker-Koopman J.M.F.G. Aerts 1995 Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins J. Biol. Chem. 270 2198 2202 7836450 10.1074/jbc.270.44.26252 1:CAS:528:DyaK2MXjsV2ksbk%3D
    • (1995) J. Biol. Chem. , vol.270 , pp. 2198-2202
    • Renkema, G.H.1    Boot, R.G.2    Muijsers, A.O.3    Donker-Koopman, W.E.4    Aerts, J.M.F.G.5
  • 17
    • 0023110718 scopus 로고
    • Search for microbial insect growth regulators. II. Allosamidin, a novel insect chitinase inhibitor
    • 1:CAS:528:DyaL2sXhslWisr8%3D
    • S. Sakuda A. Isogai S. Matsumoto A. Suzuki 1987 Search for microbial insect growth regulators. II. Allosamidin, a novel insect chitinase inhibitor J. Antibiot. (Tokyo) 40 296 300 1:CAS:528:DyaL2sXhslWisr8%3D
    • (1987) J. Antibiot. (Tokyo) , vol.40 , pp. 296-300
    • Sakuda, S.1    Isogai, A.2    Matsumoto, S.3    Suzuki, A.4
  • 18
    • 0000640340 scopus 로고
    • A simple method for the determination of glucose in blood
    • 1:CAS:528:DyaH28XhtFGjsw%3D%3D
    • O. Schales S.S. Schales 1945 A simple method for the determination of glucose in blood Arch. Biochem. 8 285 292 1:CAS:528:DyaH28XhtFGjsw%3D%3D
    • (1945) Arch. Biochem. , vol.8 , pp. 285-292
    • Schales, O.1    Schales, S.S.2
  • 19
    • 0028774705 scopus 로고
    • Crystal structures of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor
    • 7704528 10.1016/S0969-2126(94)00120-0 1:STN:280:DyaK2M3hvFersg%3D%3D
    • A.C. Terwisscha van Scheltinga K.H. Kalk J.J. Beitema B.W. Dijkstra 1994 Crystal structures of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor Structure 2 1181 1189 7704528 10.1016/S0969-2126(94)00120-0 1:STN:280:DyaK2M3hvFersg%3D%3D
    • (1994) Structure , vol.2 , pp. 1181-1189
    • Terwisscha Van Scheltinga, A.C.1    Kalk, K.H.2    Beitema, J.J.3    Dijkstra, B.W.4
  • 20
    • 0028828695 scopus 로고
    • Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: Evidence for substrate assisted catalysis
    • 10.1021/bi00048a003 1:CAS:528:DyaK2MXpt12rtL8%3D
    • A.C. Terwisscha van Scheltinga S. Armand K.H. Kalk A. Isogai B. Henrissat B.W. Dijkstra 1995 Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis Biochem. 34 15619 15623 10.1021/bi00048a003 1:CAS:528:DyaK2MXpt12rtL8%3D
    • (1995) Biochem. , vol.34 , pp. 15619-15623
    • Terwisscha Van Scheltinga, A.C.1    Armand, S.2    Kalk, K.H.3    Isogai, A.4    Henrissat, B.5    Dijkstra, B.W.6
  • 21
    • 0030595119 scopus 로고    scopus 로고
    • The 1.8 A resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18
    • DOI 10.1006/jmbi.1996.0510
    • A.C. Terwisscha van Scheltinga M. Hennig B.W. Dijkstra 1996 The 1.8 Å resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18 J. Mol. Biol. 262 243 257 8831791 10.1006/jmbi.1996.0510 1:STN:280:DyaK28vivVKruw%3D%3D (Pubitemid 26326974)
    • (1996) Journal of Molecular Biology , vol.262 , Issue.2 , pp. 243-257
    • Terwisscha Van Scheltinga, A.C.1    Hennig, M.2    Dijkstra, B.W.3
  • 23
    • 0023137199 scopus 로고
    • Transglycosylation reaction of a chitinase purified from Nocardia orientalis. Biochim
    • 1:CAS:528:DyaL2sXktVeisrs%3D
    • T. Usui Y. Hayachi F. Nanjo K. Sakai Y. Ishido 1987 Transglycosylation reaction of a chitinase purified from Nocardia orientalis. Biochim Biophys. Acta 923 302 309 1:CAS:528:DyaL2sXktVeisrs%3D
    • (1987) Biophys. Acta , vol.923 , pp. 302-309
    • Usui, T.1    Hayachi, Y.2    Nanjo, F.3    Sakai, K.4    Ishido, Y.5
  • 25
    • 0033598751 scopus 로고    scopus 로고
    • The chitinase PfCHT1 from the human malaria parasite Plasmodium falciparum lacks proenzyme and chitin-binding domains and displays unique substrate preferences
    • 10570198 10.1073/pnas.96.24.14061 1:CAS:528:DyaK1MXns1Oqu7c%3D
    • J.M. Vinetz S.K. Dave C.A. Specht K.A. Brameld B. Xu R. Hayward D.A. Fidock 1999 The chitinase PfCHT1 from the human malaria parasite Plasmodium falciparum lacks proenzyme and chitin-binding domains and displays unique substrate preferences Proc. Natl. Acad. Sci. USA 96 14061 14066 10570198 10.1073/pnas.96.24.14061 1:CAS:528:DyaK1MXns1Oqu7c%3D
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14061-14066
    • Vinetz, J.M.1    Dave, S.K.2    Specht, C.A.3    Brameld, K.A.4    Xu, B.5    Hayward, R.6    Fidock, D.A.7
  • 26
    • 0024955069 scopus 로고
    • Chitinase produced by Myrothecium verrucaria and its significance for fungal mycelia degradation
    • 10.2323/jgam.35.343 1:CAS:528:DyaK3cXitFelu74%3D
    • P. Vyas M.V. Deshpande 1989 Chitinase produced by Myrothecium verrucaria and its significance for fungal mycelia degradation J. Gen. Appl. Microbiol. 35 343 350 10.2323/jgam.35.343 1:CAS:528:DyaK3cXitFelu74%3D
    • (1989) J. Gen. Appl. Microbiol. , vol.35 , pp. 343-350
    • Vyas, P.1    Deshpande, M.V.2
  • 27
    • 0035834760 scopus 로고    scopus 로고
    • Expression and Secretion of a Larval-specific Chitinase (Family 18 Glycosyl Hydrolase) by the Infective Stages of the Parasitic Nematode, Onchocerca volvulus
    • DOI 10.1074/jbc.M103479200
    • Y. Wu G. Egerton A.P. Underwood S. Sakuda A.E. Bianco 2001 Expression and secretion of a larval-specific chitinase (family 18 glycosyl hydrolase) by the infective stages of the parasitic nematode, Onchocerca volvulus. J Biol. Chem. 276 42557 42564 10.1074/jbc.M103479200 1:CAS:528:DC%2BD3MXosVGmtr0%3D (Pubitemid 37371171)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.45 , pp. 42557-42564
    • Wu, Y.1    Egerton, G.2    Underwood, A.P.3    Sakuda, S.4    Bianco, A.E.5
  • 28
    • 37549019928 scopus 로고    scopus 로고
    • Cloning and expression of chitinase gene from Aspergillus fumigatus YJ-407
    • 1:CAS:528:DC%2BD2MXotVSgu74%3D
    • Y. Wang J. Wang H. Hu X. Yang S. Yang X. Yu C. Jin 2004 Cloning and expression of chitinase gene from Aspergillus fumigatus YJ-407 Chin. J. Biotechnol. 20 843 850 1:CAS:528:DC%2BD2MXotVSgu74%3D
    • (2004) Chin. J. Biotechnol. , vol.20 , pp. 843-850
    • Wang, Y.1    Wang, J.2    Hu, H.3    Yang, X.4    Yang, S.5    Yu, X.6    Jin, C.7
  • 29
    • 0034834977 scopus 로고    scopus 로고
    • A novel chitinase having a unique mode of action from Aspergillus fumigatus YJ-407
    • DOI 10.1046/j.1432-1327.2001.02323.x
    • G. Xia C. Jin J. Zhou S. Yang S. Zhang C. Jin 2001 A novel chitinase having a unique mode of action from Aspergillus fumigatus YJ-407 Eur. J. Biochem. 268 4079 4085 11454002 10.1046/j.1432-1327.2001.02323.x 1:CAS:528:DC%2BD3MXlsVejs7Y%3D (Pubitemid 32868621)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.14 , pp. 4079-4085
    • Xia, G.1    Jin, C.2    Zhou, J.3    Yang, S.4    Zhang, S.5    Jin, C.6


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