메뉴 건너뛰기




Volumn 2, Issue 1, 2012, Pages

Characterization of β-N-acetylhexosaminidase (LeHex20A), a member of glycoside hydrolase family 20, from Lentinula edodes (shiitake mushroom)

Author keywords

Basidiomycete; Chitin; Fungal cell wall; Glycoside hydrolase family 20; N acetylglucosaminide

Indexed keywords

BETA N ACETYLGALACTOSAMINIDE; BETA N ACETYLGLUCOSAMINIDE; BETA N ACETYLHEXOSAMINIDASE; CHITOBIOSE; GLYCOSIDASE; MONOSACCHARIDE; UNCLASSIFIED DRUG;

EID: 84863955492     PISSN: None     EISSN: 21910855     Source Type: Journal    
DOI: 10.1186/2191-0855-2-29     Document Type: Article
Times cited : (29)

References (45)
  • 1
    • 0029884662 scopus 로고    scopus 로고
    • Comparative studies of chitinases A and B from Serratia marcescens
    • Brurberg MB, Nes IF, Eijsink VG (1996) Comparative studies of chitinases A and B from Serratia marcescens. Microbiology 142:1581-1589
    • (1996) Microbiology , vol.142 , pp. 1581-1589
    • Brurberg, M.B.1    Nes, I.F.2    Eijsink, V.G.3
  • 2
    • 0028301746 scopus 로고
    • Molecular cloning and expression of the Candida albicans β-N-acetylglucosaminidase (HEX1) gene
    • Cannon RD, Niimi K, Jenkinson HF, Shepherd MG (1994) Molecular cloning and expression of the Candida albicans β-N-acetylglucosaminidase (HEX1) gene. J Bacteriol 176:2640-2647
    • (1994) J Bacteriol , vol.176 , pp. 2640-2647
    • Cannon, R.D.1    Niimi, K.2    Jenkinson, H.F.3    Shepherd, M.G.4
  • 4
    • 0028988019 scopus 로고
    • Cloning and expression of the β-Nacetylglucosaminidase gene from Streptococcus pneumoniae. Generation of truncated enzymes with modified aglycon specificity
    • Clarke VA, Platt N, Butters TD (1995) Cloning and expression of the β-Nacetylglucosaminidase gene from Streptococcus pneumoniae. Generation of truncated enzymes with modified aglycon specificity. J Biol Chem 270:8805-8814
    • (1995) J Biol Chem , vol.270 , pp. 8805-8814
    • Clarke, V.A.1    Platt, N.2    Butters, T.D.3
  • 5
    • 0031466989 scopus 로고    scopus 로고
    • Serratia marcescens chitobiase is a retaining glycosidase utilizing substrate acetamido group participation
    • Drouillard S, Armand S, Davies GJ, Vorgias CE, Henrissat B (1997) Serratia marcescens chitobiase is a retaining glycosidase utilizing substrate acetamido group participation. Biochem J 328:945-949
    • (1997) Biochem J , vol.328 , pp. 945-949
    • Drouillard, S.1    Armand, S.2    Davies, G.J.3    Vorgias, C.E.4    Henrissat, B.5
  • 7
    • 0025802824 scopus 로고
    • Comparison of four methods for measuring chitinase activity and the application of the 4-MUF assay in aquatic environments
    • Hood MA (1991) Comparison of four methods for measuring chitinase activity and the application of the 4-MUF assay in aquatic environments. J Microbiol Methods 13:151-160
    • (1991) J Microbiol Methods , vol.13 , pp. 151-160
    • Hood, M.A.1
  • 8
    • 0016632309 scopus 로고
    • Powdered chitin agar as a selective medium for enumeration of actinomycetes in water and soil
    • Hsu SC, Lockwood JL (1975) Powdered chitin agar as a selective medium for enumeration of actinomycetes in water and soil. Appl Microbiol 29:422-426
    • (1975) Appl Microbiol , vol.29 , pp. 422-426
    • Hsu, S.C.1    Lockwood, J.L.2
  • 9
    • 48749102098 scopus 로고    scopus 로고
    • Phylogenetic analyses suggest multiple changes of substrate specificity within the glycosyl hydrolase 20 family
    • Intra J, Pavesi G, Horner DS (2008) Phylogenetic analyses suggest multiple changes of substrate specificity within the glycosyl hydrolase 20 family. BMC Evol Biol 8:214
    • (2008) BMC Evol Biol , vol.8 , pp. 214
    • Intra, J.1    Pavesi, G.2    Horner, D.S.3
  • 10
    • 0343472049 scopus 로고
    • Role of chitinase and other lysosomal enzymes of Coprinus Zagopus in the autolysis of fruiting bodies
    • Iten W, Matile P (1970) Role of chitinase and other lysosomal enzymes of Coprinus Zagopus in the autolysis of fruiting bodies. J Gen Microbiol 61:301-309
    • (1970) J Gen Microbiol , vol.61 , pp. 301-309
    • Iten, W.1    Matile, P.2
  • 11
    • 0019289005 scopus 로고
    • Purification, properties, kinetics, and mechanism of β-Nacetylglucosamidase from Aspergillus niger
    • Jones CS, Kosman DJ (1980) Purification, properties, kinetics, and mechanism of β-Nacetylglucosamidase from Aspergillus niger. J Biol Chem 255:11861-11869
    • (1980) J Biol Chem , vol.255 , pp. 11861-11869
    • Jones, C.S.1    Kosman, D.J.2
  • 12
    • 0019915216 scopus 로고
    • Autolysis in vitro of the stipe cell wall in Coprinus macrorhizus
    • Kamada T, Hamada Y, Takemaru T (1982) Autolysis in vitro of the stipe cell wall in Coprinus macrorhizus. Microbiology 128:1041-1046
    • (1982) Microbiology , vol.128 , pp. 1041-1046
    • Kamada, T.1    Hamada, Y.2    Takemaru, T.3
  • 13
    • 0030447616 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic β-Nacetylglucosaminidase
    • Keyhani NO, Roseman S (1996) The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic β-Nacetylglucosaminidase. J Biol Chem 271:33425-33434
    • (1996) J Biol Chem , vol.271 , pp. 33425-33434
    • Keyhani, N.O.1    Roseman, S.2
  • 14
    • 1842837225 scopus 로고    scopus 로고
    • Cloning and characterization of the nagA gene that encodes β-N-acetylglucosaminidase from Aspergillus nidulans and its expression in Aspergillus oryzae
    • Kim S, Matsuo I, Ajisaka K, Nakajima H, Kitamoto K (2002) Cloning and characterization of the nagA gene that encodes β-N-acetylglucosaminidase from Aspergillus nidulans and its expression in Aspergillus oryzae. Biosci Biotechnol Biochem 66:2168-2175
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 2168-2175
    • Kim, S.1    Matsuo, I.2    Ajisaka, K.3    Nakajima, H.4    Kitamoto, K.5
  • 15
    • 0030087991 scopus 로고    scopus 로고
    • Purification and characterization of β-N-acetylhexosaminidase from the liver of a prawn, Penaeus japonicus
    • Koga D, Hoshika H, Matsushita M, Tanaka A, Ide A, Kono M (1996) Purification and characterization of β-N-acetylhexosaminidase from the liver of a prawn, Penaeus japonicus. Biosci Biotechnol Biochem 60:194-199
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 194-199
    • Koga, D.1    Hoshika, H.2    Matsushita, M.3    Tanaka, A.4    Ide, A.5    Kono, M.6
  • 16
    • 80052635742 scopus 로고    scopus 로고
    • An endo-β-1,6-glucanase involved in Lentinula edodes fruiting body autolysis
    • Konno N, Sakamoto Y (2011) An endo-β-1,6-glucanase involved in Lentinula edodes fruiting body autolysis. Appl Microbiol Biotechnol 91:1365-1373
    • (2011) Appl Microbiol Biotechnol , vol.91 , pp. 1365-1373
    • Konno, N.1    Sakamoto, Y.2
  • 18
    • 18844476379 scopus 로고    scopus 로고
    • Life history and developmental processes in the basidiomycete Coprinus cinereus
    • Kües U (2000) Life history and developmental processes in the basidiomycete Coprinus cinereus. Microbiol Mol Biol Rev 64:316-353
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 316-353
    • Kües, U.1
  • 19
    • 69449098260 scopus 로고    scopus 로고
    • The β-Nacetylglucosaminidases NAG1 and NAG2 are essential for growth of Trichoderma atroviride on chitin
    • López-Mondéjar R, Catalano V, Kubicek CP, Seidl V (2009) The β-Nacetylglucosaminidases NAG1 and NAG2 are essential for growth of Trichoderma atroviride on chitin. FEBS J 276:5137-5148
    • (2009) FEBS J , vol.276 , pp. 5137-5148
    • López-Mondéjar, R.1    Catalano, V.2    Kubicek, C.P.3    Seidl, V.4
  • 20
  • 21
    • 33745216253 scopus 로고    scopus 로고
    • Characterization of a β-N-acetylhexosaminidase and a β-N-acetylglucosaminidase/β-glucosidase from Cellulomonas fimi
    • Mayer C, Vocadlo DJ, Mah M, Rupitz K, Stoll D, Warren RA, Withers SG (2006) Characterization of a β-N-acetylhexosaminidase and a β-N-acetylglucosaminidase/β-glucosidase from Cellulomonas fimi. FEBS J 273:2929-2941
    • (2006) FEBS J , vol.273 , pp. 2929-2941
    • Mayer, C.1    Vocadlo, D.J.2    Mah, M.3    Rupitz, K.4    Stoll, D.5    Warren, R.A.6    Withers, S.G.7
  • 23
    • 2942638057 scopus 로고    scopus 로고
    • An exo β-1,3 glucanase synthesized de novo dgrades lentinan during storage of Lentinula edodes and diminishes immunomodulationg activity of the mushroom
    • Minato K, Kawakami S, Nomura K, Tsuchida H, Mizuno M (2004) An exo β-1,3 glucanase synthesized de novo dgrades lentinan during storage of Lentinula edodes and diminishes immunomodulationg activity of the mushroom. Carbohydr Polym 56:279-286
    • (2004) Carbohydr Polym , vol.56 , pp. 279-286
    • Minato, K.1    Kawakami, S.2    Nomura, K.3    Tsuchida, H.4    Mizuno, M.5
  • 24
    • 0013871030 scopus 로고
    • Autolytic enzymes in fungal cell walls
    • Mitchell R, Sabar N (1966) Autolytic enzymes in fungal cell walls. J Gen Microbiol 42:39-42
    • (1966) J Gen Microbiol , vol.42 , pp. 39-42
    • Mitchell, R.1    Sabar, N.2
  • 25
    • 0141814841 scopus 로고    scopus 로고
    • Important role of fungal intracellular laccase for melanin synthesis: Purification and characterization of an intracellular laccase from Lentinula edodes fruit bodies
    • Nagai M, Kawata M, Watanabe H, Ogawa M, Saito K, Takesawa T, Kanda K, Sato T (2003) Important role of fungal intracellular laccase for melanin synthesis: purification and characterization of an intracellular laccase from Lentinula edodes fruit bodies. Microbiology 149:2455-2462
    • (2003) Microbiology , vol.149 , pp. 2455-2462
    • Nagai, M.1    Kawata, M.2    Watanabe, H.3    Ogawa, M.4    Saito, K.5    Takesawa, T.6    Kanda, K.7    Sato, T.8
  • 26
    • 78650521845 scopus 로고    scopus 로고
    • Development of innovative technologies to decrease the environmental burdens associated with using chitin as a biomass resource: Mechanochemical grinding and enzymatic degradation
    • Nakagawa YS, Oyama Y, Kon N, Nikaido M, Tanno K, Kogawa J, Inomata S, Masui A, Yamamura A, Kawaguchi M, Matahira Y, Totani K (2011) Development of innovative technologies to decrease the environmental burdens associated with using chitin as a biomass resource: mechanochemical grinding and enzymatic degradation. Carbohydr Polym 83:1843-1849
    • (2011) Carbohydr Polym , vol.83 , pp. 1843-1849
    • Nakagawa, Y.S.1    Oyama, Y.2    Kon, N.3    Nikaido, M.4    Tanno, K.5    Kogawa, J.6    Inomata, S.7    Masui, A.8    Yamamura, A.9    Kawaguchi, M.10    Matahira, Y.11    Totani, K.12
  • 27
    • 0029799714 scopus 로고    scopus 로고
    • Molecular cloning and expression of the nag1 gene (N-acetyl-β-D-glucosaminidase-encoding gene) from Trichoderma harzianum P1
    • Peterbauer CK, Lorito M, Hayes CK, Harman GE, Kubicek CP (1996) Molecular cloning and expression of the nag1 gene (N-acetyl-β-D-glucosaminidase-encoding gene) from Trichoderma harzianum P1. Curr Genet 30:325-331
    • (1996) Curr Genet , vol.30 , pp. 325-331
    • Peterbauer, C.K.1    Lorito, M.2    Hayes, C.K.3    Harman, G.E.4    Kubicek, C.P.5
  • 28
    • 0026331471 scopus 로고
    • A complex chitinolytic system in exponentially growing mycelium of Mucor rouxii: Properties and function
    • Rast DM, Horsch M, Furter R, Gooday GW (1991) A complex chitinolytic system in exponentially growing mycelium of Mucor rouxii: properties and function. J Gen Microbiol 137:2797-2810
    • (1991) J Gen Microbiol , vol.137 , pp. 2797-2810
    • Rast, D.M.1    Horsch, M.2    Furter, R.3    Gooday, G.W.4
  • 29
    • 23844527848 scopus 로고    scopus 로고
    • Isolation and characterization of a fruiting body-specific exo-β-1,3-glucanase-encoding gene, exg1, from Lentinula edodes
    • Sakamoto Y, Irie T, Sato T (2005a) Isolation and characterization of a fruiting body-specific exo-β-1,3-glucanase-encoding gene, exg1, from Lentinula edodes. Curr Genet 47:244-252
    • (2005) Curr Genet , vol.47 , pp. 244-252
    • Sakamoto, Y.1    Irie, T.2    Sato, T.3
  • 30
    • 27644531604 scopus 로고    scopus 로고
    • Characterization of the Lentinula edodes exg2 gene encoding a lentinan-degrading exo-β-1,3-glucanase
    • Sakamoto Y, Minato K, Nagai M, Kawakami S, Mizuno M, Sato T (2005b) Characterization of the Lentinula edodes exg2 gene encoding a lentinan-degrading exo-β-1,3-glucanase. Curr Genet 48:195-203
    • (2005) Curr Genet , vol.48 , pp. 195-203
    • Sakamoto, Y.1    Minato, K.2    Nagai, M.3    Kawakami, S.4    Mizuno, M.5    Sato, T.6
  • 31
    • 33745674717 scopus 로고    scopus 로고
    • Lentinula edodes tlg1 encodes a thaumatin-like protein that is involved in lentinan degradation and fruiting body senescence
    • Sakamoto Y, Watanabe H, Nagai M, Nakade K, Takahashi M, Sato T (2006) Lentinula edodes tlg1 encodes a thaumatin-like protein that is involved in lentinan degradation and fruiting body senescence. Plant Physiol 141:793-801
    • (2006) Plant Physiol , vol.141 , pp. 793-801
    • Sakamoto, Y.1    Watanabe, H.2    Nagai, M.3    Nakade, K.4    Takahashi, M.5    Sato, T.6
  • 32
    • 68649094186 scopus 로고    scopus 로고
    • Characterization of the post-harvest changes in gene transcription in the gill of the Lentinula edodes fruiting body
    • Sakamoto Y, Nakade K, Sato T (2009) Characterization of the post-harvest changes in gene transcription in the gill of the Lentinula edodes fruiting body. Curr Genet 55:409-423
    • (2009) Curr Genet , vol.55 , pp. 409-423
    • Sakamoto, Y.1    Nakade, K.2    Sato, T.3
  • 33
    • 83255186866 scopus 로고    scopus 로고
    • Endo-β-1,3-glucanase GLU1, from the fruiting body of Lentinula edodes, belongs to a new glycoside hydrolase family
    • Sakamoto Y, Nakade K, Konno N (2011) Endo-β-1,3-glucanase GLU1, from the fruiting body of Lentinula edodes, belongs to a new glycoside hydrolase family. Appl Environ Microbiol 77:8350-8354
    • (2011) Appl Environ Microbiol , vol.77 , pp. 8350-8354
    • Sakamoto, Y.1    Nakade, K.2    Konno, N.3
  • 34
    • 33746052090 scopus 로고    scopus 로고
    • A screening system for carbon sources enhancing β-N-acetylglucosaminidase formation in Hypocrea atroviridis (Trichoderma atroviride)
    • Seidl V, Druzhinina IS, Kubicek CP (2006) A screening system for carbon sources enhancing β-N-acetylglucosaminidase formation in Hypocrea atroviridis (Trichoderma atroviride). Microbiology 152:2003-2012
    • (2006) Microbiology , vol.152 , pp. 2003-2012
    • Seidl, V.1    Druzhinina, I.S.2    Kubicek, C.P.3
  • 35
    • 0345687346 scopus 로고    scopus 로고
    • The genetic basis of cellular morphogenesis in the filamentous fungus Neurospora crassa
    • Seiler S, Plamann M (2003) The genetic basis of cellular morphogenesis in the filamentous fungus Neurospora crassa. Mol Biol Cell 14:4352-4364
    • (2003) Mol Biol Cell , vol.14 , pp. 4352-4364
    • Seiler, S.1    Plamann, M.2
  • 36
    • 0019630839 scopus 로고
    • Structure of the alkali-insoluble skeletal glucan of Lentinus edodes
    • Shida M, Ushioda Y, Nakajima T, Matsuda K (1981) Structure of the alkali-insoluble skeletal glucan of Lentinus edodes. J Biochem 90:1093-1100
    • (1981) J Biochem , vol.90 , pp. 1093-1100
    • Shida, M.1    Ushioda, Y.2    Nakajima, T.3    Matsuda, K.4
  • 37
    • 66149153866 scopus 로고    scopus 로고
    • Differential roles of the ChiB chitinase in autolysis and cell death of Aspergillus nidulans
    • Shin KS, Kwon NJ, Kim YH, Park HS, Kwon GS, Yu JH (2009) Differential roles of the ChiB chitinase in autolysis and cell death of Aspergillus nidulans. Eukaryot Cell 8:738-746
    • (2009) Eukaryot Cell , vol.8 , pp. 738-746
    • Shin, K.S.1    Kwon, N.J.2    Kim, Y.H.3    Park, H.S.4    Kwon, G.S.5    Yu, J.H.6
  • 38
    • 0017838045 scopus 로고
    • Purification and characterization of β-D-mannosidase and β-Nacetyl-D-hexosaminidase of Tremella fuciformis
    • Sone Y, Misaki A (1978) Purification and characterization of β-D-mannosidase and β-Nacetyl-D-hexosaminidase of Tremella fuciformis. J Biochem 83:1135-1144
    • (1978) J Biochem , vol.83 , pp. 1135-1144
    • Sone, Y.1    Misaki, A.2
  • 39
    • 77957172631 scopus 로고    scopus 로고
    • Novel β-N-acetylglucosaminidases from Vibrio harveyi 650: Cloning, expression, enzymatic properties, and subsite identification
    • Suginta W, Chuenark D, Mizuhara M, Fukamizo T (2010) Novel β-N-acetylglucosaminidases from Vibrio harveyi 650: cloning, expression, enzymatic properties, and subsite identification. BMC Biochem 11:40
    • (2010) BMC Biochem , vol.11 , pp. 40
    • Suginta, W.1    Chuenark, D.2    Mizuhara, M.3    Fukamizo, T.4
  • 40
    • 0035929579 scopus 로고    scopus 로고
    • Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Tanaka T, Fukui T, Imanaka T (2001) Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J Biol Chem 276:35629-35635
    • (2001) J Biol Chem , vol.276 , pp. 35629-35635
    • Tanaka, T.1    Fukui, T.2    Imanaka, T.3
  • 41
    • 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
  • 42
    • 0001558035 scopus 로고
    • Purification and some properties of β-N-Acetylglucosaminidase from Aeromonas sp. 10S-24
    • Ueda M, Arai M (1992) Purification and some properties of β-N-Acetylglucosaminidase from Aeromonas sp. 10S-24. Biosci Biotechnol Biochem 56:1204-1207
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 1204-1207
    • Ueda, M.1    Arai, M.2
  • 43
    • 33751532123 scopus 로고    scopus 로고
    • Chitin content of cultivated mushrooms Agaricus bisporus, Pleurotus ostreatus and Lentinula edodes
    • Vetter J (2007) Chitin content of cultivated mushrooms Agaricus bisporus, Pleurotus ostreatus and Lentinula edodes. Food Chem Volume 102:6-9
    • (2007) Food Chem Volume , vol.102 , pp. 6-9
    • Vetter, J.1
  • 44
    • 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
  • 45
    • 54849434406 scopus 로고    scopus 로고
    • A novel β-N-acetyl-D-hexosaminidase from the insect Ostrinia furnacalis (Guenée)
    • Yang Q, Liu T, Liu F, Qu M, Qian X (2008) A novel β-N-acetyl-D-hexosaminidase from the insect Ostrinia furnacalis (Guenée). FEBS J 275:5690-5702
    • (2008) FEBS J , vol.275 , pp. 5690-5702
    • Yang, Q.1    Liu, T.2    Liu, F.3    Qu, M.4    Qian, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.