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Volumn 185, Issue 11, 2003, Pages 3352-3360

Genomic analysis and initial characterization of the chitinolytic system of Microbulbifer degradans strain 2-40

Author keywords

[No Author keywords available]

Indexed keywords

4 METHYLUMBELLIFERYL BETA DEXTRO N,N' DIACETYLCHITOBIOSIDE; 4 METHYLUMBELLIFERYL BETA DEXTRO N,N',N'' TRIACETYLCHITOTRIOSIDE; BACTERIAL ENZYME; CHITIN; CHITIN BINDING PROTEIN; CHITIN DEPOLYMERASE; CHITIN DERIVATIVE; CHITINASE; CHITODEXTRINASE; CYTOPLASM PROTEIN; GLUTAMIC ACID; GLYCOSIDASE; N ACETYL BETA GLUCOSAMINIDASE; N ACETYLGLUCOSAMINE; PROTEIN CHIA; PROTEIN CHIB; PROTEIN CHIC; UNCLASSIFIED DRUG;

EID: 0038191046     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.11.3352-3360.2003     Document Type: Article
Times cited : (63)

References (52)
  • 2
    • 0009694866 scopus 로고
    • Isolation of a new polysaccharide digesting bacterium from a salt marsh
    • Andrykovich, G., and I. Marx. 1988. Isolation of a new polysaccharide digesting bacterium from a salt marsh. Appl. Microbiol. Biotechnol. 54:1061-1062.
    • (1988) Appl. Microbiol. Biotechnol. , vol.54 , pp. 1061-1062
    • Andrykovich, G.1    Marx, I.2
  • 3
    • 0036187913 scopus 로고    scopus 로고
    • Extensive feature detection of N-terminal protein sorting signals
    • Bannai, H., Y. Tamada, O. Maruyama, K. Nakai, and S. Miyano. 2002. Extensive feature detection of N-terminal protein sorting signals. Bioinformatics 18:298-305.
    • (2002) Bioinformatics , vol.18 , pp. 298-305
    • Bannai, H.1    Tamada, Y.2    Maruyama, O.3    Nakai, K.4    Miyano, S.5
  • 4
    • 0026315623 scopus 로고
    • Chemotaxis to chitin oligosaccharides by Vibrio furnissii
    • Bassler, B., P. Gibbons, C. Yu, and S. Roseman. 1991. Chemotaxis to chitin oligosaccharides by Vibrio furnissii. J. Biol. Chem. 266:24268-24275.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24268-24275
    • Bassler, B.1    Gibbons, P.2    Yu, C.3    Roseman, S.4
  • 5
    • 0032932006 scopus 로고    scopus 로고
    • The SIS domain: A phosphosugar-binding domain
    • Bateman, A. 1999. The SIS domain: a phosphosugar-binding domain. Trends Biochem. Sci. 24:94-95.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 94-95
    • Bateman, A.1
  • 7
    • 0029824486 scopus 로고    scopus 로고
    • Evidence that linker sequences and cellulose-binding domains enhance the activity of hemicellulases against complex substrates
    • Black, G. W., J. E. Rixon, J. H. Clarke, G. P. Hazlewood, M. K. Theodorou, P. Morris, and H. J. Gilbert. 1996. Evidence that linker sequences and cellulose-binding domains enhance the activity of hemicellulases against complex substrates. Biochem. J. 319:515-520.
    • (1996) Biochem. J. , vol.319 , pp. 515-520
    • Black, G.W.1    Rixon, J.E.2    Clarke, J.H.3    Hazlewood, G.P.4    Theodorou, M.K.5    Morris, P.6    Gilbert, H.J.7
  • 8
    • 0035310348 scopus 로고    scopus 로고
    • Pectate lyase 10A from Pseudomonas cellulosa is a modular enzyme containing a family 2a carbohydrate-binding module
    • Brown, I. E., M. H. Mallen, S. J. Charnock, G. J. Davies, and G. W. Black. 2001. Pectate lyase 10A from Pseudomonas cellulosa is a modular enzyme containing a family 2a carbohydrate-binding module. Biochem. J. 355:155-165.
    • (2001) Biochem. J. , vol.355 , pp. 155-165
    • Brown, I.E.1    Mallen, M.H.2    Charnock, S.J.3    Davies, G.J.4    Black, G.W.5
  • 9
    • 0031774284 scopus 로고    scopus 로고
    • Endochitinase is transported to the extracellular milieu by the eps-encoded general secretory pathway of Vibrio cholerae
    • Connell, T., D. Metzger, J. Lynch, and J. Folster. 1998. Endochitinase is transported to the extracellular milieu by the eps-encoded general secretory pathway of Vibrio cholerae. J. Bacteriol. 180:5591-5600.
    • (1998) J. Bacteriol. , vol.180 , pp. 5591-5600
    • Connell, T.1    Metzger, D.2    Lynch, J.3    Folster, J.4
  • 11
    • 0032847602 scopus 로고    scopus 로고
    • Expression of multiple complex polysaccharide-degrading enzyme systems by marine bacterium strain 2-40
    • Ensor, L., S. Stosz, and R. Weiner. 1999. Expression of multiple complex polysaccharide-degrading enzyme systems by marine bacterium strain 2-40. J. Ind. Microbiol. Biotechnol. 21:123-126.
    • (1999) J. Ind. Microbiol. Biotechnol. , vol.21 , pp. 123-126
    • Ensor, L.1    Stosz, S.2    Weiner, R.3
  • 12
    • 0035212668 scopus 로고    scopus 로고
    • Characterization of Pseudomonas aeruginosa chitinase, a gradually secreted protein
    • Folders, J., J. Algra, M. Roelofs, L. Loon, J. Tommassen, and W. Bitter. 2001. Characterization of Pseudomonas aeruginosa chitinase, a gradually secreted protein. J. Bacteriol. 183:7044-7052.
    • (2001) J. Bacteriol. , vol.183 , pp. 7044-7052
    • Folders, J.1    Algra, J.2    Roelofs, M.3    Loon, L.4    Tommassen, J.5    Bitter, W.6
  • 13
    • 0024297010 scopus 로고
    • Precise excision of the cellulose binding domains from two Cellulomonasfimi cellulases by a homologous protease and the effect on catalysis
    • Gilkes, N. R., R. A. Warren, R. C. Miller, Jr., and D. G. Kilburn. 1988. Precise excision of the cellulose binding domains from two Cellulomonasfimi cellulases by a homologous protease and the effect on catalysis. J. Biol. Chem. 263:10401-10407.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10401-10407
    • Gilkes, N.R.1    Warren, R.A.2    Miller R.C., Jr.3    Kilburn, D.G.4
  • 14
    • 0342314484 scopus 로고    scopus 로고
    • Phylogenetic characterization of a marine bacterium strain 2-40, a degrader of complex polysaccharides
    • Gonzalez, J., and R. Weiner. 2000. Phylogenetic characterization of a marine bacterium strain 2-40, a degrader of complex polysaccharides. Int. J. Syst. Bacteriol. 8:831-834.
    • (2000) Int. J. Syst. Bacteriol. , vol.8 , pp. 831-834
    • Gonzalez, J.1    Weiner, R.2
  • 15
    • 0002256521 scopus 로고
    • Physiology of microbial degradation of chitin and chitosan
    • C. Ratledge (ed.). Kluwer, Dordrecht, The Netherlands
    • Gooday, G. 1994. Physiology of microbial degradation of chitin and chitosan. p. 279-312. In C. Ratledge (ed.), Biochemistry of microbial degradation. Kluwer, Dordrecht, The Netherlands.
    • (1994) Biochemistry of Microbial Degradation , pp. 279-312
    • Gooday, G.1
  • 16
    • 0029090730 scopus 로고
    • The non-catalytic cellulose-binding domain of a novel cellulase from Pseudomonas fluorescens subsp. cellulosa is important for the efficient hydrolysis of Avicel
    • Hall, J., G. W. Black, L. M. Ferreira, S. J. Millward-Sadler, B. R. Ali, G. P. Hazlewood, and H. J. Gilbert. 1995. The non-catalytic cellulose-binding domain of a novel cellulase from Pseudomonas fluorescens subsp. cellulosa is important for the efficient hydrolysis of Avicel. Biochem. J. 309:749-756.
    • (1995) Biochem. J. , vol.309 , pp. 749-756
    • Hall, J.1    Black, G.W.2    Ferreira, L.M.3    Millward-Sadler, S.J.4    Ali, B.R.5    Hazlewood, G.P.6    Gilbert, H.J.7
  • 17
    • 0024722941 scopus 로고
    • Conserved serine-rich sequences in xylanase and cellulase from Pseudomonas fluorescens subspecies cellulosa: Internal signal sequence and unusual protein processing
    • Hall, J., G. P. Hazlewood, N. S. Huskisson, A. J. Durrant, and H. J. Gilbert. 1989. Conserved serine-rich sequences in xylanase and cellulase from Pseudomonas fluorescens subspecies cellulosa: internal signal sequence and unusual protein processing. Mol. Microbiol. 3:1211-1219.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1211-1219
    • Hall, J.1    Hazlewood, G.P.2    Huskisson, N.S.3    Durrant, A.J.4    Gilbert, H.J.5
  • 20
    • 0029976603 scopus 로고    scopus 로고
    • Using CLUSTAL for multiple sequence alignments
    • Higgins, D. G., J. D. Thompson, and T. J. Gibson. 1996. Using CLUSTAL for multiple sequence alignments. Methods Enzymol. 266:383-402.
    • (1996) Methods Enzymol. , vol.266 , pp. 383-402
    • Higgins, D.G.1    Thompson, J.D.2    Gibson, T.J.3
  • 21
    • 0034693322 scopus 로고    scopus 로고
    • Identification and molecular cloning of a chitoporin
    • Keyhani, N., X. Li, and S. Roseman. 2000. Identification and molecular cloning of a chitoporin. J. Biol. Chem. 275:33068-33076.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33068-33076
    • Keyhani, N.1    Li, X.2    Roseman, S.3
  • 22
    • 0030474759 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic chitodextrinase
    • Keyhani, N., and S. Roseman. 1996. The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic chitodextrinase. J. Biol. Chem. 271:33414-33424.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33414-33424
    • Keyhani, N.1    Roseman, S.2
  • 23
    • 0030447616 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic beta-N-acetylglucosaminidase
    • Keyhani, N., and S. Roseman. 1996. The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic beta-N-acetylglucosaminidase. J. Biol. Chem. 271:33425-33432.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33425-33432
    • Keyhani, N.1    Roseman, S.2
  • 24
    • 0030478209 scopus 로고    scopus 로고
    • Characterization of an N,N′-diacetylchitobiose transport system
    • Keyhani, N., L. Wang, Y. Lee, and S. Roseman. 1996. Characterization of an N,N′-diacetylchitobiose transport system. J. Biol. Chem. 271:33409-33413.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33409-33413
    • Keyhani, N.1    Wang, L.2    Lee, Y.3    Roseman, S.4
  • 25
    • 0034693218 scopus 로고    scopus 로고
    • The chitin disaccharide. N,N′-diacetylchitobiose, is catabolized by E. coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system
    • Keyhani, N., L. Wang, Y. Lee, and S. Roseman. 2000. The chitin disaccharide, N,N′-diacetylchitobiose, is catabolized by E. 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.1    Wang, L.2    Lee, Y.3    Roseman, S.4
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0038332468 scopus 로고    scopus 로고
    • Native, industrial, and fossil chitins
    • R. A. Muzzarelli and P. Jooaes (ed.). Birkhauser, Basel, Switzerland
    • Muzzarelli, R. 1999. Native, industrial, and fossil chitins, p. 1-5. In R. A. Muzzarelli and P. Jooaes (ed.), Chitin and chitinases. Birkhauser, Basel, Switzerland.
    • (1999) Chitin and Chitinases , pp. 1-5
    • Muzzarelli, R.1
  • 31
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Englebrecht, S. Brunak, and G. von Heijne. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Englebrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 33
    • 0025074317 scopus 로고
    • Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli
    • Peri, K. G., H. Goldie, and E. B. Waygood. 1990. Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli. Biochem. Cell Biol. 68:123-137.
    • (1990) Biochem. Cell Biol. , vol.68 , pp. 123-137
    • Peri, K.G.1    Goldie, H.2    Waygood, E.B.3
  • 34
    • 0035004025 scopus 로고    scopus 로고
    • Regulation of PTS gene expression by the homologous transcriptional regulators, Mlc and NagC, in Escherichia coli (or how two similar repressors can behave differently)
    • Plumbridge, J. 2001. Regulation of PTS gene expression by the homologous transcriptional regulators, Mlc and NagC, in Escherichia coli (or how two similar repressors can behave differently). J. Mol. Microbiol. Biotechnol. 3:371-380.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 371-380
    • Plumbridge, J.1
  • 35
    • 0025971343 scopus 로고
    • CAP and Nag repressor binding to the regulatory regions of the nagE-B and manX genes of Escherichia coli
    • Plumbridge, J., and A. Kolb. 1991. CAP and Nag repressor binding to the regulatory regions of the nagE-B and manX genes of Escherichia coli. J. Mol. Biol. 217:661-679.
    • (1991) J. Mol. Biol. , vol.217 , pp. 661-679
    • Plumbridge, J.1    Kolb, A.2
  • 36
    • 0024469348 scopus 로고
    • Sequence of the nagBACD operon in Escherichia coli K12 and pattern of transcription within the nag regulon
    • Plumbridge, J. A. 1989. Sequence of the nagBACD operon in Escherichia coli K12 and pattern of transcription within the nag regulon. Mol. Microbiol. 3:505-515.
    • (1989) Mol. Microbiol. , vol.3 , pp. 505-515
    • Plumbridge, J.A.1
  • 37
    • 0036841522 scopus 로고    scopus 로고
    • Widespread N-acetyl-D-glucosamine uptake among pelagic marine bacteria and its ecological implications
    • Riemann, L., and F. Azam. 2002. Widespread N-acetyl-D-glucosamine uptake among pelagic marine bacteria and its ecological implications. Appl. Environ. Microbiol. 68:5554-5562.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5554-5562
    • Riemann, L.1    Azam, F.2
  • 40
    • 0025923034 scopus 로고
    • Deletion of the linker connecting the catalytic and cellulose-binding domains of endoglucanase A (CenA) of Cellulomonas fimi alters its conformation and catalytic activity
    • Shen, H., M. Schmuck, I. Pilz, N. R. Gilkes, D. G. Kilburn, R. C. Miller, Jr., and R. A. Warren. 1991. Deletion of the linker connecting the catalytic and cellulose-binding domains of endoglucanase A (CenA) of Cellulomonas fimi alters its conformation and catalytic activity. J. Biol. Chem. 266:11335-11340.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11335-11340
    • Shen, H.1    Schmuck, M.2    Pilz, I.3    Gilkes, N.R.4    Kilburn, D.G.5    Miller R.C., Jr.6    Warren, R.A.7
  • 42
    • 0027197513 scopus 로고
    • Sequence analysis of the beta-N-acetylhexosaminidase gene of Vibrio vulnificus: Evidence for a common evolutionary origin of hexosaminidases
    • Somerville, C. C., and R. R. Colwell. 1993. Sequence analysis of the beta-N-acetylhexosaminidase gene of Vibrio vulnificus: evidence for a common evolutionary origin of hexosaminidases. Proc. Natl. Acad. Sci. USA 90:6751-6755.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6751-6755
    • Somerville, C.C.1    Colwell, R.R.2
  • 44
    • 0032955632 scopus 로고    scopus 로고
    • Multiple genes involved in chitin degradation from the marine bacterium Pseudoaltermonas sp. strain S91
    • Techkarnjanaruk, S., and A. Goodman. 1999. Multiple genes involved in chitin degradation from the marine bacterium Pseudoaltermonas sp. strain S91. Microbiology 145:925-934.
    • (1999) Microbiology , vol.145 , pp. 925-934
    • Techkarnjanaruk, S.1    Goodman, A.2
  • 45
    • 0025102841 scopus 로고
    • Detection of chitin deacetylase activity after polyacrylamide gel electrophoresis
    • Trudel, J., and A. Asselin. 1990. Detection of chitin deacetylase activity after polyacrylamide gel electrophoresis. Anal. Biochem. 189:249-253.
    • (1990) Anal. Biochem. , vol.189 , pp. 249-253
    • Trudel, J.1    Asselin, A.2
  • 47
    • 0036135173 scopus 로고    scopus 로고
    • Identification and characterization of the gene cluster involved in chitin degradation in a marine bacterium, Alteromonas sp. strain O-7
    • Tsujibo, H., H. Orikoshi, N. Baba, M. Miyahara, K. Miyamoto, M. Yasuda, and Y. Inamori. 2002. Identification and characterization of the gene cluster involved in chitin degradation in a marine bacterium, Alteromonas sp. strain O-7. Appl. Environ. Microbiol. 68:263-270.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 263-270
    • Tsujibo, H.1    Orikoshi, H.2    Baba, N.3    Miyahara, M.4    Miyamoto, K.5    Yasuda, M.6    Inamori, Y.7
  • 48
    • 0035055568 scopus 로고    scopus 로고
    • Purification, cloning, and DNA sequence analysis of a chitinase from an overproducing mutant of Streptomyces peucetius defective in daunorubicin biosynthesis
    • Vetrivel, K. S., S. K. Pandian, U. Chaudhary, and K. Dharmalingam. 2001. Purification, cloning, and DNA sequence analysis of a chitinase from an overproducing mutant of Streptomyces peucetius defective in daunorubicin biosynthesis. Can. J. Microbiol. 47:179-187.
    • (2001) Can. J. Microbiol. , vol.47 , pp. 179-187
    • Vetrivel, K.S.1    Pandian, S.K.2    Chaudhary, U.3    Dharmalingam, K.4
  • 49
    • 0030953360 scopus 로고    scopus 로고
    • 4-Methylumbelliferyl glycosides of N-acetyl 4-thiochito-oligosaccharides as fluorogenic substrates for chitodextrinase from Vibrio furnissii
    • Wang, L., N. Keyhani, S. Roseman, and Y. Lee. 1997. 4-Methylumbelliferyl glycosides of N-acetyl 4-thiochito-oligosaccharides as fluorogenic substrates for chitodextrinase from Vibrio furnissii. Glycobiology 7:855-860.
    • (1997) Glycobiology , vol.7 , pp. 855-860
    • Wang, L.1    Keyhani, N.2    Roseman, S.3    Lee, Y.4
  • 51
    • 0037994591 scopus 로고    scopus 로고
    • Degradosomes: Potential importance in the ocean's carbon cycle and in aquaculture and algal culture
    • N. Seaxena (ed.). Pacon International, New York, N.Y.
    • Weiner, R., L. Taylor, N. Ekborg, and L. Whitehead. 2001. Degradosomes: potential importance in the ocean's carbon cycle and in aquaculture and algal culture, p. 259-268. In N. Seaxena (ed.), Recent advances in marine science and technology, 2000. Pacon International, New York, N.Y.
    • (2001) Recent Advances in Marine Science and Technology, 2000 , pp. 259-268
    • Weiner, R.1    Taylor, L.2    Ekborg, N.3    Whitehead, L.4
  • 52
    • 0001681096 scopus 로고
    • The occurrence and characteristics of chitinoclastic bacteria in the sea
    • Zobell, C., and S. Rittenberg. 1937. The occurrence and characteristics of chitinoclastic bacteria in the sea. J. Bacteriol. 35:275-287.
    • (1937) J. Bacteriol. , vol.35 , pp. 275-287
    • Zobell, C.1    Rittenberg, S.2


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