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Volumn 102, Issue 1, 2006, Pages 60-65

Novel poly-γ-glutamate-processing enzyme catalyzing γ-glutamyl DD-amidohydrolysis

Author keywords

glutamyl DD amidohydrolase; Bacillus subtilis; enzymatic poly glutamate processing; poly glutamate

Indexed keywords

AMINO ACIDS; BENZENE; BIOCHEMISTRY; CATALYSIS; HYDROLYSIS; MOLECULAR WEIGHT;

EID: 33748459631     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.102.60     Document Type: Article
Times cited : (24)

References (26)
  • 2
    • 0042255061 scopus 로고    scopus 로고
    • Poly-γ-glutamic acid
    • Fahnestock S.R., and Steinbüchel A. (Eds), Wiley-VCH, Weinheim
    • Ashiuchi M., and Misono H. Poly-γ-glutamic acid. In: Fahnestock S.R., and Steinbüchel A. (Eds). Biopolymers vol. 7 (2002), Wiley-VCH, Weinheim 123-174
    • (2002) Biopolymers , vol.7 , pp. 123-174
    • Ashiuchi, M.1    Misono, H.2
  • 3
    • 33645513746 scopus 로고    scopus 로고
    • Natural and edible biopolymer poly-γ-glutamic acid: synthesis, production, and application
    • Sung M.-H., Park C., Kim C.-J., Poo H., Soda K., and Ashiuchi M. Natural and edible biopolymer poly-γ-glutamic acid: synthesis, production, and application. Chem. Rec. 5 (2005) 352-366
    • (2005) Chem. Rec. , vol.5 , pp. 352-366
    • Sung, M.-H.1    Park, C.2    Kim, C.-J.3    Poo, H.4    Soda, K.5    Ashiuchi, M.6
  • 4
    • 85004571497 scopus 로고
    • Screening for microorganism having poly(γ-glutamic acid) endohydrolase activity and the enzyme production by Myrothecium sp. TM-4222
    • Tanaka T., Yamaguchi T., Hiruta O., Futamura T., Uotani K., Satoh A., Taniguchi M., and Oi S. Screening for microorganism having poly(γ-glutamic acid) endohydrolase activity and the enzyme production by Myrothecium sp. TM-4222. Biosci. Biotechnol. Biochem. 57 (1993) 1809-1810
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1809-1810
    • Tanaka, T.1    Yamaguchi, T.2    Hiruta, O.3    Futamura, T.4    Uotani, K.5    Satoh, A.6    Taniguchi, M.7    Oi, S.8
  • 5
    • 85007856438 scopus 로고
    • Purification and characterization of poly(γ-glutamic acid) hydrolase from a filamentous fungus, Myrothecium sp. TM-4222
    • Tanaka T., Hiruta O., Futamura T., Uotani K., Satoh A., Taniguchi M., and Oi S. Purification and characterization of poly(γ-glutamic acid) hydrolase from a filamentous fungus, Myrothecium sp. TM-4222. Biosci. Biotechnol. Biochem. 57 (1993) 2148-2153
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 2148-2153
    • Tanaka, T.1    Hiruta, O.2    Futamura, T.3    Uotani, K.4    Satoh, A.5    Taniguchi, M.6    Oi, S.7
  • 6
    • 0031442532 scopus 로고    scopus 로고
    • Existence of an optically heterogeneous peptide unit in poly(γ-glutamic acid) by produced by Bacillus subtilis
    • Tanaka T., Fujita K., Takenishi S., and Taniguchi M. Existence of an optically heterogeneous peptide unit in poly(γ-glutamic acid) by produced by Bacillus subtilis. J. Ferment. Bioeng. 84 (1997) 361-364
    • (1997) J. Ferment. Bioeng. , vol.84 , pp. 361-364
    • Tanaka, T.1    Fujita, K.2    Takenishi, S.3    Taniguchi, M.4
  • 8
    • 0037727706 scopus 로고    scopus 로고
    • Amidase domains from bacterial and phage autolysins define a family of γ-D,L-glutamate-specific amidohydrolases
    • Rigden D.J., Jedrzejas M.J., and Galperin M.Y. Amidase domains from bacterial and phage autolysins define a family of γ-D,L-glutamate-specific amidohydrolases. Trends Biochem. Sci. 28 (2003) 230-234
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 230-234
    • Rigden, D.J.1    Jedrzejas, M.J.2    Galperin, M.Y.3
  • 9
    • 0037379280 scopus 로고    scopus 로고
    • Characterization of the Bacillus subtilis ywtD gene, whose product is involved in γ-polyglutamic acid degradation
    • Suzuki T., and Tahara Y. Characterization of the Bacillus subtilis ywtD gene, whose product is involved in γ-polyglutamic acid degradation. J. Bacteriol. 185 (2003) 2379-2382
    • (2003) J. Bacteriol. , vol.185 , pp. 2379-2382
    • Suzuki, T.1    Tahara, Y.2
  • 12
    • 0029998145 scopus 로고    scopus 로고
    • Identification, sequence, and expression of the gene encoding γ-glutamyltranspeptidase in Bacillus subtilis
    • Xu K., and Strauch M.A. Identification, sequence, and expression of the gene encoding γ-glutamyltranspeptidase in Bacillus subtilis. J. Bacteriol. 178 (1996) 4319-4322
    • (1996) J. Bacteriol. , vol.178 , pp. 4319-4322
    • Xu, K.1    Strauch, M.A.2
  • 13
    • 0031240577 scopus 로고    scopus 로고
    • Purification and properties of two isozymes of γ-glutamyltranspeptidase from Bacillus subtilis TAM-4
    • Abe K., Ito Y., Ohmachi T., and Asada Y. Purification and properties of two isozymes of γ-glutamyltranspeptidase from Bacillus subtilis TAM-4. Biosci. Biotechnol. Biochem. 61 (1997) 1621-1625
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1621-1625
    • Abe, K.1    Ito, Y.2    Ohmachi, T.3    Asada, Y.4
  • 14
    • 11044230062 scopus 로고    scopus 로고
    • Characterization of Bacillus subtilis γ-glutamyltransferase and its involvement in the degradation of capsule poly-γ-glutamate
    • Kimura K., Tran L.-S.P., Uchida I., and Itoh Y. Characterization of Bacillus subtilis γ-glutamyltransferase and its involvement in the degradation of capsule poly-γ-glutamate. Microbiology 150 (2004) 4115-4123
    • (2004) Microbiology , vol.150 , pp. 4115-4123
    • Kimura, K.1    Tran, L.-S.P.2    Uchida, I.3    Itoh, Y.4
  • 17
    • 0026059172 scopus 로고
    • Physico-mechanical properties of degradable polymers used in medical applications: a comparative study
    • Engelberg I., and Kohn J. Physico-mechanical properties of degradable polymers used in medical applications: a comparative study. Biomaterials 12 (1991) 292-304
    • (1991) Biomaterials , vol.12 , pp. 292-304
    • Engelberg, I.1    Kohn, J.2
  • 18
    • 0027250038 scopus 로고
    • Identification of a novel gene, dep, associated with depolymerization of the capsular polymer in Bacillus anthracis
    • Uchida I., Makino S., Sawamura C., Yoshikawa M., Sugimato C., and Terakado M. Identification of a novel gene, dep, associated with depolymerization of the capsular polymer in Bacillus anthracis. Mol. Microbiol. 9 (1993) 487-496
    • (1993) Mol. Microbiol. , vol.9 , pp. 487-496
    • Uchida, I.1    Makino, S.2    Sawamura, C.3    Yoshikawa, M.4    Sugimato, C.5    Terakado, M.6
  • 19
    • 13244255402 scopus 로고    scopus 로고
    • Capsule synthesis by Bacillus anthracis is required for dissemination in murine inhalation anthrax
    • Drysdale M., Heninger S., Hutt J., Chen Y., Lyons C.R., and Koehler T.M. Capsule synthesis by Bacillus anthracis is required for dissemination in murine inhalation anthrax. EMBO J. 24 (2005) 221-227
    • (2005) EMBO J. , vol.24 , pp. 221-227
    • Drysdale, M.1    Heninger, S.2    Hutt, J.3    Chen, Y.4    Lyons, C.R.5    Koehler, T.M.6
  • 20
    • 0033802118 scopus 로고    scopus 로고
    • Polymer production by two newly isolated extremely halophilic archaea: application of a novel corrosion-resistant bioreactor
    • Hezayen F.F., Rehm B.H.A., Eberhardt R., and Steinbüchel A. Polymer production by two newly isolated extremely halophilic archaea: application of a novel corrosion-resistant bioreactor. Appl. Microbiol. Biotechnol. 54 (2000) 319-325
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 319-325
    • Hezayen, F.F.1    Rehm, B.H.A.2    Eberhardt, R.3    Steinbüchel, A.4
  • 21
    • 0034980464 scopus 로고    scopus 로고
    • Transfer of Natrialba asiatica B1T to Natrialba taiwanensis sp. nov., a novel extremely halophilic, aerobic, non-pigmented member of the Archaea from Egypt that produces extracellular poly(glutamic acid)
    • Hezayen F.F., Rehm B.H.A., Tindall B.J., and Steinbüchel A. Transfer of Natrialba asiatica B1T to Natrialba taiwanensis sp. nov., a novel extremely halophilic, aerobic, non-pigmented member of the Archaea from Egypt that produces extracellular poly(glutamic acid). Int. J. Syst. Evol. Microbiol. 51 (2001) 1133-1142
    • (2001) Int. J. Syst. Evol. Microbiol. , vol.51 , pp. 1133-1142
    • Hezayen, F.F.1    Rehm, B.H.A.2    Tindall, B.J.3    Steinbüchel, A.4
  • 22
    • 0024971240 scopus 로고
    • Nematocysts (stinging capsules of Cnidaria) as Donnan-potential-dominated osmotic systems
    • Weber J. Nematocysts (stinging capsules of Cnidaria) as Donnan-potential-dominated osmotic systems. Eur. J. Biochem. 184 (1989) 465-476
    • (1989) Eur. J. Biochem. , vol.184 , pp. 465-476
    • Weber, J.1
  • 23
    • 0025324529 scopus 로고
    • Poly(γ-glutamic acid)s are the major constituents of nematocysts in Hydra (Hydrozoa, Cnidaria)
    • Weber J. Poly(γ-glutamic acid)s are the major constituents of nematocysts in Hydra (Hydrozoa, Cnidaria). J. Biol. Chem. 265 (1990) 9664-9669
    • (1990) J. Biol. Chem. , vol.265 , pp. 9664-9669
    • Weber, J.1
  • 24
    • 0037545836 scopus 로고    scopus 로고
    • Characterization of poly-γ-glutamate hydrolase encoded by a bacteriophage genome: possible role in phage infection of Bacillus subtilis encapsulated with poly-γ-glutamate
    • Kimura K., and Itoh Y. Characterization of poly-γ-glutamate hydrolase encoded by a bacteriophage genome: possible role in phage infection of Bacillus subtilis encapsulated with poly-γ-glutamate. Appl. Environ. Microbiol. 69 (2003) 2491-2497
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 2491-2497
    • Kimura, K.1    Itoh, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.