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Volumn 145, Issue 12, 1999, Pages 3353-3363

Family 19 chitinases of Streptomyces species: Characterization and distribution

Author keywords

Allosamidin; Chitinase; Streptomyces

Indexed keywords

ALLOSAMIDIN; BACTERIAL DNA; BACTERIAL ENZYME; CHITINASE; DNA FRAGMENT;

EID: 0033381250     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-145-12-3353     Document Type: Article
Times cited : (144)

References (48)
  • 1
    • 0029619176 scopus 로고
    • Cloning and sequencing of chic gene of bacillus circulans wl-12 and relationship of its product to some other chitinases and chitinase-like proteins
    • Alam, M. M., Nikaidou, N., Tanaka, H. & Watanabe, T. (1995). Cloning and sequencing of chiC gene of Bacillus circulans WL-12 and relationship of its product to some other chitinases and chitinase-like proteins. J Ferment Bioeng 80, 454-461.
    • (1995) J Ferment Bioeng , vol.80 , pp. 454-461
    • Alam, M.M.1    Nikaidou, N.2    Tanaka, H.3    Watanabe, T.4
  • 2
    • 0015986813 scopus 로고
    • Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs
    • Ames, G. F. L (1974). Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. J Biol Chem 249, 634-644.
    • (1974) J Biol Chem , vol.249 , pp. 634-644
    • Ames, G.F.L.1
  • 3
    • 0028316274 scopus 로고
    • Stereochemical course of hydrolysis reaction catalyzed by chitinase A1 and D from Bacillus circulans WL-12
    • Armand, S., Tomita, H., Heyraud, A., Gey, C., Watanabe, T. & Henrissat, B. (1994). Stereochemical course of hydrolysis reaction catalyzed by chitinase A1 and D from Bacillus circulans WL-12. FEBS Lett 343, 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
  • 4
    • 0032584768 scopus 로고    scopus 로고
    • Substrate assistance in the mechanism of family 18 chitinases: Theoretical studies of potential intermediates and inhibitor
    • Brameld, K. A., Shrader, D. W. D., Imperiali, B. & Goddard, W. A., III (1998). Substrate assistance in the mechanism of family 18 chitinases: theoretical studies of potential intermediates and inhibitor. J Mol Biol 280, 913-923.
    • (1998) J Mol Biol , vol.280 , pp. 913-923
    • Brameld, K.A.1    Shrader, D.W.D.2    Imperiali, B.3    Goddard W.A. III4
  • 5
    • 0342972186 scopus 로고
    • Comparison of some molecular, enzymatic and antifungal properties of chitinases from thorn-apple, tobacco and wheat
    • Broekaert, W. F., Parijs, J. V., Allen, A. K. & Peumans, W. J. (1988). Comparison of some molecular, enzymatic and antifungal properties of chitinases from thorn-apple, tobacco and wheat. Physiol Mol Plant Pathol 33, 319-331.
    • (1988) Physiol Mol Plant Pathol , vol.33 , pp. 319-331
    • Broekaert, W.F.1    Parijs, J.V.2    Allen, A.K.3    Peumans, W.J.4
  • 7
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies, G. & Henrissat B. (1995). Structures and mechanisms of glycosyl hydrolases. Structure 3, 853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 8
    • 0001616015 scopus 로고
    • Comparative biochemistry of chitinase - Anomeric form of reaction products
    • Fukamizo, T., Koga, D. & Goto, S. (1995). Comparative biochemistry of chitinase - anomeric form of reaction products. Biosci Biotechnol Biochem 59, 311-313.
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 311-313
    • Fukamizo, T.1    Koga, D.2    Goto, S.3
  • 10
    • 0030909499 scopus 로고    scopus 로고
    • Structural and evolutionary relationships among chitinases of flowering plants
    • Hamel, F., Boivin, R., Tremblay, C. & Bellemare, G. (1997). Structural and evolutionary relationships among chitinases of flowering plants. J Mol Evol 44, 614-624.
    • (1997) J Mol Evol , vol.44 , pp. 614-624
    • Hamel, F.1    Boivin, R.2    Tremblay, C.3    Bellemare, G.4
  • 11
    • 0029071185 scopus 로고
    • The refined crystal structure of an endochitinase from Hordeum vulgare L. Seeds at 1·8 Å resolution
    • Hart, P. J., Pfluger, H. D., Monzingo, A. F., Hollis, T. & Robertus, J. D. (1995). The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1·8 Å resolution. J Mol Biol 248, 402-413.
    • (1995) J Mol Biol , vol.248 , pp. 402-413
    • Hart, P.J.1    Pfluger, H.D.2    Monzingo, A.F.3    Hollis, T.4    Robertus, J.D.5
  • 12
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. (1991). A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 280, 309-316.
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 13
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. & Bairoch, A. (1993). New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 293, 781-788.
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 15
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto, T. & Yagishita, K. (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
  • 16
    • 0027666351 scopus 로고
    • The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity
    • Iseli, B., Boller, T. & Neuhaus, J.-M. (1993). The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity. Plant Physiol 103, 221-226.
    • (1993) Plant Physiol , vol.103 , pp. 221-226
    • Iseli, B.1    Boller, T.2    Neuhaus, J.-M.3
  • 17
  • 18
  • 20
    • 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
  • 21
    • 0026063521 scopus 로고
    • Biochemical and molecular characterization of three barley seed proteins with antifungal properties
    • Lean, R., Tommerup, H., Svendsen, I. & Mundy, J. (1991). Biochemical and molecular characterization of three barley seed proteins with antifungal properties. J Biol Chem 266, 1564-1573.
    • (1991) J Biol Chem , vol.266 , pp. 1564-1573
    • Lean, R.1    Tommerup, H.2    Svendsen, I.3    Mundy, J.4
  • 22
    • 0023028051 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil, C. & Beckwith, J. (1986). A genetic approach to analyzing membrane protein topology. Science 233, 1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 23
    • 0029154798 scopus 로고
    • Purification and characterization of novel chitinases from Streptomyces griseus HUT6037
    • Mitsutomi, M., Hata, T. & Kuwahara, T. (1995). Purification and characterization of novel chitinases from Streptomyces griseus HUT6037. J Ferment Bioeng 80, 153-158.
    • (1995) J Ferment Bioeng , vol.80 , pp. 153-158
    • Mitsutomi, M.1    Hata, T.2    Kuwahara, T.3
  • 24
    • 0001039236 scopus 로고    scopus 로고
    • Action patterns of microbial chitinases and chitosanases on partially N-acetylated chitosan
    • Mitsutomi, M., Ueda, M., Arai, M., Ando, A. & Watanabe, T. (1996). Action patterns of microbial chitinases and chitosanases on partially N-acetylated chitosan. Chitin Enzymol 2, 273-284.
    • (1996) Chitin Enzymol , vol.2 , pp. 273-284
    • Mitsutomi, M.1    Ueda, M.2    Arai, M.3    Ando, A.4    Watanabe, T.5
  • 25
    • 0000886095 scopus 로고    scopus 로고
    • Mode of action of family 19 chitinases
    • Edited by A. Domard, G. A. F. Roberts & K. M. Varum. Lyon: Jacques André Publisher
    • Mitsutomi, M., Uchiyama, A., Yamagami, T. & Watanabe, T. (1997). Mode of action of family 19 chitinases. In Advances in Chitin Science, vol. 2, pp. 250-255. Edited by A. Domard, G. A. F. Roberts & K. M. Varum. Lyon: Jacques André Publisher.
    • (1997) Advances in Chitin Science , vol.2 , pp. 250-255
    • Mitsutomi, M.1    Uchiyama, A.2    Yamagami, T.3    Watanabe, T.4
  • 26
    • 0017610344 scopus 로고
    • A rapid and sensitive assay for chitinase using tritiated chitin
    • Molano, J., Duran, A. & Cabib, E. (1977). A rapid and sensitive assay for chitinase using tritiated chitin. Anal Biochem 83, 648-656.
    • (1977) Anal Biochem , vol.83 , pp. 648-656
    • Molano, J.1    Duran, A.2    Cabib, E.3
  • 27
    • 0014540906 scopus 로고
    • The chitinase of Serratia marcescens
    • Monreal, J. & Reese, E. T. (1969). The chitinase of Serratia marcescens. Can J Microbiol 15, 689-696.
    • (1969) Can J Microbiol , vol.15 , pp. 689-696
    • Monreal, J.1    Reese, E.T.2
  • 28
    • 0030032332 scopus 로고    scopus 로고
    • Chitinases, chitosanases, and lysozymes can be divided into prokaryotic and eukaryotic families sharing a conserved core
    • Monzingo, A. F., Marcotte, E. M., Hart, P. J. & Robertus, J. D. (1996). Chitinases, chitosanases, and lysozymes can be divided into prokaryotic and eukaryotic families sharing a conserved core. Nature Struct Biol 3, 133-140.
    • (1996) Nature Struct Biol , vol.3 , pp. 133-140
    • Monzingo, A.F.1    Marcotte, E.M.2    Hart, P.J.3    Robertus, J.D.4
  • 29
    • 0029835188 scopus 로고    scopus 로고
    • A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037
    • Ohno, T., Armand, S., Hata, T., Nikaidou, N., Henrissat, B., Mitsutomi, M. & Watanabe, T. (1996). A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037. J Bacteriol 178, 5065-5070.
    • (1996) J Bacteriol , vol.178 , pp. 5065-5070
    • Ohno, T.1    Armand, S.2    Hata, T.3    Nikaidou, N.4    Henrissat, B.5    Mitsutomi, M.6    Watanabe, T.7
  • 30
    • 0025441352 scopus 로고
    • The effect of nuclease on transformation efficiency in Serratia marcescens
    • Palomar, J., Guasch, J. F., Regue, M. & Vinas, M. (1990). The effect of nuclease on transformation efficiency in Serratia marcescens. FEMS Microbiol Lett 57, 255-258.
    • (1990) FEMS Microbiol Lett , vol.57 , pp. 255-258
    • Palomar, J.1    Guasch, J.F.2    Regue, M.3    Vinas, M.4
  • 33
    • 0001194009 scopus 로고
    • Plant and bacterial chitinases differ in antifungal activity
    • Roberts, W. K. & Selitrennikoff, C. P. (1988). Plant and bacterial chitinases differ in antifungal activity. J Gen Microbiol 134, 169-176.
    • (1988) J Gen Microbiol , vol.134 , pp. 169-176
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 35
    • 0000602126 scopus 로고
    • The structure of allosamidin, a novel insect chitinase inhibitor, produced by Streptomyces sp
    • Sakuda, S., Isogai, A., Matsumoto, S. & Suzuki, A. (1986). The structure of allosamidin, a novel insect chitinase inhibitor, produced by Streptomyces sp. Tetrahedron Lett 27, 2475-2478.
    • (1986) Tetrahedron Lett , vol.27 , pp. 2475-2478
    • Sakuda, S.1    Isogai, A.2    Matsumoto, S.3    Suzuki, A.4
  • 36
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum, A., Mauch, F., Vögeli, U. & Boller, T. (1986). Plant chitinases are potent inhibitors of fungal growth. Nature 324, 365-367.
    • (1986) Nature , vol.324 , pp. 365-367
    • Schlumbaum, A.1    Mauch, F.2    Vögeli, U.3    Boller, T.4
  • 37
    • 0025402915 scopus 로고
    • Structure of a tobacco endochitinase gene: Evidence that different genes can arise by transposition of sequences encoding a cysteine-rich domain
    • Shinshi, H., Neuhaus, J.-M., Ryals, J. & Meins, F. (1990). Structure of a tobacco endochitinase gene: evidence that different genes can arise by transposition of sequences encoding a cysteine-rich domain. Plant Mol Biol 14, 357-368.
    • (1990) Plant Mol Biol , vol.14 , pp. 357-368
    • Shinshi, H.1    Neuhaus, J.-M.2    Ryals, J.3    Meins, F.4
  • 38
    • 0000784312 scopus 로고
    • Cooperative description of type culture of Streptomyces. V. Additional descriptions
    • Shirling, E. B. & Gottlieb, D. (1972). Cooperative description of type culture of Streptomyces. V. Additional descriptions, Int J Syst Bacteriol 22, 265-394.
    • (1972) Int J Syst Bacteriol , vol.22 , pp. 265-394
    • Shirling, E.B.1    Gottlieb, D.2
  • 39
    • 0031602025 scopus 로고    scopus 로고
    • Chitin binding protein (CBP21) in the culture supernatant of Serratia marcescens 2170
    • Suzuki, K., Suzuki, M., Taiyoji, M., Nikaidou, N. & Watanabe, T. (1998). Chitin binding protein (CBP21) in the culture supernatant of Serratia marcescens 2170. Biosci Biotechnol Biochem 62, 128-135.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 128-135
    • Suzuki, K.1    Suzuki, M.2    Taiyoji, M.3    Nikaidou, N.4    Watanabe, T.5
  • 40
    • 0033229842 scopus 로고    scopus 로고
    • The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases
    • Suzuki, K., Taiyoji, M., Sugawara, N., Nikaidou, N., Henrissat, B. & Watanabe, T. (1999). The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases. Biochem J 343, 587-596.
    • (1999) Biochem J , vol.343 , pp. 587-596
    • Suzuki, K.1    Taiyoji, M.2    Sugawara, N.3    Nikaidou, N.4    Henrissat, B.5    Watanabe, T.6
  • 41
    • 0000206650 scopus 로고
    • Enzymatic hydrolysis of yeast cell walls. I. Isolation of wall-decomposing organism and separation and purification of lytic enzymes
    • Tanaka, H. & Phaff, H. J. (1965). Enzymatic hydrolysis of yeast cell walls. I. Isolation of wall-decomposing organism and separation and purification of lytic enzymes. J Bacteriol 89, 1570-1580.
    • (1965) J Bacteriol , vol.89 , pp. 1570-1580
    • Tanaka, H.1    Phaff, H.J.2
  • 42
    • 0007735495 scopus 로고
    • Taxonomic studies on the Streptomyces species, isolated as causal organisms of potato scab
    • Tashiro, N., Miyahita, K. & Suzuki, T. (1990). Taxonomic studies on the Streptomyces species, isolated as causal organisms of potato scab. Ann Phytopathol Soc Jpn 56, 73-82.
    • (1990) Ann Phytopathol Soc Jpn , vol.56 , pp. 73-82
    • Tashiro, N.1    Miyahita, K.2    Suzuki, T.3
  • 43
    • 0028774705 scopus 로고
    • Crystal structure of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhihitor
    • Terwisscha van Scheltinga, A. C., Kalk, K. H., Beintema, J. J. & Dijkstra, B. W. (1994). Crystal structure of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhihitor. Structure 2, 1181-1189.
    • (1994) Structure , vol.2 , pp. 1181-1189
    • Terwisscha Van Scheltinga, A.C.1    Kalk, K.H.2    Beintema, J.J.3    Dijkstra, B.W.4
  • 45
    • 0025561986 scopus 로고
    • Purification and some properties of extracellular chitinases from Streptomyces sp. S-84
    • Ueno, H., Miyashita, K., Sawada, Y. & Oba, Y. (1990). Purification and some properties of extracellular chitinases from Streptomyces sp. S-84. J Gen Appl Microbiol 36, 377-392.
    • (1990) J Gen Appl Microbiol , vol.36 , pp. 377-392
    • Ueno, H.1    Miyashita, K.2    Sawada, Y.3    Oba, Y.4
  • 46
    • 0025314392 scopus 로고
    • Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation
    • Watanabe, T., Oyanagi, W., Suzuki, K. & Tanaka, H. (1990). Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation. J Bacteriol 172, 4017-4022.
    • (1990) J Bacteriol , vol.172 , pp. 4017-4022
    • Watanabe, T.1    Oyanagi, W.2    Suzuki, K.3    Tanaka, H.4
  • 48
    • 0019883721 scopus 로고
    • A convenient synthesis of glycol chitin, a substrate of lysozyme
    • Yamada, H. & Imoto, T. (1981). A convenient synthesis of glycol chitin, a substrate of lysozyme. Carbohydr Res 92, 160-162.
    • (1981) Carbohydr Res , vol.92 , pp. 160-162
    • Yamada, H.1    Imoto, T.2


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