메뉴 건너뛰기




Volumn 185, Issue 17, 2003, Pages 5175-5181

Characterization of an exo-β-D-glucosaminidase involved in a novel chitinolytic pathway from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1

Author keywords

[No Author keywords available]

Indexed keywords

BETA GLYCOSYL HYDROLASE; CHITIN; CHITINASE; CHITOSE OLIGOSACCHARIDE; EXOGLUCOSAMINIDASE; GENE PRODUCT; GLUCOSAMINIDASE; OLIGOSACCHARIDE; PROTEIN KOD1; UNCLASSIFIED DRUG;

EID: 0042890412     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.17.5175-5181.2003     Document Type: Article
Times cited : (92)

References (36)
  • 1
    • 0028819234 scopus 로고
    • Tomato exo-(1-→4)-β-D-galactanase. Isolation, changes during ripening in normal and mutant tomato fruit, and characterization of a related cDNA clone
    • Carey, A. T., K. Holt, S. Picard, R. Wilde, G. A. Tucker, C. R. Bird, W. Schuch, and G. B. Seymour. 1995. Tomato exo-(1-→4)-β-D-galactanase. Isolation, changes during ripening in normal and mutant tomato fruit, and characterization of a related cDNA clone. Plant Physiol. 108:1099-1107.
    • (1995) Plant Physiol. , vol.108 , pp. 1099-1107
    • Carey, A.T.1    Holt, K.2    Picard, S.3    Wilde, R.4    Tucker, G.A.5    Bird, C.R.6    Schuch, W.7    Seymour, G.B.8
  • 2
    • 0032729449 scopus 로고    scopus 로고
    • Biochemical and phylogenetic analyses of a cold-active β-galactosidase from the lactic acid bacterium Carnobacterium piscicola BA
    • Coombs, J. M., and J. E. Brenchley. 1999. Biochemical and phylogenetic analyses of a cold-active β-galactosidase from the lactic acid bacterium Carnobacterium piscicola BA. Appl. Environ. Microbiol. 65:5443-5450.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5443-5450
    • Coombs, J.M.1    Brenchley, J.E.2
  • 3
    • 0033027296 scopus 로고    scopus 로고
    • Relationship between glycosyl hydrolase inventory and growth physiology of the hyperthermophile Pyrococcus furiosus on carbohydrate-based media
    • Driskill, L. E., K. Kusy, M. W. Bauer, and R. M. Kelly. 1999. Relationship between glycosyl hydrolase inventory and growth physiology of the hyperthermophile Pyrococcus furiosus on carbohydrate-based media. Appl. Environ. Microbiol. 65:893-897.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 893-897
    • Driskill, L.E.1    Kusy, K.2    Bauer, M.W.3    Kelly, R.M.4
  • 5
    • 0000630352 scopus 로고
    • Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate
    • Ghosh, S., H. J. Blumenthal, E. Davidson, and S. Roseman. 1960. Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate. J. Biol. Chem 235:1265-1273.
    • (1960) J. Biol. Chem. , vol.235 , pp. 1265-1273
    • Ghosh, S.1    Blumenthal, H.J.2    Davidson, E.3    Roseman, S.4
  • 6
    • 0002256521 scopus 로고
    • Physiology of microbial degradation of chitin and chitosan
    • C. Ratledge (ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Gooday, G. W. 1994. Physiology of microbial degradation of chitin and chitosan, p. 279-312. In C. Ratledge (ed.), Biochemistry of microbial degradation. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1994) Biochemistry of Microbial Degradation , pp. 279-312
    • Gooday, G.W.1
  • 7
    • 0030971550 scopus 로고    scopus 로고
    • A novel Arthrobacter β-galactosidase with homology to eukaryotic β-galactosidases
    • Gutshall, K., K. Wang, and J. E. Brenchley. 1997. A novel Arthrobacter β-galactosidase with homology to eukaryotic β-galactosidases. J. Bacteriol. 179:3064-3067.
    • (1997) J. Bacteriol. , vol.179 , pp. 3064-3067
    • Gutshall, K.1    Wang, K.2    Brenchley, J.E.3
  • 8
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • Henrissat, B., I. Callebaut, S. Fabrega, P. Lehn, J. P. Mornon, and G. Davies. 1995. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. USA 92:7090-7094.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.P.5    Davies, G.6
  • 9
    • 0022641866 scopus 로고
    • Structure of a β-galactosidase gene of Bacillus stearothermophilus
    • Hirata, H., T. Fukazawa, S. Negoro, and H. Okada. 1986. Structure of a β-galactosidase gene of Bacillus stearothermophilus. J. Bacteriol. 166:722-727.
    • (1986) J. Bacteriol. , vol.166 , pp. 722-727
    • Hirata, H.1    Fukazawa, T.2    Negoro, S.3    Okada, H.4
  • 10
    • 0034128505 scopus 로고    scopus 로고
    • Sequence and expression of a halobacterial β-galactosidase gene
    • Holmes, M. L., and M. L. Dyall-Smith. 2000. Sequence and expression of a halobacterial β-galactosidase gene. Mol. Microbiol. 36:114-122.
    • (2000) Mol. Microbiol. , vol.36 , pp. 114-122
    • Holmes, M.L.1    Dyall-Smith, M.L.2
  • 11
    • 0035464187 scopus 로고    scopus 로고
    • Molecular and biochemical analysis of two β-galactosidases from Bifidobacterium infantis HL96
    • Hung, M. N., Z. Xia, N. T. Hu, and B. H. Lee. 2001. Molecular and biochemical analysis of two β-galactosidases from Bifidobacterium infantis HL96. Appl. Environ. Microbiol. 67:4256-4263.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 4256-4263
    • Hung, M.N.1    Xia, Z.2    Hu, N.T.3    Lee, B.H.4
  • 12
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto, T., and K. Yagishita. 1971. A simple activity measurement of lysozyme. Agric. Biol. Chem. 35:1154-1156.
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 13
    • 0031201761 scopus 로고    scopus 로고
    • Cloning and characterization of the gene encoding a novel β-galactosidase from Bacillus circulans
    • Ito, Y., and T. Sasaki. 1997. Cloning and characterization of the gene encoding a novel β-galactosidase from Bacillus circulans. Biosci. Biotechnol. Biochem. 61:1270-1276.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1270-1276
    • Ito, Y.1    Sasaki, T.2
  • 15
    • 0031473543 scopus 로고    scopus 로고
    • Wild-type Escherichia coli grows on the chitin disaccharide, N,N′-diacetylchitobiose, by expressing the cel operon
    • Keyhani, N. O., and S. Roseman. 1997. Wild-type Escherichia coli grows on the chitin disaccharide, N,N′-diacetylchitobiose, by expressing the cel operon. Proc. Natl. Acad. Sci. USA 94:14367-14371.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14367-14371
    • Keyhani, N.O.1    Roseman, S.2
  • 16
    • 0034693218 scopus 로고    scopus 로고
    • The chitin disaccharide, N,N′-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system
    • Keyhani, N. O., L. X. Wang, Y. C. Lee, and S. Roseman. 2000. The chitin disaccharide, N,N′-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system. J. Biol. Chem. 275:33084-33090.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33084-33090
    • Keyhani, N.O.1    Wang, L.X.2    Lee, Y.C.3    Roseman, S.4
  • 17
    • 0034529961 scopus 로고    scopus 로고
    • Biochemical characterization, cloning, and sequencing of ADP-dependent (AMP-forming) glucokinase from two hyperthermophilic archaea, Pyrococcus furiosus and Thermococcus litoralis
    • Koga, S., I. Yoshioka, H. Sakuraba, M. Takahashi, S. Sakasegawa, S. Shimizu, and T. Ohshima. 2000. Biochemical characterization, cloning, and sequencing of ADP-dependent (AMP-forming) glucokinase from two hyperthermophilic archaea, Pyrococcus furiosus and Thermococcus litoralis. J. Biochem. (Tokyo) 128:1079-1085.
    • (2000) J. Biochem. (Tokyo) , vol.128 , pp. 1079-1085
    • Koga, S.1    Yoshioka, I.2    Sakuraba, H.3    Takahashi, M.4    Sakasegawa, S.5    Shimizu, S.6    Ohshima, T.7
  • 18
    • 0036952134 scopus 로고    scopus 로고
    • Characterization of two noncellulosomal subunits, ArfA and BgaA, from Clostridium cellulovorans that cooperate with the cellulosome in plant cell wall degradation
    • Kosugi, A., K. Murashima, and R. H. Doi. 2002. Characterization of two noncellulosomal subunits, ArfA and BgaA, from Clostridium cellulovorans that cooperate with the cellulosome in plant cell wall degradation. J. Bacteriol. 184:6859-6865.
    • (2002) J. Bacteriol. , vol.184 , pp. 6859-6865
    • Kosugi, A.1    Murashima, K.2    Doi, R.H.3
  • 19
    • 14744287752 scopus 로고
    • Saccharomyces cerevisiae cells secreting an Aspelgillus niger β-galactosidase grow on whey permeate
    • Kumar, V., S. Ramakrishnan, T. T. Teeri, J. K. Knowles, and B. S. Hartley. 1992. Saccharomyces cerevisiae cells secreting an Aspelgillus niger β-galactosidase grow on whey permeate. Bio/Technology (N.Y.) 10:82-85.
    • (1992) Bio/Technology (N.Y.) , vol.10 , pp. 82-85
    • Kumar, V.1    Ramakrishnan, S.2    Teeri, T.T.3    Knowles, J.K.4    Hartley, B.S.5
  • 20
    • 0033024997 scopus 로고    scopus 로고
    • One-step preparation of alkyl-β-D-glucosaminide by the transglycosylation of chitosan and alcohol using purified exo-β-D-glucosaminidase
    • Matsumura, S., E. Yao, and K. Toshima. 1999. One-step preparation of alkyl-β-D-glucosaminide by the transglycosylation of chitosan and alcohol using purified exo-β-D-glucosaminidase. Biotechnol. Lett. 21:451-456.
    • (1999) Biotechnol. Lett. , vol.21 , pp. 451-456
    • Matsumura, S.1    Yao, E.2    Toshima, K.3
  • 21
    • 0025695020 scopus 로고
    • Molecular cloning of mouse acid β-galactosidase cDNA: Sequence, expression of catalytic activity and comparison with the human enzyme
    • Nanba, E., and K. Suzuki. 1990. Molecular cloning of mouse acid β-galactosidase cDNA: sequence, expression of catalytic activity and comparison with the human enzyme. Biochem. Biophys. Res. Commun. 173:141-148.
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 141-148
    • Nanba, E.1    Suzuki, K.2
  • 22
    • 0025329913 scopus 로고
    • Purification and characterization of an exo-β-D-glucosaminidase, a novel type of enzyme, from Nocardia orientalis
    • Nanjo, F., R. Katsumi, and K. Sakai. 1990. Purification and characterization of an exo-β-D-glucosaminidase, a novel type of enzyme, from Nocardia orientalis. J. Biol. Chem. 265:10088-10094.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10088-10094
    • Nanjo, F.1    Katsumi, R.2    Sakai, K.3
  • 23
    • 0027205157 scopus 로고
    • Molecular cloning and analysis of the NAG1 cDNA coding for glucosamine-6-phosphate deaminase from Candida albicans
    • Natarajan, K., and A. Datta. 1993. Molecular cloning and analysis of the NAG1 cDNA coding for glucosamine-6-phosphate deaminase from Candida albicans. J. Biol. Chem. 268:9206-9214.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9206-9214
    • Natarajan, K.1    Datta, A.2
  • 25
    • 0031951409 scopus 로고    scopus 로고
    • Purification and characterization of exo-β-D-glucosaminidase from a cellulolytic fungus, Trichoderma reesei PC-3-7
    • Nogawa, M., H. Takahashi, A. Kashiwagi, K. Ohshima, H. Okada, and Y. Morikawa. 1998. Purification and characterization of exo-β-D-glucosaminidase from a cellulolytic fungus, Trichoderma reesei PC-3-7. Appl. Environ. Microbiol. 64:890-895.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 890-895
    • Nogawa, M.1    Takahashi, H.2    Kashiwagi, A.3    Ohshima, K.4    Okada, H.5    Morikawa, Y.6
  • 26
    • 0032135068 scopus 로고    scopus 로고
    • Thermostable β-galactosidase from an extreme thermophile, Thermus sp. A4: Enzyme purification and characterization, and gene cloning and sequencing
    • Ohtsu, N., H. Motoshima, K. Goto, F. Tsukasaki, and H. Matsuzawa. 1998. Thermostable β-galactosidase from an extreme thermophile, Thermus sp. A4: enzyme purification and characterization, and gene cloning and sequencing. Biosci. Biotechnol. Biochem. 62:1539-1545.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1539-1545
    • Ohtsu, N.1    Motoshima, H.2    Goto, K.3    Tsukasaki, F.4    Matsuzawa, H.5
  • 28
    • 0001547692 scopus 로고    scopus 로고
    • Chitin catabolism in the marine bacterium Vibrio furnissii. Identification, molecular cloning, and characterization of a N,N′-diacetylchitobiose phosphorylase
    • Park, J. K., N. O. Keyhani, and S. Roseman. 2000 Chitin catabolism in the marine bacterium Vibrio furnissii. Identification, molecular cloning, and characterization of a N,N′-diacetylchitobiose phosphorylase. J. Biol. Chem. 275:33077-33083.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33077-33083
    • Park, J.K.1    Keyhani, N.O.2    Roseman, S.3
  • 29
    • 0028518730 scopus 로고
    • Apple β-galactosidase. Activity against cell wall polysaccharides and characterization of a related cDNA clone
    • Ross, G. S., T. Wegrzyn, E. A. MacRae, and R. J. Redgwell. 1994. Apple β-galactosidase. Activity against cell wall polysaccharides and characterization of a related cDNA clone. Plant Physiol. 106:521-528.
    • (1994) Plant Physiol. , vol.106 , pp. 521-528
    • Ross, G.S.1    Wegrzyn, T.2    MacRae, E.A.3    Redgwell, R.J.4
  • 31
    • 0034080264 scopus 로고    scopus 로고
    • Characterization of a salt-tolerant family 42 β-galactosidase from a psychrophilic antarctic Planococcus isolate
    • Sheridan, P. P., and J. E. Brenchley. 2000. Characterization of a salt-tolerant family 42 β-galactosidase from a psychrophilic antarctic Planococcus isolate. Appl. Environ. Microbiol. 66:2438-2444.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2438-2444
    • Sheridan, P.P.1    Brenchley, J.E.2
  • 32
    • 0032728411 scopus 로고    scopus 로고
    • A unique chitinase with dual active sites and triple substrate binding sites from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1
    • Tanaka, T., S. Fujiwara, S. Nishikori, T. Fukui, M. Takagi, and T. Imanaka. 1999. A unique chitinase with dual active sites and triple substrate binding sites from the hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1. Appl. Environ. Microbiol. 65:5338-5344.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5338-5344
    • Tanaka, T.1    Fujiwara, S.2    Nishikori, S.3    Fukui, T.4    Takagi, M.5    Imanaka, T.6
  • 33
    • 0035929579 scopus 로고    scopus 로고
    • Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon kodakaraensis KOD1
    • Tanaka, T., T. Fukui, and T. Imanaka. 2001. Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon 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
  • 34
    • 0028971947 scopus 로고
    • A novel β-galactosidase gene isolated from the bacterium Xanthomonas manihotis exhibits strong homology to several eukaryotic β-galactosidases
    • Taron, C. H., J. S. Benner, L. J. Hornstra, and E. P. Guthrie. 1995. A novel β-galactosidase gene isolated from the bacterium Xanthomonas manihotis exhibits strong homology to several eukaryotic β-galactosidases. Glycobiology 5:603-610.
    • (1995) Glycobiology , vol.5 , pp. 603-610
    • Taron, C.H.1    Benner, J.S.2    Hornstra, L.J.3    Guthrie, E.P.4
  • 35
    • 0031777568 scopus 로고    scopus 로고
    • Structure of the β-galactosidase gene from Thermus sp. strain T2: Expression in Escherichia coli and purification in a single step of an active fusion protein
    • Vian, A., A. V, Carrascosa, J. L. García, and E. Cortés. 1998. Structure of the β-galactosidase gene from Thermus sp. strain T2: expression in Escherichia coli and purification in a single step of an active fusion protein. Appl. Environ. Microbiol. 64:2187-2191.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2187-2191
    • Vian A.Carrascosa, A.V.1    García, J.L.2    Cortés, E.3
  • 36
    • 0034279420 scopus 로고    scopus 로고
    • Purification and characterization of chitosanase and exo-β-D-glucosaminidase from a koji mold, Aspergillus oryzae IAM2660
    • Zhang, X. Y., A. L. Dai, X. K. Zhang, K. Kuroiwa, R. Kodaira, M. Shimosaka, and M. Okazaki. 2000. Purification and characterization of chitosanase and exo-β-D-glucosaminidase from a koji mold, Aspergillus oryzae IAM2660. Biosci. Biotechnol. Biochem. 64:1896-1902.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1896-1902
    • Zhang, X.Y.1    Dai, A.L.2    Zhang, X.K.3    Kuroiwa, K.4    Kodaira, R.5    Shimosaka, M.6    Okazaki, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.