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Volumn 70, Issue 2, 2004, Pages 937-942

Highly Stable L-Lysine 6-Dehydrogenase from the Thermophile Geobacillus stearothermophilus Isolated from a Japanese Hot Spring: Characterization, Gene Cloning and Sequencing, and Expression

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CLONING; ENZYMES; ESCHERICHIA COLI; GENES;

EID: 2342617445     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.70.2.937-942.2004     Document Type: Article
Times cited : (19)

References (27)
  • 1
    • 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
  • 2
    • 0014023195 scopus 로고
    • L-Lysine dehydrogenase deficiency in a patient with congenital lysine intolerance
    • Burgi, W., R. Ricchterich, and J. P. Colombo. 1966. L-Lysine dehydrogenase deficiency in a patient with congenital lysine intolerance. Nature 211:854-855.
    • (1966) Nature , vol.211 , pp. 854-855
    • Burgi, W.1    Ricchterich, R.2    Colombo, J.P.3
  • 3
    • 0030693246 scopus 로고    scopus 로고
    • 1-Piperideine-6-carboxylate dehydrogenase, a new enzyme that forms α-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes
    • 1-Piperideine-6-carboxylate dehydrogenase, a new enzyme that forms α-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes. Biochem. J. 327:59-64.
    • (1997) Biochem. J. , vol.327 , pp. 59-64
    • De La Fuente, J.L.1    Rumbero, A.2    Martin, J.F.3    Liras, P.4
  • 4
    • 0026534677 scopus 로고
    • A lysine dehydrogenase-based electrode for biosensing of L-lysine
    • Dempsey, E., J. Wang, U. Wollenberger, and M. Ozsoz. 1992. A lysine dehydrogenase-based electrode for biosensing of L-lysine. Biosens. Bioelectron. 7:323-327.
    • (1992) Biosens. Bioelectron. , vol.7 , pp. 323-327
    • Dempsey, E.1    Wang, J.2    Wollenberger, U.3    Ozsoz, M.4
  • 5
    • 0036490960 scopus 로고    scopus 로고
    • Biotransformation of L-lysine to L-pipecolic acid catalyzed by L-lysine 6-aminotransferase and pyrroline-5-carboxylate reductase
    • Fujii, T., M. Mukaihara, H. Agematu, and H. Tsunekawa. 2002. Biotransformation of L-lysine to L-pipecolic acid catalyzed by L-lysine 6-aminotransferase and pyrroline-5-carboxylate reductase. Biosci. Biotechnol. Biochem. 66:622-627.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 622-627
    • Fujii, T.1    Mukaihara, M.2    Agematu, H.3    Tsunekawa, H.4
  • 7
    • 0026029478 scopus 로고
    • Occurrence of a novel yeast enzyme, L-lysine ε-dehydrogenase, which catalyzes the first step of lysine catabolism in Candida albicans
    • Hammer, T., R. Bode, and D. Birnbaum. 1991. Occurrence of a novel yeast enzyme, L-lysine ε-dehydrogenase, which catalyzes the first step of lysine catabolism in Candida albicans. J. Gen. Microbiol. 137:711-715.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 711-715
    • Hammer, T.1    Bode, R.2    Birnbaum, D.3
  • 8
    • 0024698252 scopus 로고
    • Activation of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens by several amino acids and monocarboxylates
    • Hashimoto, H., H. Misono, S. Nagata, and S. Nagasaki. 1989. Activation of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens by several amino acids and monocarboxylates. J. Biochem. 106:76-80.
    • (1989) J. Biochem. , vol.106 , pp. 76-80
    • Hashimoto, H.1    Misono, H.2    Nagata, S.3    Nagasaki, S.4
  • 9
    • 85004332593 scopus 로고
    • Selective determination of L-lysine with L-lysine ε-dehydrogenase
    • Hashimoto, H., H. Misono, S. Nagata, and S. Nagasaki. 1990. Selective determination of L-lysine with L-lysine ε-dehydrogenase. Agric. Biol. Chem. 54:291-294.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 291-294
    • Hashimoto, H.1    Misono, H.2    Nagata, S.3    Nagasaki, S.4
  • 10
    • 85005697480 scopus 로고
    • Dehydrogenases for the synthesis of chiral compounds
    • Hummel, W., and M.-R. Kula. 1989. Dehydrogenases for the synthesis of chiral compounds. Eur. J. Biochem. 184:1-13.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 1-13
    • Hummel, W.1    Kula, M.-R.2
  • 12
    • 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
  • 13
    • 0035910123 scopus 로고    scopus 로고
    • Oceanobacillus iheyensis gen. nov., sp. nov., a deep-sea extremely halotolerant and alkaliphilic species isolated from a depth of 1050 m on the Iheya Ridge
    • Lu, J., Y. Nogi, and H. Takami. 2002. Oceanobacillus iheyensis gen. nov., sp. nov., a deep-sea extremely halotolerant and alkaliphilic species isolated from a depth of 1050 m on the Iheya Ridge. FEMS Microbiol. Lett. 205:291-297.
    • (2002) FEMS Microbiol. Lett. , vol.205 , pp. 291-297
    • Lu, J.1    Nogi, Y.2    Takami, H.3
  • 14
    • 0018411624 scopus 로고
    • Two-dimensional electrophoresis of plasma proteins without denaturing agents
    • Manabe, T., K. Tachi, K. Kijima, and T. Okayama. 1979. Two-dimensional electrophoresis of plasma proteins without denaturing agents. J. Biochem. (Tokyo) 85:649-659.
    • (1979) J. Biochem. (Tokyo) , vol.85 , pp. 649-659
    • Manabe, T.1    Tachi, K.2    Kijima, K.3    Okayama, T.4
  • 15
    • 0024676699 scopus 로고
    • Properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens
    • Misono, H., H. Hashimoto, H. Uehigashi, S. Nagata, and S. Nagasaki. 1989. Properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens. J. Biochem. 105:1002-1008.
    • (1989) J. Biochem. , vol.105 , pp. 1002-1008
    • Misono, H.1    Hashimoto, H.2    Uehigashi, H.3    Nagata, S.4    Nagasaki, S.5
  • 16
    • 0343879594 scopus 로고
    • Distribution and physiological function of L-lysine ε-dehydrogenase
    • Misono, H., and S. Nagasaki. 1983. Distribution and physiological function of L-lysine ε-dehydrogenase. Agric. Biol. Chem. 47:631-633.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 631-633
    • Misono, H.1    Nagasaki, S.2
  • 17
    • 0019983852 scopus 로고
    • Occurrence of L-lysine ε-dehydrogenase in Agrobacterium tumefaciens
    • Misono, H., and S. Nagasaki. 1982. Occurrence of L-lysine ε-dehydrogenase in Agrobacterium tumefaciens. J. Bacteriol. 150:398-401.
    • (1982) J. Bacteriol. , vol.150 , pp. 398-401
    • Misono, H.1    Nagasaki, S.2
  • 18
    • 0008956970 scopus 로고
    • Purification and properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens
    • Misono, H., H. Uehigashi, E. Morimoto, and S. Nagasaki. 1985. Purification and properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens. Agric. Biol. Chem. 49:2253-2255.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 2253-2255
    • Misono, H.1    Uehigashi, H.2    Morimoto, E.3    Nagasaki, S.4
  • 19
    • 0035725687 scopus 로고    scopus 로고
    • A novel hyperthermophilic archaeal glyoxylate reductase from Thermococcus litralis
    • Ohshima, T., and H. Sakuraba. 2001. A novel hyperthermophilic archaeal glyoxylate reductase from Thermococcus litralis. Eur. J. Biochem. 268:4740-4747.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4740-4747
    • Ohshima, T.1    Sakuraba, H.2
  • 20
    • 0022630727 scopus 로고
    • Purification and characterization of malate dehydrogenase from the phototropic bacterium, Rhodopseudomonas capsulata
    • Ohshima, T., and H. Sakuraba. 1986. Purification and characterization of malate dehydrogenase from the phototropic bacterium, Rhodopseudomonas capsulata. Biochim. Biophys. Acta 869:171-177.
    • (1986) Biochim. Biophys. Acta , vol.869 , pp. 171-177
    • Ohshima, T.1    Sakuraba, H.2
  • 21
    • 2342601115 scopus 로고    scopus 로고
    • Stereoselective biocatalysis: Amino acid dehydrogenases, their applications
    • R. N. Patel (ed.). Marcel Dekker Inc., New York, N.Y.
    • Ohshima, T., and K. Soda. 2000. Stereoselective biocatalysis: amino acid dehydrogenases, their applications, p. 877-902. In R. N. Patel (ed.), Stereo-selective biocatalysis. Marcel Dekker Inc., New York, N.Y.
    • (2000) Stereo-Selective Biocatalysis , pp. 877-902
    • Ohshima, T.1    Soda, K.2
  • 22
    • 0024711964 scopus 로고
    • Thermostable amino acid dehydrogenases: Applications and gene cloning
    • Ohshima, T., and K. Soda. 1989. Thermostable amino acid dehydrogenases: applications and gene cloning. Trends Biotechnol. 7:210-214.
    • (1989) Trends Biotechnol. , vol.7 , pp. 210-214
    • Ohshima, T.1    Soda, K.2
  • 24
    • 0017681196 scopus 로고
    • DNA sequencing with chain-terminating inhibitors
    • Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. 74:5463-5467.
    • (1977) Proc. Natl. Acad. Sci. , vol.74 , pp. 5463-5467
    • Sanger, F.1    Nicklen, S.2    Coulson, A.R.3
  • 25
    • 0037106449 scopus 로고    scopus 로고
    • Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments
    • Takami, H., Takaki, Y., and I. Uchiyama. 2002. Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments. Nucleic Acids Res. 30: 3927-3935.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3927-3935
    • Takami, H.1    Takaki, Y.2    Uchiyama, I.3
  • 26
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding β-α-β fold in proteins, using an amino acid sequence fingerprint
    • Wierenga, R. K., P. Terpsta, and W. G. J. Hol. 1986. Prediction of the occurrence of the ADP-binding β-α-β fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187:101-107.
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpsta, P.2    Hol, W.G.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.