메뉴 건너뛰기




Volumn 273, Issue 13, 2006, Pages 2929-2941

Characterization of a β-N-acetylhexosaminidase and a β-N-acetylglucosaminidase/β-glucosidase from Cellulomonas fimi

Author keywords

Bifunctional glycosidase; Cell wall recycling; Chitin metabolism; murein; Peptidoglycan

Indexed keywords

BACTERIAL ENZYME; BETA GLUCOSIDASE; BETA N ACETYLHEXOSAMINIDASE; CELL ENZYME; GLYCOSIDASE; N ACETYL BETA GLUCOSAMINIDASE;

EID: 33745216253     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05308.x     Document Type: Article
Times cited : (58)

References (46)
  • 1
    • 33745210452 scopus 로고    scopus 로고
    • β-N-Acetylhexosaminidases: Two enzyme families, two mechanisms
    • In. Peter, M.G. Domard, A. Muzzarelli, R.A.A., eds), pp. University of Potsdam, Potsdam.
    • Mayer C Vocadlo DJ Withers SG ( 2000) β-N-Acetylhexosaminidases: two enzyme families, two mechanisms. In Advances in Chitin Science ( Peter MG Domard A Muzzarelli RAA, eds), pp. 612 619. University of Potsdam, Potsdam.
    • (2000) Advances in Chitin Science , pp. 612-619
    • Mayer, C.1    Vocadlo, D.J.2    Withers, S.G.3
  • 2
    • 0032059448 scopus 로고    scopus 로고
    • Glycosidase families
    • Henrissat B ( 1998) Glycosidase families. Biochem Soc Trans 26, 153 156.
    • (1998) Biochem Soc Trans , vol.26 , pp. 153-156
    • Henrissat, B.1
  • 3
    • 0031277599 scopus 로고    scopus 로고
    • β-N-Acetylhexosaminidase: A target for the design of antifungal agents
    • Horsch M Mayer C Sennhauser U Rast DM ( 1997) β-N- Acetylhexosaminidase: a target for the design of antifungal agents. Pharmacol Ther 76, 187 218.
    • (1997) Pharmacol Ther , vol.76 , pp. 187-218
    • Horsch, M.1    Mayer, C.2    Sennhauser, U.3    Rast, D.M.4
  • 4
    • 0030451823 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel β-N-acetyl-d- glucosaminidase from Vibrio furnissii
    • Chitlaru E Roseman S ( 1996) Molecular cloning and characterization of a novel β-N-acetyl-d-glucosaminidase from Vibrio furnissii. J Biol Chem 271, 33433 33439.
    • (1996) J Biol Chem , vol.271 , pp. 33433-33439
    • Chitlaru, E.1    Roseman, S.2
  • 6
    • 0031904683 scopus 로고    scopus 로고
    • A novel β-N-acetylglucosaminidase from Streptomyces thermoviolaceus OPC-520: Gene cloning, expression, and assignment to family 3 of the glycosyl hydrolases
    • Tsujibo H Hatano N Mikami T Hirasawa A Miyamoto K Inamori Y ( 1998) A novel β-N-acetylglucosaminidase from Streptomyces thermoviolaceus OPC-520: gene cloning, expression, and assignment to family 3 of the glycosyl hydrolases. Appl Environ Microbiol 64, 2920 2924.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2920-2924
    • Tsujibo, H.1    Hatano, N.2    Mikami, T.3    Hirasawa, A.4    Miyamoto, K.5    Inamori, Y.6
  • 7
    • 0034635169 scopus 로고    scopus 로고
    • Mechanism of action and identification of Asp242 as the catalytic nucleophile of Vibrio furnisii N-acetyl-β-d-glucosaminidase using 2-acetamido-2-deoxy-5-fluoro-alpha-1-idopyranosyl fluoride
    • Vocadlo DJ Mayer C He S Withers SG ( 2000) Mechanism of action and identification of Asp242 as the catalytic nucleophile of Vibrio furnisii N-acetyl-β-d-glucosaminidase using 2-acetamido-2-deoxy-5-fluoro-alpha-1- idopyranosyl fluoride. Biochemistry 39, 117 126.
    • (2000) Biochemistry , vol.39 , pp. 117-126
    • Vocadlo, D.J.1    Mayer, C.2    He, S.3    Withers, S.G.4
  • 8
    • 25444533563 scopus 로고    scopus 로고
    • Detailed comparative analysis of the catalytic mechanisms of β-N-acetylglucosaminidases from families 3 and 20 of glycoside hydrolases
    • Vocadlo DJ Withers SG ( 2005) Detailed comparative analysis of the catalytic mechanisms of β-N-acetylglucosaminidases from families 3 and 20 of glycoside hydrolases. Biochemistry 44, 12809 12818.
    • (2005) Biochemistry , vol.44 , pp. 12809-12818
    • Vocadlo, D.J.1    Withers, S.G.2
  • 10
    • 0035834783 scopus 로고    scopus 로고
    • Biochemical and structural assessment of the 1-N-azasugar GalNAc-isofagomine as a potent family 20 β-N-acetylhexosaminidase inhibitor
    • Mark BL Vocadlo DJ Zhao D Knapp S Withers SG James MN ( 2001) Biochemical and structural assessment of the 1-N-azasugar GalNAc-isofagomine as a potent family 20 β-N-acetylhexosaminidase inhibitor. J Biol Chem 276, 42131 42137.
    • (2001) J Biol Chem , vol.276 , pp. 42131-42137
    • Mark, B.L.1    Vocadlo, D.J.2    Zhao, D.3    Knapp, S.4    Withers, S.G.5    James, M.N.6
  • 11
    • 0037131312 scopus 로고    scopus 로고
    • Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state
    • Williams SJ Mark BL Vocadlo DJ James MN Withers SG ( 2002) Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. J Biol Chem 277, 40055 40065.
    • (2002) J Biol Chem , vol.277 , pp. 40055-40065
    • Williams, S.J.1    Mark, B.L.2    Vocadlo, D.J.3    James, M.N.4    Withers, S.G.5
  • 12
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • Vocadlo DJ Davies GJ Laine R Withers SG ( 2001) Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature 412, 835 838.
    • (2001) Nature , vol.412 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 13
    • 0034681333 scopus 로고    scopus 로고
    • Cloning, expression, characterization, and nucleophile identification of family 3, Aspergillus nigerβ-glucosidase
    • Dan S Marton I Dekel M Bravdo BA He S Withers SG Shoseyov O ( 2000) Cloning, expression, characterization, and nucleophile identification of family 3, Aspergillus nigerβ-glucosidase. J Biol Chem 275, 4973 4980.
    • (2000) J Biol Chem , vol.275 , pp. 4973-4980
    • Dan, S.1    Marton, I.2    Dekel, M.3    Bravdo, B.A.4    He, S.5    Withers, S.G.6    Shoseyov, O.7
  • 14
    • 0033657315 scopus 로고    scopus 로고
    • Identification of active site residues in glycosidases by use of tandem mass spectrometry
    • Vocadlo DJ Withers SG ( 2000) Identification of active site residues in glycosidases by use of tandem mass spectrometry. Methods Mol Biol 146, 203 222.
    • (2000) Methods Mol Biol , vol.146 , pp. 203-222
    • Vocadlo, D.J.1    Withers, S.G.2
  • 15
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: Anatomy of a finely tuned catalyst
    • Zechel DL Withers SG ( 2000) Glycosidase mechanisms: anatomy of a finely tuned catalyst. Acc Chem Res 33, 11 18.
    • (2000) Acc Chem Res , vol.33 , pp. 11-18
    • Zechel, D.L.1    Withers, S.G.2
  • 16
    • 0029670041 scopus 로고    scopus 로고
    • Barley β-d-glucan exohydrolases with β-d-glucosidase activity. Purification, characterization, and determination of primary structure from a cDNA clone
    • Hrmova M Harvey AJ Wang J Shirley NJ Jones GP Stone BA Hoj PB Fincher GB ( 1996) Barley β-d-glucan exohydrolases with β-d-glucosidase activity. Purification, characterization, and determination of primary structure from a cDNA clone. J Biol Chem 271, 5277 5286.
    • (1996) J Biol Chem , vol.271 , pp. 5277-5286
    • Hrmova, M.1    Harvey, A.J.2    Wang, J.3    Shirley, N.J.4    Jones, G.P.5    Stone, B.A.6    Hoj, P.B.7    Fincher, G.B.8
  • 17
    • 0034333059 scopus 로고    scopus 로고
    • Comparative modeling of the three-dimensional structures of family 3 glycoside hydrolases
    • Harvey AJ Hrmova M De Gori R Varghese JN Fincher GB ( 2000) Comparative modeling of the three-dimensional structures of family 3 glycoside hydrolases. Proteins 41, 257 269.
    • (2000) Proteins , vol.41 , pp. 257-269
    • Harvey, A.J.1    Hrmova, M.2    De Gori, R.3    Varghese, J.N.4    Fincher, G.B.5
  • 18
    • 0033081517 scopus 로고    scopus 로고
    • Three-dimensional structure of a barley β-d-glucan exohydrolase, a family 3 glycosyl hydrolase
    • Varghese JN Hrmova M Fincher GB ( 1999) Three-dimensional structure of a barley β-d-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure Fold Des 7, 179 190.
    • (1999) Structure Fold des , vol.7 , pp. 179-190
    • Varghese, J.N.1    Hrmova, M.2    Fincher, G.B.3
  • 19
    • 1042301375 scopus 로고    scopus 로고
    • Three-dimensional structure of the barley β-d-glucan glucohydrolase in complex with a transition state mimic
    • Hrmova M De Gori R Smith BJ Vasella A Varghese JN Fincher GB ( 2004) Three-dimensional structure of the barley β-d-glucan glucohydrolase in complex with a transition state mimic. J Biol Chem 279, 4970 4980.
    • (2004) J Biol Chem , vol.279 , pp. 4970-4980
    • Hrmova, M.1    De Gori, R.2    Smith, B.J.3    Vasella, A.4    Varghese, J.N.5    Fincher, G.B.6
  • 20
    • 0033897724 scopus 로고    scopus 로고
    • Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling
    • Cheng Q Li H Merdek K Park JT ( 2000) Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling. J Bacteriol 182, 4836 4840.
    • (2000) J Bacteriol , vol.182 , pp. 4836-4840
    • Cheng, Q.1    Li, H.2    Merdek, K.3    Park, J.T.4
  • 21
    • 0034671524 scopus 로고    scopus 로고
    • Characterization of a β-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction
    • Vötsch W Templin MF ( 2000) Characterization of a β-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction. J Biol Chem 275, 39032 39038.
    • (2000) J Biol Chem , vol.275 , pp. 39032-39038
    • Vötsch, W.1    Templin, M.F.2
  • 22
    • 0032714186 scopus 로고    scopus 로고
    • Physiological aspects of chitin catabolism in marine bacteria
    • Keyhani NO Roseman S ( 1999) Physiological aspects of chitin catabolism in marine bacteria. Biochim Biophys Acta 1473, 108 122.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 108-122
    • Keyhani, N.O.1    Roseman, S.2
  • 25
    • 0026315624 scopus 로고
    • Chitin utilization by marine bacteria. Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii
    • Bassler BL Yu C Lee YC Roseman S ( 1991) Chitin utilization by marine bacteria. Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii. J Biol Chem 266, 24276 24286.
    • (1991) J Biol Chem , vol.266 , pp. 24276-24286
    • Bassler, B.L.1    Yu, C.2    Lee, Y.C.3    Roseman, S.4
  • 27
    • 0029270304 scopus 로고
    • The action of Bacillus circulans WL-12 chitinases on partially N-acetylated chitosan
    • Mitsutomi M Kidoh H Tomita H Watanabe T ( 1995) The action of Bacillus circulans WL-12 chitinases on partially N-acetylated chitosan. Biosci Biotechnol Biochem 59, 529 531.
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 529-531
    • Mitsutomi, M.1    Kidoh, H.2    Tomita, H.3    Watanabe, T.4
  • 28
    • 0027401279 scopus 로고
    • Cellulose-binding polypeptides from Cellulomonas fimi: Endoglucanase D (CenD), a family a β-1,4-glucanase
    • Meinke A Gilkes NR Kilburn DG Miller RC Jr. Warren RA ( 1993) Cellulose-binding polypeptides from Cellulomonas fimi: endoglucanase D (CenD), a family A β-1,4-glucanase. J Bacteriol 175, 1910 1918.
    • (1993) J Bacteriol , vol.175 , pp. 1910-1918
    • Meinke, A.1    Gilkes, N.R.2    Kilburn, D.G.3    Miller Jr., R.C.4    Warren, R.A.5
  • 29
    • 0028180319 scopus 로고
    • Cellobiohydrolase a (CbhA) from the cellulolytic bacterium Cellulomonas fimi is a β-1,4-exocellobiohydrolase analogous to Trichoderma reesei CBH II
    • Meinke A Gilkes NR Kwan E Kilburn DG Warren RA Miller RC Jr. ( 1994) Cellobiohydrolase A (CbhA) from the cellulolytic bacterium Cellulomonas fimi is a β-1,4-exocellobiohydrolase analogous to Trichoderma reesei CBH II. Mol Microbiol 12, 413 422.
    • (1994) Mol Microbiol , vol.12 , pp. 413-422
    • Meinke, A.1    Gilkes, N.R.2    Kwan, E.3    Kilburn, D.G.4    Warren, R.A.5    Miller Jr., R.C.6
  • 30
    • 0029940470 scopus 로고    scopus 로고
    • Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease
    • Tews I Perrakis A Oppenheim A Dauter Z Wilson KS Vorgias CE ( 1996) Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat Struct Biol 3, 638 648.
    • (1996) Nat Struct Biol , vol.3 , pp. 638-648
    • Tews, I.1    Perrakis, A.2    Oppenheim, A.3    Dauter, Z.4    Wilson, K.S.5    Vorgias, C.E.6
  • 31
    • 0031727045 scopus 로고    scopus 로고
    • Cloning, characterization and expression of β-N- acetylglucosaminidase gene from Streptomyces thermoviolaceus OPC-520 (1)
    • Tsujibo H Hatano N Mikami T Izumizawa Y Miyamoto K Inamori Y ( 1998) Cloning, characterization and expression of β-N-acetylglucosaminidase gene from Streptomyces thermoviolaceus OPC-520 (1). Biochim Biophys Acta 1425, 437 440.
    • (1998) Biochim Biophys Acta , vol.1425 , pp. 437-440
    • Tsujibo, H.1    Hatano, N.2    Mikami, T.3    Izumizawa, Y.4    Miyamoto, K.5    Inamori, Y.6
  • 32
    • 0029988341 scopus 로고    scopus 로고
    • Substrate specificity of endoglucanase a from Cellulomonas fimi: Fundamental differences between endoglucanases and exoglucanases from family 6
    • Damude HG Ferro V Withers SG Warren RA ( 1996) Substrate specificity of endoglucanase A from Cellulomonas fimi: fundamental differences between endoglucanases and exoglucanases from family 6. Biochem J 315, 467 472.
    • (1996) Biochem J , vol.315 , pp. 467-472
    • Damude, H.G.1    Ferro, V.2    Withers, S.G.3    Warren, R.A.4
  • 33
    • 0028939503 scopus 로고
    • Site-directed mutation of the putative catalytic residues of endoglucanase CenA from Cellulomonas fimi
    • Damude HG Withers SG Kilburn DG Miller RC Jr. Warren RA ( 1995) Site-directed mutation of the putative catalytic residues of endoglucanase CenA from Cellulomonas fimi. Biochemistry 34, 2220 2224.
    • (1995) Biochemistry , vol.34 , pp. 2220-2224
    • Damude, H.G.1    Withers, S.G.2    Kilburn, D.G.3    Miller Jr., R.C.4    Warren, R.A.5
  • 35
    • 0026722420 scopus 로고
    • The tertiary structure of endo-β-1,4-glucanase B (CenB), a multidomain cellulase from the bacterium Cellulomonas fimi
    • Meinke A Schmuck M Gilkes NR Kilburn DG Miller RC Jr. Warren RA ( 1992) The tertiary structure of endo-β-1,4-glucanase B (CenB), a multidomain cellulase from the bacterium Cellulomonas fimi. Glycobiology 2, 321 326.
    • (1992) Glycobiology , vol.2 , pp. 321-326
    • Meinke, A.1    Schmuck, M.2    Gilkes, N.R.3    Kilburn, D.G.4    Miller Jr., R.C.5    Warren, R.A.6
  • 37
    • 0029128366 scopus 로고
    • Cellobiohydrolase B, a second exo-cellobiohydrolase from the cellulolytic bacterium Cellulomonas fimi
    • Shen H Gilkes NR Kilburn DG Miller RC Jr. Warren RA ( 1995) Cellobiohydrolase B, a second exo-cellobiohydrolase from the cellulolytic bacterium Cellulomonas fimi. Biochem J 311, 67 74.
    • (1995) Biochem J , vol.311 , pp. 67-74
    • Shen, H.1    Gilkes, N.R.2    Kilburn, D.G.3    Miller Jr., R.C.4    Warren, R.A.5
  • 38
    • 0029896866 scopus 로고    scopus 로고
    • Characterization of CenC, an enzyme from Cellulomonas fimi with both endo- and exoglucanase activities
    • Tomme P Kwan E Gilkes NR Kilburn DG Warren RA ( 1996) Characterization of CenC, an enzyme from Cellulomonas fimi with both endo- and exoglucanase activities. J Bacteriol 178, 4216 4223.
    • (1996) J Bacteriol , vol.178 , pp. 4216-4223
    • Tomme, P.1    Kwan, E.2    Gilkes, N.R.3    Kilburn, D.G.4    Warren, R.A.5
  • 39
    • 0031568840 scopus 로고    scopus 로고
    • Purification and characterization of an exo-N,N′- diacetylchitobiohydrolase-like enzyme from Cellulomonas flavigena NTOU1
    • Chen H-C Hsu M-F Jiang S-T ( 1997) Purification and characterization of an exo-N,N′-diacetylchitobiohydrolase-like enzyme from Cellulomonas flavigena NTOU1. Enzyme Microb Technol 20, 191 197.
    • (1997) Enzyme Microb Technol , vol.20 , pp. 191-197
    • Chen, H.-C.1    Hsu, M.-F.2    Jiang, S.-T.3
  • 40
    • 0347625654 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of ChiA, the major enzyme component for the solubilization of chitin by Cellulomonas uda
    • Reguera G Leschine SB ( 2003) Biochemical and genetic characterization of ChiA, the major enzyme component for the solubilization of chitin by Cellulomonas uda. Arch Microbiol 180, 434 443.
    • (2003) Arch Microbiol , vol.180 , pp. 434-443
    • Reguera, G.1    Leschine, S.B.2
  • 42
    • 0038413775 scopus 로고    scopus 로고
    • Bifunctional family 3 glycoside hydrolases from barley with α-1-arabinofuranosidase and β-d-xylosidase activity. Characterization, primary structures, and COOH-terminal processing
    • Lee RC Hrmova M Burton RA Lahnstein J Fincher GB ( 2003) Bifunctional family 3 glycoside hydrolases from barley with α-1-arabinofuranosidase and β-d-xylosidase activity. Characterization, primary structures, and COOH-terminal processing. J Biol Chem 278, 5377 5387.
    • (2003) J Biol Chem , vol.278 , pp. 5377-5387
    • Lee, R.C.1    Hrmova, M.2    Burton, R.A.3    Lahnstein, J.4    Fincher, G.B.5
  • 44
    • 21844464281 scopus 로고    scopus 로고
    • O-GlcNAcase uses substrate-assisted catalysis: Kinetic analysis and development of highly selective mechanism-inspired inhibitors
    • Macauley MS Whitworth GE Debowski AW Chin D Vocadlo DJ ( 2005) O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors. J Biol Chem 280, 25313 25122.
    • (2005) J Biol Chem , vol.280 , pp. 25313-25122
    • MacAuley, M.S.1    Whitworth, G.E.2    Debowski, A.W.3    Chin, D.4    Vocadlo, D.J.5
  • 45
    • 0033954715 scopus 로고    scopus 로고
    • The E358S mutant of Agrobacterium sp. β-glucosidase is a greatly improved glycosynthase
    • Mayer C Zechel DL Reid SP Warren RA Withers SG ( 2000) The E358S mutant of Agrobacterium sp. β-glucosidase is a greatly improved glycosynthase. FEBS Lett 466, 40 44.
    • (2000) FEBS Lett , vol.466 , pp. 40-44
    • Mayer, C.1    Zechel, D.L.2    Reid, S.P.3    Warren, R.A.4    Withers, S.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.