메뉴 건너뛰기




Volumn 1473, Issue 1, 1999, Pages 108-122

Physiological aspects of chitin catabolism in marine bacteria

Author keywords

[No Author keywords available]

Indexed keywords

CHITIN;

EID: 0032714186     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(99)00172-5     Document Type: Review
Times cited : (264)

References (94)
  • 1
    • 0030748702 scopus 로고    scopus 로고
    • Human enzymatic activities related to the therapeutic administration of chitin derivatives
    • Muzzarelli R.A. Human enzymatic activities related to the therapeutic administration of chitin derivatives. Cell. Mol. Life Sci. 53:1997;131-140.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 131-140
    • Muzzarelli, R.A.1
  • 2
    • 0030334022 scopus 로고
    • Applications of chitin and chitosan for biomaterials
    • Shigemasa Y., Minami S. Applications of chitin and chitosan for biomaterials. Biotechnol. Genet. Eng. Rev. 13:1995;383-420.
    • (1995) Biotechnol. Genet. Eng. Rev. , vol.13 , pp. 383-420
    • Shigemasa, Y.1    Minami, S.2
  • 4
    • 0004184147 scopus 로고
    • Pergamon Press, Oxford
    • R.A.A. Muzzarelli, Chitin, Pergamon Press, Oxford, 1977, pp. -309.
    • (1977) Chitin , pp. 309
    • Muzzarelli, R.A.A.1
  • 9
    • 0025227385 scopus 로고
    • The relative contribution of marine snow of different origins to biological processes in coastal waters
    • Alldredge A.L., Gotschalk C.C. The relative contribution of marine snow of different origins to biological processes in coastal waters. Cont. Shelf Res. 10:1990;41-58.
    • (1990) Cont. Shelf Res. , vol.10 , pp. 41-58
    • Alldredge, A.L.1    Gotschalk, C.C.2
  • 10
    • 0001681096 scopus 로고
    • The occurrence and characteristics of chitinoclastic bacteria in the sea
    • Zobell C.E., Rittenberg S.C. The occurrence and characteristics of chitinoclastic bacteria in the sea. J. Bacteriol. 35:1937;275-287.
    • (1937) J. Bacteriol. , vol.35 , pp. 275-287
    • Zobell, C.E.1    Rittenberg, S.C.2
  • 11
    • 0348193542 scopus 로고
    • Chitin biomass in marine sediments
    • in: G. Skjak-Braek, T. Anthonsen, P. Sandford (Eds.), Elsevier Applied Science, London
    • M. Poulicek, C. Jeuniaux, Chitin biomass in marine sediments, in: G. Skjak-Braek, T. Anthonsen, P. Sandford (Eds.), Chitin and Chitosan, Elsevier Applied Science, London, 1988, pp. 151-155.
    • (1988) Chitin and Chitosan , pp. 151-155
    • Poulicek, M.1    Jeuniaux, C.2
  • 12
    • 0007642632 scopus 로고
    • Chromatographie der in der chitinreihe wirksamen Enzyme des emulsins
    • Zechmeister L., Tóth G. Chromatographie der in der chitinreihe wirksamen Enzyme des emulsins. Enzymologia. 7:1939;165-169.
    • (1939) Enzymologia , vol.7 , pp. 165-169
    • Zechmeister, L.1    Tóth, G.2
  • 13
    • 0007714386 scopus 로고
    • Chromatographie der in der chitinreihe wirksamen Enzyme der weinbergschnecke (helix pomatia)
    • Zechmeister L., Tóth G., Vajda E. Chromatographie der in der chitinreihe wirksamen Enzyme der weinbergschnecke (helix pomatia). Enzymologia. 7:1939;170-175.
    • (1939) Enzymologia , vol.7 , pp. 170-175
    • Zechmeister, L.1    Tóth, G.2    Vajda, E.3
  • 15
    • 0024252560 scopus 로고
    • Biomass, Part B, Lignin, Pectin and Chitin
    • Academic Press
    • W.A. Wood, S.T. Kellog, Biomass, Part B, Lignin, Pectin and Chitin. Methods in Enzymology, Academic Press, 1988.
    • (1988) Methods in Enzymology
    • Wood, W.A.1    Kellog, S.T.2
  • 16
  • 17
    • 0028911536 scopus 로고
    • Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins
    • Renkema G.H., Boot R.G., Muijsers A.O., Donker-Koopman W.E., Aerts J.M.F.G. Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins. J. Biol. Chem. 270:1995;2198-2202.
    • (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
  • 18
  • 19
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat B., Davies G. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7:1997;637-644.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 20
  • 21
    • 0030909499 scopus 로고    scopus 로고
    • Structural and evolutionary relationships among chitinases of flowering plants
    • Hamel F., Boivin R., Tremblay C., Bellemare G. Structural and evolutionary relationships among chitinases of flowering plants. J. Mol. Evol. 44:1997;614-624.
    • (1997) J. Mol. Evol. , vol.44 , pp. 614-624
    • Hamel, F.1    Boivin, R.2    Tremblay, C.3    Bellemare, G.4
  • 24
  • 25
    • 0024228913 scopus 로고
    • Characteristics, dynamics and significance of marine snow
    • Alldredge A.L., Silver M.W. Characteristics, dynamics and significance of marine snow. Prog. Oceanogr. 20:1988;41-82.
    • (1988) Prog. Oceanogr. , vol.20 , pp. 41-82
    • Alldredge, A.L.1    Silver, M.W.2
  • 26
    • 0027847061 scopus 로고
    • Simulating bacterial clustering around phytoplankton cells in a turbulent ocean
    • Bowen J.D., Stolzenbach K.D., Chisholm S.W. Simulating bacterial clustering around phytoplankton cells in a turbulent ocean. Limnol. Oceanogr. 38:1993;36-51.
    • (1993) Limnol. Oceanogr. , vol.38 , pp. 36-51
    • Bowen, J.D.1    Stolzenbach, K.D.2    Chisholm, S.W.3
  • 27
    • 0024797460 scopus 로고
    • Simulation of bacterial attraction and adhesion to falling particles in an aquatic environment
    • Jackson G.A. Simulation of bacterial attraction and adhesion to falling particles in an aquatic environment. Limnol. Oceanogr. 34:1989;514-530.
    • (1989) Limnol. Oceanogr. , vol.34 , pp. 514-530
    • Jackson, G.A.1
  • 28
    • 0000887786 scopus 로고    scopus 로고
    • Flagella and Motility
    • in: F.C. Neidhardt (Ed.) ASM Press
    • R.M. Macnab, Flagella and Motility, in: F.C. Neidhardt (Ed.) Escherichia coli and Salmonella typhimurium, ASM Press, 1996, pp. 123-145.
    • (1996) Escherichia Coli and Salmonella Typhimurium , pp. 123-145
    • Macnab, R.M.1
  • 29
    • 0016716291 scopus 로고
    • Effect of temperature, salts, pH and other factors on the development of peritrichous flagella in Vibrio alginolyticus
    • Ulitzur S. Effect of temperature, salts, pH and other factors on the development of peritrichous flagella in Vibrio alginolyticus. Arch. Microbiol. 104:1975;285-288.
    • (1975) Arch. Microbiol. , vol.104 , pp. 285-288
    • Ulitzur, S.1
  • 30
    • 0029854432 scopus 로고    scopus 로고
    • Chemotactic responses to an attractant and a repellent by the polar and lateral flagellar system of Vibrio alginolyticus
    • Homma M., Oota H., Kojima S., Kawagishi I., Imae Y. Chemotactic responses to an attractant and a repellent by the polar and lateral flagellar system of Vibrio alginolyticus. Microbiology. 142:1996;2777-2783.
    • (1996) Microbiology , vol.142 , pp. 2777-2783
    • Homma, M.1    Oota, H.2    Kojima, S.3    Kawagishi, I.4    Imae, Y.5
  • 31
    • 0025100947 scopus 로고
    • Chemotactic control of the two flagellar systems of Vibrio parahaemolyticus
    • Sar N., McCarter L., Simon M., Silverman M. Chemotactic control of the two flagellar systems of Vibrio parahaemolyticus. J. Bacteriol. 172:1990;334-341.
    • (1990) J. Bacteriol. , vol.172 , pp. 334-341
    • Sar, N.1    McCarter, L.2    Simon, M.3    Silverman, M.4
  • 32
    • 0344887449 scopus 로고
    • Chitinases: Plant defense proteins related to resistance against fungal pathogens
    • in: R. Muzzarelli, C. Jeuniaux, G.W. Gooday (Eds.), Plenum Press, New York
    • D. Roby, A. Toppan, T.M.T. Esquerré, Chitinases: Plant defense proteins related to resistance against fungal pathogens, in: R. Muzzarelli, C. Jeuniaux, G.W. Gooday (Eds.), Chitin in nature and technology, Plenum Press, New York. ,1986, pp. 231-233.
    • (1986) Chitin in Nature and Technology , pp. 231-233
    • Roby, D.1    Toppan, A.2    Esquerré, T.M.T.3
  • 33
    • 0029955266 scopus 로고    scopus 로고
    • The sodium-driven polar flagellar motor of marine Vibrio as the mechanosensor that regulates lateral flagellar expression
    • Kawagishi I., Imagawa M., Imae Y., McCarter L., Homma M. The sodium-driven polar flagellar motor of marine Vibrio as the mechanosensor that regulates lateral flagellar expression. Mol. Microbiol. 20:1996;693-699.
    • (1996) Mol. Microbiol. , vol.20 , pp. 693-699
    • Kawagishi, I.1    Imagawa, M.2    Imae, Y.3    McCarter, L.4    Homma, M.5
  • 34
    • 0030033211 scopus 로고    scopus 로고
    • Chemotactic motility is required for invasion of the host by the fish pathogen Vibrio anguillarum
    • O'Toole R., Milton D.L., Wolf-Watz H. Chemotactic motility is required for invasion of the host by the fish pathogen Vibrio anguillarum. Mol. Microbiol. 19:1996;625-637.
    • (1996) Mol. Microbiol. , vol.19 , pp. 625-637
    • O'Toole, R.1    Milton, D.L.2    Wolf-Watz, H.3
  • 35
    • 0019359663 scopus 로고
    • Role of chemotaxis in the association of motile bacteria with intestinal mucosa: Chemotactic responses of Vibrio cholerae and description of motile nonchemotactic mutants
    • Freter R., O'Brien P.C. Role of chemotaxis in the association of motile bacteria with intestinal mucosa: chemotactic responses of Vibrio cholerae and description of motile nonchemotactic mutants. Infect. Immun. 34:1981;215-221.
    • (1981) Infect. Immun. , vol.34 , pp. 215-221
    • Freter, R.1    O'Brien, P.C.2
  • 37
    • 0028973377 scopus 로고
    • Natural assemblages of marine bacteria exhibiting high-speed motility and large accelerations
    • Mitchell J.G., Pearson L., Dillon S., Kantalis K. Natural assemblages of marine bacteria exhibiting high-speed motility and large accelerations. Appl. Environ. Microbiol. 61:1995;4436-4440.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 4436-4440
    • Mitchell, J.G.1    Pearson, L.2    Dillon, S.3    Kantalis, K.4
  • 38
    • 0026677710 scopus 로고
    • Cellobiose chemotaxis by the cellulolytic bacterium Cellulomonas gelida
    • Hsing W., Canale-Parola E. Cellobiose chemotaxis by the cellulolytic bacterium Cellulomonas gelida. J. Bacteriol. 174:1992;7996-8002.
    • (1992) J. Bacteriol. , vol.174 , pp. 7996-8002
    • Hsing, W.1    Canale-Parola, E.2
  • 39
    • 0017275072 scopus 로고
    • Eological aspects of microbial chemotactic behavior
    • Chet I., Mitchell R. Eological aspects of microbial chemotactic behavior. Annu. Rev. Microbiol. 30:1976;221-239.
    • (1976) Annu. Rev. Microbiol. , vol.30 , pp. 221-239
    • Chet, I.1    Mitchell, R.2
  • 40
    • 0023001757 scopus 로고
    • Effect of N-Acetylchito-oligosaccharides on activation of phagocytes
    • Suzuki K., Tokoro A., Okawa Y., Suzuki S., Suzuki M. Effect of N-Acetylchito-oligosaccharides on activation of phagocytes. Microbiol. Immunol. 30:1986;777-787.
    • (1986) Microbiol. Immunol. , vol.30 , pp. 777-787
    • Suzuki, K.1    Tokoro, A.2    Okawa, Y.3    Suzuki, S.4    Suzuki, M.5
  • 42
    • 0024411095 scopus 로고
    • Chemotaxis to chitin oligosaccharides by Vibrio furnissii, a chitinivorous marine bacterium
    • Bassler B.L., Gibbons P.J., Roseman S. Chemotaxis to chitin oligosaccharides by Vibrio furnissii, a chitinivorous marine bacterium. Biochem. Biophys. Res. Commun. 161:1989;1172-1176.
    • (1989) Biochem. Biophys. Res. Commun. , vol.161 , pp. 1172-1176
    • Bassler, B.L.1    Gibbons, P.J.2    Roseman, S.3
  • 43
    • 0026315623 scopus 로고
    • Chitin utilization by marine bacteria: Chemotaxis to chitin oligosaccharides by Vibrio furnissii
    • Bassler B.L., Gibbons P.J., Yu C., Roseman S. Chitin utilization by marine bacteria: chemotaxis to chitin oligosaccharides by Vibrio furnissii. J. Biol. Chem. 266:1991;24268-24275.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24268-24275
    • Bassler, B.L.1    Gibbons, P.J.2    Yu, C.3    Roseman, S.4
  • 44
    • 0027309275 scopus 로고
    • Chemotaxis of the marine bacterium Vibrio furnissii to sugar substrates of the phosphoenolpyruvate: Glycose phosphotransferase system
    • Yu C., Bassler B.L., Roseman S. Chemotaxis of the marine bacterium Vibrio furnissii to sugar substrates of the phosphoenolpyruvate: glycose phosphotransferase system. J. Biol. Chem. 268:1993;9405-9409.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9405-9409
    • Yu, C.1    Bassler, B.L.2    Roseman, S.3
  • 45
    • 0343765474 scopus 로고
    • Arthropoda Academic Press, New York
    • M. Florkin, B.T. Scheer, Chemical Zoology, Arthropoda Academic Press, New York, 1970, pp. 147-194.
    • (1970) Chemical Zoology , pp. 147-194
    • Florkin, M.1    Scheer, B.T.2
  • 46
    • 0003868932 scopus 로고
    • Federation of American Societies for Experimental Biology, Bethesda, MD
    • P.L. Altman, D.S. Dittmer, Blood and other body fluids, Federation of American Societies for Experimental Biology, Bethesda, MD, 1971, pp. 287-289.
    • (1971) Blood and Other Body Fluids , pp. 287-289
    • Altman, P.L.1    Dittmer, D.S.2
  • 48
    • 84885768007 scopus 로고
    • Cholera, Copepods and Chitinase
    • Nalin D.R. Cholera, Copepods and Chitinase. Lancet. 2:1976;958.
    • (1976) Lancet , vol.2 , pp. 958
    • Nalin, D.R.1
  • 50
    • 0345318590 scopus 로고
    • C.H. Oppenheimer (Ed.), C.C. Thomas, Springfield, IL
    • D.W. lear, Symposium on Marine Microbiology, C.H. Oppenheimer (Ed.), C.C. Thomas, Springfield, IL, 1963, p. 608.
    • (1963) Symposium on Marine Microbiology , pp. 608
    • Lear, D.W.1
  • 51
    • 0028847180 scopus 로고
    • Attachment of non-culturable toxigenic vibrio cholerae-01 and non-01 and aeromonas spp. to the aquatic arthropod gerris-spinolae and plants in the river-Ganga, Varanasi
    • Shukla B.N., Singh D.V., Sanyal S.C. Attachment of non-culturable toxigenic vibrio cholerae-01 and non-01 and aeromonas spp. to the aquatic arthropod gerris-spinolae and plants in the river-Ganga, Varanasi. FEMS Immunol. Med. Microbiol. 12:1995;113-120.
    • (1995) FEMS Immunol. Med. Microbiol. , vol.12 , pp. 113-120
    • Shukla, B.N.1    Singh, D.V.2    Sanyal, S.C.3
  • 52
    • 0030950843 scopus 로고    scopus 로고
    • Epibiotic microorganisms on copepods and other marine crustaceans
    • Carman K.R., Dobbs F.C. Epibiotic microorganisms on copepods and other marine crustaceans. Microsc. Res. Tech. 37:1997;116-135.
    • (1997) Microsc. Res. Tech. , vol.37 , pp. 116-135
    • Carman, K.R.1    Dobbs, F.C.2
  • 54
    • 0029888438 scopus 로고    scopus 로고
    • Molecular basis of intercellular adhesion in the biofilm-forming Staphylococcus epidermidis
    • Heilmann C., Schweitzer O., Gerke C., Vanittanakom N., Mack D., Gotz F. Molecular basis of intercellular adhesion in the biofilm-forming Staphylococcus epidermidis. Mol. Microbiol. 20:1996;1083-1091.
    • (1996) Mol. Microbiol. , vol.20 , pp. 1083-1091
    • Heilmann, C.1    Schweitzer, O.2    Gerke, C.3    Vanittanakom, N.4    Mack, D.5    Gotz, F.6
  • 55
    • 0028993617 scopus 로고
    • Adhesion of bacteria and diatoms to surfaces in the sea: A review
    • Cooksey K.E., Wigglesworth-Cooksey B. Adhesion of bacteria and diatoms to surfaces in the sea: a review. Aquat. Microb. Ecol. 9:1995;87-96.
    • (1995) Aquat. Microb. Ecol. , vol.9 , pp. 87-96
    • Cooksey, K.E.1    Wigglesworth-Cooksey, B.2
  • 56
    • 0025148929 scopus 로고
    • Marine adhesive proteins: Natural composite thermosets
    • Waite J.H. Marine adhesive proteins: natural composite thermosets. Int. J. Biol. Macromol. 12:1990;139-144.
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 139-144
    • Waite, J.H.1
  • 57
    • 0019808208 scopus 로고
    • Adhesion: A tactic in the survival strategy of a marine vibrio during starvation
    • Dawson M.P., Humphrey B.A., Marshall K.C. Adhesion: a tactic in the survival strategy of a marine vibrio during starvation. Curr. Microbiol. 6:1981;195-199.
    • (1981) Curr. Microbiol. , vol.6 , pp. 195-199
    • Dawson, M.P.1    Humphrey, B.A.2    Marshall, K.C.3
  • 58
    • 0027474233 scopus 로고
    • Role of chitin-binding proteins in the specific attachment of the marine bacterium Vibrio harveyi to chitin
    • Montgomery M.T., Kirchman D.L. Role of chitin-binding proteins in the specific attachment of the marine bacterium Vibrio harveyi to chitin. Appl. Environ. Microbiol. 59:1993;373-379.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 373-379
    • Montgomery, M.T.1    Kirchman, D.L.2
  • 59
    • 0028153318 scopus 로고
    • Induction of chitin-binding proteins during the specific attachment of the marine bacterium Vibrio harveyi to chitin
    • Montgomery M.T., Kirchman D.L. Induction of chitin-binding proteins during the specific attachment of the marine bacterium Vibrio harveyi to chitin. Appl. Environ. Microbiol. 60:1994;4284-4288.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4284-4288
    • Montgomery, M.T.1    Kirchman, D.L.2
  • 60
    • 0028566393 scopus 로고
    • Chitovibrin: A chitin-binding lectin from Vibrio parahemolyticus
    • Gildemeister O.S., Zhu B.C.R., Laine R.A. Chitovibrin: a chitin-binding lectin from Vibrio parahemolyticus. Glycoconjugate J. 11:1994;518-526.
    • (1994) Glycoconjugate J. , vol.11 , pp. 518-526
    • Gildemeister, O.S.1    Zhu, B.C.R.2    Laine, R.A.3
  • 61
    • 0029801453 scopus 로고    scopus 로고
    • Attachment of Vibrio alginolyticus to chitin mediated by chitin-binding proteins
    • Pruzzo C., Crippa A., Bertone S., Pane L., Carli A. Attachment of Vibrio alginolyticus to chitin mediated by chitin-binding proteins. Microbiology. 142:1996;2181-2186.
    • (1996) Microbiology , vol.142 , pp. 2181-2186
    • Pruzzo, C.1    Crippa, A.2    Bertone, S.3    Pane, L.4    Carli, A.5
  • 62
    • 0023668652 scopus 로고
    • The sugar-specific adhesion/deadhesion apparatus of the marine bacterium Vibrio furnissii is a sensorium that continuously monitors nutrient levels in the environment
    • Yu C., Lee A.M., Roseman S. The sugar-specific adhesion/deadhesion apparatus of the marine bacterium Vibrio furnissii is a sensorium that continuously monitors nutrient levels in the environment. Biochem. Biophys. Res. Commun. 149:1987;86-92.
    • (1987) Biochem. Biophys. Res. Commun. , vol.149 , pp. 86-92
    • Yu, C.1    Lee, A.M.2    Roseman, S.3
  • 63
    • 0026350890 scopus 로고
    • Chitin utilization by marine bacteria: A physiological function for bacterial adhesion to immobilized carbohydrates
    • Yu C., Lee A.M., Bassler B.L., Roseman S. Chitin utilization by marine bacteria: a physiological function for bacterial adhesion to immobilized carbohydrates. J. Biol. Chem. 266:1991;24260-24267.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24260-24267
    • Yu, C.1    Lee, A.M.2    Bassler, B.L.3    Roseman, S.4
  • 64
  • 65
    • 0000746334 scopus 로고
    • Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase
    • Comb D.G., Roseman S. Glucosamine metabolism. IV. Glucosamine-6-phosphate deaminase. J. Biol. Chem. 232:1958;807-827.
    • (1958) J. Biol. Chem. , vol.232 , pp. 807-827
    • Comb, D.G.1    Roseman, S.2
  • 66
    • 0026315624 scopus 로고
    • Chitin utilization by marine bacteria: Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii
    • Bassler B.L., Yu C., Lee Y.C., Roseman S. Chitin utilization by marine bacteria: degradation and catabolism of chitin oligosaccharides by Vibrio furnissii. J. Biol. Chem. 266:1991;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
  • 67
    • 0009404427 scopus 로고
    • Sur la fonction fungicide des bulbes d′ophrydées
    • Bernard M. Sur la fonction fungicide des bulbes d′ophrydées. Am. Sci. Nat. Bot. Paris. 14:1911;221-234.
    • (1911) Am. Sci. Nat. Bot. Paris , vol.14 , pp. 221-234
    • Bernard, M.1
  • 69
    • 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
    • Terwisscha van Scheltinga A.C., Armand S., Kalk K.H., Isogai A., Henrissat B.X.D.B.W. Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry. 34:1995;15619-15623.
    • (1995) Biochemistry , vol.34 , pp. 15619-15623
    • Terwisscha Van Scheltinga, A.C.1    Armand, S.2    Kalk, K.H.3    Isogai, A.4    Henrissat, B.X.D.B.W.5
  • 70
    • 0028316274 scopus 로고
    • Stereochemical course of the hydrolysis reaction catalyzed by chitinases A1 and D from Bacillus circulans WL-12
    • Armand S., Tomita H., Heyraud A., Gey C., Watanabe T., Henrissat B. Stereochemical course of the hydrolysis reaction catalyzed by chitinases A1 and D from Bacillus circulans WL-12. FEBS Lett. 343:1994;177-180.
    • (1994) FEBS Lett. , vol.343 , pp. 177-180
    • Armand, S.1    Tomita, H.2    Heyraud, A.3    Gey, C.4    Watanabe, T.5    Henrissat, B.6
  • 71
    • 0027216435 scopus 로고
    • Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity
    • Watanabe T., Kobori K., Miyashita K., Fujii T., Sakai H., Uchida M., Tanaka H. Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J. Biol. Chem. 268:1993;18567-18572.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18567-18572
    • Watanabe, T.1    Kobori, K.2    Miyashita, K.3    Fujii, T.4    Sakai, H.5    Uchida, M.6    Tanaka, H.7
  • 74
    • 0023901367 scopus 로고
    • Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli
    • Robbins P.W., Albright C., Benfield B. Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli. J. Biol. Chem. 263:1988;443-447.
    • (1988) J. Biol. Chem. , vol.263 , pp. 443-447
    • Robbins, P.W.1    Albright, C.2    Benfield, B.3
  • 75
    • 0025816274 scopus 로고
    • Isolation and characterization of thermostable chitinase from Bacillus licheniformis X-7u
    • Takayanagi T., Ajisaka K., Takiguchi Y., Shimahara K. Isolation and characterization of thermostable chitinase from Bacillus licheniformis X-7u. Biochim. Biophys. Acta. 1078:1991;404-410.
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 404-410
    • Takayanagi, T.1    Ajisaka, K.2    Takiguchi, Y.3    Shimahara, K.4
  • 76
    • 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.O., Roseman S. The chitin catabolic cascade in the marine bacterium Vibrio furnissii: Molecular cloning, isolation and characterization of a periplasmic chitodextrinase. J. Biol. Chem. 271:1996;33414-33424.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33414-33424
    • Keyhani, N.O.1    Roseman, S.2
  • 77
    • 0030447616 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio furnissii: Molecular cloning, isolation and characterization of a periplasmic β-N-Acetylglucosaminidase
    • Keyhani N.O., Roseman S. The chitin catabolic cascade in the marine bacterium Vibrio furnissii: Molecular cloning, isolation and characterization of a periplasmic β-N-Acetylglucosaminidase. J. Biol. Chem. 271:1996;33425-33432.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33425-33432
    • Keyhani, N.O.1    Roseman, S.2
  • 78
    • 0030451823 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel β-N-acetyl-D-glucosaminidase from Vibrio furnissii
    • Chitlaru E., Roseman S. Molecular cloning and characterization of a novel β-N-acetyl-D-glucosaminidase from Vibrio furnissii. J. Biol. Chem. 271:1996;33433-33439.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33433-33439
    • Chitlaru, E.1    Roseman, S.2
  • 79
    • 0030220261 scopus 로고    scopus 로고
    • Porins: General to specific, native to engineered passive pores
    • Schulz G.E. Porins: general to specific, native to engineered passive pores. Curr. Opin. Struct. Biol. 6:1996;485-490.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 485-490
    • Schulz, G.E.1
  • 80
    • 0030478209 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio furnissii: Characterization of an N, N′-diacetylchitobiose transport system
    • Keyhani N.O., Wang L.-X., Lee Y.C., Roseman S. The chitin catabolic cascade in the marine bacterium Vibrio furnissii: Characterization of an N, N′-diacetylchitobiose transport system. J. Biol. Chem. 271:1996;33409-33413.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33409-33413
    • Keyhani, N.O.1    Wang, L.-X.2    Lee, Y.C.3    Roseman, S.4
  • 81
    • 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., Roseman S. Wild-type Escherichia coli grows on the chitin disaccharide, N, N′-diacetylchitobiose, by expressing the cel operon. Proc. Natl. Acad. Sci. USA. 94:1997;14367-14371.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14367-14371
    • Keyhani, N.O.1    Roseman, S.2
  • 82
    • 0030743041 scopus 로고    scopus 로고
    • Use of a promoterless lacZ gene insertion to investigate chitinase gene expression in the marine bacterium Pseudoalteromonas sp. strain S9
    • Techkarnjanaruk S., Pongpattanakitshote S., Goodman A.E. Use of a promoterless lacZ gene insertion to investigate chitinase gene expression in the marine bacterium Pseudoalteromonas sp. strain S9. Appl. Environ. Microbiol. 63:1997;2989-2996.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2989-2996
    • Techkarnjanaruk, S.1    Pongpattanakitshote, S.2    Goodman, A.E.3
  • 83
    • 0032454787 scopus 로고    scopus 로고
    • GlkA is involved in glucose repression of chitinase production in Streptomyces lividans
    • Saito A., Fujii T., Yoneyama T., Miyashita K. glkA is involved in glucose repression of chitinase production in Streptomyces lividans. J. Bacteriol. 180:1998;2911-2914.
    • (1998) J. Bacteriol. , vol.180 , pp. 2911-2914
    • Saito, A.1    Fujii, T.2    Yoneyama, T.3    Miyashita, K.4
  • 84
    • 0029040621 scopus 로고
    • The glucose kinase gene of Streptomyces coelicolor is not required for glucose repression of the chi63 promoter
    • Ingram C., Westpheling J. The glucose kinase gene of Streptomyces coelicolor is not required for glucose repression of the chi63 promoter. J. Bacteriol. 177:1995;3587-3588.
    • (1995) J. Bacteriol. , vol.177 , pp. 3587-3588
    • Ingram, C.1    Westpheling, J.2
  • 85
    • 0029034530 scopus 로고
    • CcrA1: A mutation in Streptomyces coelicolor that affects the control of catabolite repression
    • Ingram C., Delic I., Westpheling J. ccrA1: A mutation in Streptomyces coelicolor that affects the control of catabolite repression. J. Bacteriol. 177:1995;3579-3586.
    • (1995) J. Bacteriol. , vol.177 , pp. 3579-3586
    • Ingram, C.1    Delic, I.2    Westpheling, J.3
  • 87
    • 0028973673 scopus 로고
    • Transcriptional regulation of bioluminesence genes from Vibrio fischeri
    • Sitnikov D.M., Schineller J.B., Baldwin T.O. Transcriptional regulation of bioluminesence genes from Vibrio fischeri. Mol. Microbiol. 17:1995;801-812.
    • (1995) Mol. Microbiol. , vol.17 , pp. 801-812
    • Sitnikov, D.M.1    Schineller, J.B.2    Baldwin, T.O.3
  • 88
    • 0030078997 scopus 로고    scopus 로고
    • Efficient preparation of β-(1→6)-(GlcNAc)(2) by enzymatic conversion of chitin and chito-oligosaccharides
    • Shimoda K., Nakajima K., Hiratsuka Y., Nishimura S.I., Kurita K. Efficient preparation of β-(1→6)-(GlcNAc)(2) by enzymatic conversion of chitin and chito-oligosaccharides. Carbohydr. Polymers. 29:1996;149-154.
    • (1996) Carbohydr. Polymers , vol.29 , pp. 149-154
    • Shimoda, K.1    Nakajima, K.2    Hiratsuka, Y.3    Nishimura, S.I.4    Kurita, K.5
  • 89
    • 0024041235 scopus 로고
    • Cloning of the genes of the chitin utilization regulon of Serratia liquefaciens
    • Joshi S., Kozlowski M., Selvaraj G., Iyer V.N., Davies R.W. Cloning of the genes of the chitin utilization regulon of Serratia liquefaciens. J. Bacteriol. 170:1988;2984-2988.
    • (1988) J. Bacteriol. , vol.170 , pp. 2984-2988
    • Joshi, S.1    Kozlowski, M.2    Selvaraj, G.3    Iyer, V.N.4    Davies, R.W.5
  • 90
    • 0030791783 scopus 로고    scopus 로고
    • Amylase and chitinase genes in Streptomyces lividans are regulated by reg1, a pleiotropic regulatory gene
    • Nguyen J., Francou F., Virolle M.-J., Guérineau M. Amylase and chitinase genes in Streptomyces lividans are regulated by reg1, a pleiotropic regulatory gene. J. Bacteriol. 179:1997;6383-6390.
    • (1997) J. Bacteriol. , vol.179 , pp. 6383-6390
    • Nguyen, J.1    Francou, F.2    Virolle, M.-J.3    Guérineau, M.4
  • 92
    • 0026571181 scopus 로고
    • Structure of the gene encoding chitinase D of Bacillus circulans WL-12 and possible homology of the enzyme of other prokaryotic chitinases and class III plant chitinases
    • Watanabe T., Oyanagi W., Suzuki K., Ohnishi K., Tanaka H. Structure of the gene encoding chitinase D of Bacillus circulans WL-12 and possible homology of the enzyme of other prokaryotic chitinases and class III plant chitinases. J. Bacteriol. 174:1992;408-414.
    • (1992) J. Bacteriol. , vol.174 , pp. 408-414
    • Watanabe, T.1    Oyanagi, W.2    Suzuki, K.3    Ohnishi, K.4    Tanaka, H.5
  • 93
    • 0025314392 scopus 로고
    • Chitinase system of Bacillus ciculans WL-12 and importance of chitinase A1 in chitin degradation
    • Watanabe T., Oyanagi W., Suzuki K., Tanaka H. Chitinase system of Bacillus ciculans WL-12 and importance of chitinase A1 in chitin degradation. J. Bacteriol. 172:1990;4017-4022.
    • (1990) J. Bacteriol. , vol.172 , pp. 4017-4022
    • Watanabe, T.1    Oyanagi, W.2    Suzuki, K.3    Tanaka, H.4
  • 94
    • 0030981929 scopus 로고    scopus 로고
    • Chitin degradation proteins produced by the marine bacterium vibrio harveyi growing on different forms of chitin
    • Svitil A.L., Chadhain S.M.N., Moore J.A., Kirchman D.L. Chitin degradation proteins produced by the marine bacterium vibrio harveyi growing on different forms of chitin. Appl. Environ. Microbiol. 63:1997;408-413.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 408-413
    • Svitil, A.L.1    Chadhain, S.M.N.2    Moore, J.A.3    Kirchman, D.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.