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Volumn 72, Issue 11, 2006, Pages 7331-7338

Effects of mutations in the substrate-binding domain of poly[(R)-3-hydroxybutyrate] (PHB) depolymerase from Ralstonia pickettii T1 on PHB degradation

Author keywords

[No Author keywords available]

Indexed keywords

ADSORPTION; AMINO ACIDS; BACTERIA; BINDING ENERGY; BIODEGRADATION; GENES; MUTAGENESIS; SUBSTRATES; THROUGHPUT;

EID: 33750990228     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.01187-06     Document Type: Article
Times cited : (33)

References (37)
  • 1
    • 0025226099 scopus 로고
    • Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates
    • Anderson, A. J., and E. A. Dawes. 1990. Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates. Microbiol. Rev. 54:450-477.
    • (1990) Microbiol. Rev. , vol.54 , pp. 450-477
    • Anderson, A.J.1    Dawes, E.A.2
  • 2
    • 0030271442 scopus 로고    scopus 로고
    • Poly(3-hydroxybutyrate) depolymerases bind to their substrate by a C-terminal located substrate binding site
    • Behrends, A., B. Klingbeil, and D. Jendrossek. 1996. Poly(3- hydroxybutyrate) depolymerases bind to their substrate by a C-terminal located substrate binding site. FEMS Microbiol. Lett. 143:191-194.
    • (1996) FEMS Microbiol. Lett. , vol.143 , pp. 191-194
    • Behrends, A.1    Klingbeil, B.2    Jendrossek, D.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0034641715 scopus 로고    scopus 로고
    • Cellulose-binding domains promote hydrolysis different sites on crystalline cellulose
    • Carrard, G., A. Koivula, H. S. Söderlund, and P. Béguin. 2000. Cellulose-binding domains promote hydrolysis different sites on crystalline cellulose. Proc. Natl. Acad. Sci. USA 97:10342-10347.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10342-10347
    • Carrard, G.1    Koivula, A.2    Söderlund, H.S.3    Béguin, P.4
  • 5
    • 0004290581 scopus 로고
    • VCH Publishers, New York, N.Y.
    • Doi, Y. 1990. Microbial polyesters, p. 33-62. VCH Publishers, New York, N.Y.
    • (1990) Microbial Polyesters , pp. 33-62
    • Doi, Y.1
  • 6
    • 29444446408 scopus 로고    scopus 로고
    • Interaction between PHB depolymerase and biodegradable polyesters by atomic force microscopy
    • Fujita, M., Y. Kobori, Y. Aoki, N. Matsumoto, H. Abe, Y. Doi, and T. Hiraishi. 2005. Interaction between PHB depolymerase and biodegradable polyesters by atomic force microscopy. Langmuir 21:11829-11835.
    • (2005) Langmuir , vol.21 , pp. 11829-11835
    • Fujita, M.1    Kobori, Y.2    Aoki, Y.3    Matsumoto, N.4    Abe, H.5    Doi, Y.6    Hiraishi, T.7
  • 7
    • 0034279048 scopus 로고    scopus 로고
    • Function of the catalytic domain of poly(3-hydroxybutyrate) depolymerase from Pseudomonas stutzeri
    • Hiraishi, T., T. Ohura, S. Ito, K. Kasuya, and Y. Doi. 2000. Function of the catalytic domain of poly(3-hydroxybutyrate) depolymerase from Pseudomonas stutzeri. Biomacromolecules 1:320-324.
    • (2000) Biomacromolecules , vol.1 , pp. 320-324
    • Hiraishi, T.1    Ohura, T.2    Ito, S.3    Kasuya, K.4    Doi, Y.5
  • 8
    • 31344472487 scopus 로고    scopus 로고
    • The crystal structure of polyhydroxybutyrate depolymerase from Penicillium funiculosum provides insights into the recognition and degradation oi biopolyesters
    • Hisano, T., K. Kasuya, Y. Tezuka, N. Ishii, T. Kobayashi, M. Shiraki, E. Oroudjev, H. Hansma, T. Iwata, Y. Doi, T. Saito, and K. Miki. 2006. The crystal structure of polyhydroxybutyrate depolymerase from Penicillium funiculosum provides insights into the recognition and degradation oi biopolyesters. J. Mol. Biol. 356:993-1004.
    • (2006) J. Mol. Biol. , vol.356 , pp. 993-1004
    • Hisano, T.1    Kasuya, K.2    Tezuka, Y.3    Ishii, N.4    Kobayashi, T.5    Shiraki, M.6    Oroudjev, E.7    Hansma, H.8    Iwata, T.9    Doi, Y.10    Saito, T.11    Miki, K.12
  • 9
    • 0008946431 scopus 로고    scopus 로고
    • Extracellular polyhydroxyalkanoate depolymerases: The key enzymes of PHA degradation
    • Y. Doi and A. Steinbüchel (ed.). Wiley-VCH Verlag GmbH, Weinheim, Germany
    • Jendrossek, D. 2002. Extracellular polyhydroxyalkanoate depolymerases: the key enzymes of PHA degradation., p 41-83 In Y. Doi and A. Steinbüchel (ed.), Biopolymers 3b. Wiley-VCH Verlag GmbH, Weinheim, Germany.
    • (2002) Biopolymers 3b , pp. 41-83
    • Jendrossek, D.1
  • 10
    • 0011126489 scopus 로고    scopus 로고
    • Recent advances in characterization of bacterial PHA depolymerases
    • G. Eggink, A. Steinbüchel, Y. Poirier, and B. Witholt, (ed.). NRC Research Press, Ottawa, Canada
    • Jendrossek, D., A. Schirmer, and R. Handrick. 1997. Recent advances in characterization of bacterial PHA depolymerases, p. 89-101 In G. Eggink, A. Steinbüchel, Y. Poirier, and B. Witholt, (ed.), 1996 International Symposium on Bacterial Polyhydroxyalkanoates. NRC Research Press, Ottawa, Canada.
    • (1997) 1996 International Symposium on Bacterial Polyhydroxyalkanoates , pp. 89-101
    • Jendrossek, D.1    Schirmer, A.2    Handrick, R.3
  • 11
    • 0028715248 scopus 로고
    • Enzymatic degradation of poly[(R)-3-hydroxyburyrate] by Comamonas testosteroni ATSU of soil bacterium
    • Kasuya, K., Y. Doi, and T. Yao. 1994. Enzymatic degradation of poly[(R)-3-hydroxyburyrate] by Comamonas testosteroni ATSU of soil bacterium. Polym. Degrad. Stab. 45:379-386.
    • (1994) Polym. Degrad. Stab. , vol.45 , pp. 379-386
    • Kasuya, K.1    Doi, Y.2    Yao, T.3
  • 12
    • 0030777589 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of the polyhydroxybutyrate depolymerase of Comamonas acidovorans YM1609, isolated from fresh water
    • Kasuya, K., Y. Inoue, T. Tanaka, T. Akehata, T. Iwata, T. Fukui, and Y. Doi. 1997. Biochemical and molecular characterization of the polyhydroxybutyrate depolymerase of Comamonas acidovorans YM1609, isolated from fresh water. Appl. Environ. Microbiol. 63:4844-4852.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4844-4852
    • Kasuya, K.1    Inoue, Y.2    Tanaka, T.3    Akehata, T.4    Iwata, T.5    Fukui, T.6    Doi, Y.7
  • 13
    • 0034208966 scopus 로고    scopus 로고
    • Identification of a marine benthic P(3HB)-degrading bacterium isolate and characterization of its P(3HB) depolymerase
    • Kasuya, K., H. Mitomo, M. Nakahara, A. Akiba, T. Kudo, and Y. Doi. 2000. Identification of a marine benthic P(3HB)-degrading bacterium isolate and characterization of its P(3HB) depolymerase. Biomacromolecules 1:194-201.
    • (2000) Biomacromolecules , vol.1 , pp. 194-201
    • Kasuya, K.1    Mitomo, H.2    Nakahara, M.3    Akiba, A.4    Kudo, T.5    Doi, Y.6
  • 14
    • 0033066633 scopus 로고    scopus 로고
    • Substrate and binding specificities of bacterial polyhydroxybutyrate depolymerases
    • Kasuya, K., T. Ohura, K. Masuda, and Y. Doi. 1999. Substrate and binding specificities of bacterial polyhydroxybutyrate depolymerases. Int. J. Biol. Macromol. 24:329-336.
    • (1999) Int. J. Biol. Macromol. , vol.24 , pp. 329-336
    • Kasuya, K.1    Ohura, T.2    Masuda, K.3    Doi, Y.4
  • 15
    • 0242409668 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a poly(3-hydroxybutyrate) depolymerase from Marinobacter sp. NK-1
    • Kasuya, K., T. Tanaka, Y. Tezuka, W. C. Hsieh, H. Mitomo, and Y. Doi. 2003. Cloning, expression and characterization of a poly(3-hydroxybutyrate) depolymerase from Marinobacter sp. NK-1. Int. J. Biol. Macromol. 33:221-226.
    • (2003) Int. J. Biol. Macromol. , vol.33 , pp. 221-226
    • Kasuya, K.1    Tanaka, T.2    Tezuka, Y.3    Hsieh, W.C.4    Mitomo, H.5    Doi, Y.6
  • 16
    • 5044233606 scopus 로고    scopus 로고
    • Direct observation of poly(3-hydroxybutyrate) depolymerase adsorbed on polyester thin film by atomic force microscopy
    • Kikkawa, Y., M. Fujita, T. Hiraishi, M. Yoshimoto, and Y. Doi. 2004. Direct observation of poly(3-hydroxybutyrate) depolymerase adsorbed on polyester thin film by atomic force microscopy. Biomacromolecules 5:1642-1646.
    • (2004) Biomacromolecules , vol.5 , pp. 1642-1646
    • Kikkawa, Y.1    Fujita, M.2    Hiraishi, T.3    Yoshimoto, M.4    Doi, Y.5
  • 17
    • 22944450656 scopus 로고    scopus 로고
    • Dynamic adsorption behavior of poly(3-hydroxybutyrate) depolymerase on polyester surface investigated by QCM and AFM
    • Kikkawa, Y., K. Yamashita, T. Hiraishi, M. Kanesato, and Y. Doi. 2005. Dynamic adsorption behavior of poly(3-hydroxybutyrate) depolymerase on polyester surface investigated by QCM and AFM. Biomacromolecules 6:2084-2090.
    • (2005) Biomacromolecules , vol.6 , pp. 2084-2090
    • Kikkawa, Y.1    Yamashita, K.2    Hiraishi, T.3    Kanesato, M.4    Doi, Y.5
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0027329331 scopus 로고
    • Microbial-degradation of poly(3-hydroxybutyrate) and poly(3- hydroxybutyrate-co-3-hydroxyvalerate) in soils
    • Mergaert, J., A. Webb, C. Anderson, A. Wouters, and J. Swings. 1993. Microbial-degradation of poly(3-hydroxybutyrate) and poly(3-hydroxybutyrate-co- 3-hydroxyvalerate) in soils. Appl. Environ. Microbiol. 59:3233-3238.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3233-3238
    • Mergaert, J.1    Webb, A.2    Anderson, C.3    Wouters, A.4    Swings, J.5
  • 20
    • 0028262871 scopus 로고
    • Efficient hydrolysis of polyhydroxyalkanoates by Pseudomonas stutzeri YM1414 isolated from lake water
    • Mukai, K., K. Yamada, and Y. Doi. 1994. Efficient hydrolysis of polyhydroxyalkanoates by Pseudomonas stutzeri YM1414 isolated from lake water. Polym. Degrad. Stab. 43:319-327.
    • (1994) Polym. Degrad. Stab. , vol.43 , pp. 319-327
    • Mukai, K.1    Yamada, K.2    Doi, Y.3
  • 21
    • 0027227008 scopus 로고
    • Enzymatic degradation of poly(hydroxyalkanoates) by a marine bacterium
    • Mukai, K., K. Yamada, and Y. Doi. 1993. Enzymatic degradation of poly(hydroxyalkanoates) by a marine bacterium. Polym. Degrad. Stab. 41:85-91.
    • (1993) Polym. Degrad. Stab. , vol.41 , pp. 85-91
    • Mukai, K.1    Yamada, K.2    Doi, Y.3
  • 22
    • 0027438347 scopus 로고
    • Kinetics and mechanism of heterogeneous hydrolysis of poly[(R)-3-hydroxybutyrate] film by PHA depolymerases
    • Mukai, K., K. Yamada, and Y. Doi. 1993. Kinetics and mechanism of heterogeneous hydrolysis of poly[(R)-3-hydroxybutyrate] film by PHA depolymerases. Int. J. Biol. Macromol. 15:361-366.
    • (1993) Int. J. Biol. Macromol. , vol.15 , pp. 361-366
    • Mukai, K.1    Yamada, K.2    Doi, Y.3
  • 23
    • 0036193920 scopus 로고    scopus 로고
    • Nonhydrolytic fragmentation of a poly[(A)-3-hydroxybutyrate] single crystal revealed by use of a mutant of polyhydroxybutyrate depolymerase
    • Murase, T., Y. Suzuki, Y. Doi, and T. Iwata. 2002. Nonhydrolytic fragmentation of a poly[(A)-3-hydroxybutyrate] single crystal revealed by use of a mutant of polyhydroxybutyrate depolymerase. Biomacromolecules 3:312-317.
    • (2002) Biomacromolecules , vol.3 , pp. 312-317
    • Murase, T.1    Suzuki, Y.2    Doi, Y.3    Iwata, T.4
  • 24
    • 0030730849 scopus 로고    scopus 로고
    • Structure and function of poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis T1
    • Nojiri, M., and T. Saito. 1997. Structure and function of poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis T1. J. Bacteriol. 179:6965-6970.
    • (1997) J. Bacteriol. , vol.179 , pp. 6965-6970
    • Nojiri, M.1    Saito, T.2
  • 25
    • 0032963796 scopus 로고    scopus 로고
    • Cloning and characterization of the polyhydroxybutyrate depolymerase gene of Pseudomonas stutzeri and analysis of the function of substrate-binding domains
    • Ohura, T., K. Kasuya, and Y. Doi. 1999. Cloning and characterization of the polyhydroxybutyrate depolymerase gene of Pseudomonas stutzeri and analysis of the function of substrate-binding domains. Appl. Environ. Microbiol. 65:189-197.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 189-197
    • Ohura, T.1    Kasuya, K.2    Doi, Y.3
  • 26
    • 0024526245 scopus 로고
    • Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis
    • Saito, T., K. Suzuki, J. Yamamoto, T. Fukui, K. Miwa, K. Tomita, S. Nakanishi, S. Odani, J. Suzuki, and K. Ishikawa. 1989. Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis. J. Bacteriol. 171:184-189.
    • (1989) J. Bacteriol. , vol.171 , pp. 184-189
    • Saito, T.1    Suzuki, K.2    Yamamoto, J.3    Fukui, T.4    Miwa, K.5    Tomita, K.6    Nakanishi, S.7    Odani, S.8    Suzuki, J.9    Ishikawa, K.10
  • 28
    • 0032098584 scopus 로고    scopus 로고
    • Simple kinetic model for the heterogeneous enzymatic hydrolysis of natural poly(3-hydroxybutyrate)
    • Scandola, M., M. L. Focarete, and G. Frisoni. 1998. Simple kinetic model for the heterogeneous enzymatic hydrolysis of natural poly(3-hydroxybutyrate). Macromolecules 31:3846-3851.
    • (1998) Macromolecules , vol.31 , pp. 3846-3851
    • Scandola, M.1    Focarete, M.L.2    Frisoni, G.3
  • 29
    • 0031944928 scopus 로고    scopus 로고
    • The adsorption of substrate binding domain of PHB depolymerases to the surface of poly(3-hydroxybutyric acid)
    • Shinomiya, M., T. Iwata, and Y. Doi. 1998. The adsorption of substrate binding domain of PHB depolymerases to the surface of poly(3-hydroxybutyric acid). Int. J. Biol. Macromol. 22:129-135.
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 129-135
    • Shinomiya, M.1    Iwata, T.2    Doi, Y.3
  • 30
    • 0030921217 scopus 로고    scopus 로고
    • Cloning of the gene for poly(3-hydroxybutyric acid) depolymerase of Comamonas testosterone and functional analysis of its substrate-binding domain
    • Shinomiya, M., T. Iwata, K. Kasuya, and Y. Doi. 1997. Cloning of the gene for poly(3-hydroxybutyric acid) depolymerase of Comamonas testosterone and functional analysis of its substrate-binding domain. FEMS Microbiol. Lett. 154:89-94.
    • (1997) FEMS Microbiol. Lett. , vol.154 , pp. 89-94
    • Shinomiya, M.1    Iwata, T.2    Kasuya, K.3    Doi, Y.4
  • 31
    • 0004155427 scopus 로고
    • W. H. Freeman and Company, New York, N.Y.
    • Stryer, L. 1988. Biochemistry, 3rd ed. W. H. Freeman and Company, New York, N.Y.
    • (1988) Biochemistry, 3rd Ed.
    • Stryer, L.1
  • 32
    • 0035917520 scopus 로고    scopus 로고
    • Analysis of mutational effects of a polyhydroxybutyrate (PHB) depolymerase on bacterial PHB accumulation using an in vivo assay system
    • Taguchi, S., A. Maehara, K, Takase, M. Nakahara, and Y. Doi. 2001. Analysis of mutational effects of a polyhydroxybutyrate (PHB) depolymerase on bacterial PHB accumulation using an in vivo assay system. FEMS Microbiol. Lett. 198:65-71.
    • (2001) FEMS Microbiol. Lett. , vol.198 , pp. 65-71
    • Taguchi, S.1    Maehara, A.2    Takase, K.3    Nakahara, M.4    Doi, Y.5
  • 34
    • 0043031090 scopus 로고    scopus 로고
    • Alteration of chain length substrate specificity of Aeromonas caviae R-enantiomer-specific enoyl-coenzyme a hydratase through site-directed mutagenesis
    • Tsuge, T., T. Hisano, S. Taguchi, and Y. Doi. 2003. Alteration of chain length substrate specificity of Aeromonas caviae R-enantiomer-specific enoyl-coenzyme A hydratase through site-directed mutagenesis. Appl. Environ. Microbiol. 69:4830-4836.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 4830-4836
    • Tsuge, T.1    Hisano, T.2    Taguchi, S.3    Doi, Y.4
  • 35
    • 23344446196 scopus 로고    scopus 로고
    • The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation
    • Vaaje-Kolstad, G., S. J. Horn, D. M. F. van Aalten, B. Synstad, and V. G. H. Eijsink. 2005. The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation. J. Biol. Chem. 280:28492-28497.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28492-28497
    • Vaaje-Kolstad, G.1    Horn, S.J.2    Van Aalten, D.M.F.3    Synstad, B.4    Eijsink, V.G.H.5
  • 36
    • 0034894206 scopus 로고    scopus 로고
    • Analysis of adsorption function of polyhydroxybutyrate depolymerase from Alcaligenes faecalis T1 by using a quartz crystal microbalance
    • Yamashita, K., Y. Aoyagi, H. Abe, and Y. Doi. 2001. Analysis of adsorption function of polyhydroxybutyrate depolymerase from Alcaligenes faecalis T1 by using a quartz crystal microbalance. Biomacromolecules 2:25-28.
    • (2001) Biomacromolecules , vol.2 , pp. 25-28
    • Yamashita, K.1    Aoyagi, Y.2    Abe, H.3    Doi, Y.4
  • 37
    • 0345491305 scopus 로고    scopus 로고
    • Characteristic interactions between poly(hydroxybutyrate) depolymerase and poly[(R)-3-hydroxybutyrate] films studied by a quartz crystal microbalance
    • Yamashita, K., T. Funato, Y. Suzuki, S. Teramachi, and Y. Doi. 2003. Characteristic interactions between poly(hydroxybutyrate) depolymerase and poly[(R)-3-hydroxybutyrate] films studied by a quartz crystal microbalance. Macromol. Biosci. 3:694-702.
    • (2003) Macromol. Biosci. , vol.3 , pp. 694-702
    • Yamashita, K.1    Funato, T.2    Suzuki, Y.3    Teramachi, S.4    Doi, Y.5


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