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Volumn 71, Issue 10, 2007, Pages 2585-2587

Analysis of the putative substrate binding region of hyperthermophilic endoglucanase from Pyrococcus horikoshii

Author keywords

Active site; Cellulase; Endoglucanase; Hyperthermophilic; Protein engineering

Indexed keywords

AMINO ACIDS; BIOMASS; CATALYST ACTIVITY; ENZYMES;

EID: 36148935237     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70322     Document Type: Article
Times cited : (12)

References (7)
  • 1
    • 0036136959 scopus 로고    scopus 로고
    • Hyperthermostable endoglucanase from Pyrococcus horikoshii
    • Ando, S., Ishida, H., Kosugi, Y., and Ishikawa, K., Hyperthermostable endoglucanase from Pyrococcus horikoshii. Appl. Environ. Microbiol., 68, 430-433 (2002).
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 430-433
    • Ando, S.1    Ishida, H.2    Kosugi, Y.3    Ishikawa, K.4
  • 2
    • 0029740205 scopus 로고    scopus 로고
    • Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose
    • Sakon, J., Adney, W. S., Himmel, M. E., Thomas, S. R., and Karplus, P. A., Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose. Biochemistry, 35, 10648-10660 (1996).
    • (1996) Biochemistry , vol.35 , pp. 10648-10660
    • Sakon, J.1    Adney, W.S.2    Himmel, M.E.3    Thomas, S.R.4    Karplus, P.A.5
  • 3
    • 14644419633 scopus 로고    scopus 로고
    • Analysis of the function of a hyperthermophilic endoglucanase from Pyrococcus horikoshii that hydrolyzes crystalline cellulose
    • Kashima, Y., Mori, K., Fukada, H., and Ishikawa, K., Analysis of the function of a hyperthermophilic endoglucanase from Pyrococcus horikoshii that hydrolyzes crystalline cellulose. Extremophiles, 9, 37-43 (2005).
    • (2005) Extremophiles , vol.9 , pp. 37-43
    • Kashima, Y.1    Mori, K.2    Fukada, H.3    Ishikawa, K.4
  • 4
    • 0007496445 scopus 로고
    • Kinetics of hydrolytic reaction catalyzed by crystalline bacterial α-amylase: The influence of temperature
    • Hiromi, K., Takahashi, Y., and Ono, S., Kinetics of hydrolytic reaction catalyzed by crystalline bacterial α-amylase: the influence of temperature. Bull. Chem. Soc. Jpn., 36, 563-569 (1963).
    • (1963) Bull. Chem. Soc. Jpn , vol.36 , pp. 563-569
    • Hiromi, K.1    Takahashi, Y.2    Ono, S.3
  • 5
    • 33847258778 scopus 로고    scopus 로고
    • Improvement of the enzymatic activity of the hyperthermophilic cellulase from Pyrococcus horikoshii
    • Kang, H.-J., Uegaki, K., Fukada, H., and Ishikawa, K., Improvement of the enzymatic activity of the hyperthermophilic cellulase from Pyrococcus horikoshii. Extremophiles, 11, 251-256 (2006).
    • (2006) Extremophiles , vol.11 , pp. 251-256
    • Kang, H.-J.1    Uegaki, K.2    Fukada, H.3    Ishikawa, K.4
  • 6
    • 0037125126 scopus 로고    scopus 로고
    • The 1.62Å structure of Thermoascus aurantiacus endoglucanase: Completing the structural picture of subfamilies in glycoside hydrolase family 5
    • Leggio, L. L., and Larsen, S., The 1.62Å structure of Thermoascus aurantiacus endoglucanase: completing the structural picture of subfamilies in glycoside hydrolase family 5. FEBS Lett., 523, 103-108 (2002).
    • (2002) FEBS Lett , vol.523 , pp. 103-108
    • Leggio, L.L.1    Larsen, S.2
  • 7
    • 0005499841 scopus 로고
    • Statistical estimations in enzyme kinetics
    • Wilkinson, G. N., Statistical estimations in enzyme kinetics. Biochem. J., 80, 324-332 (1961).
    • (1961) Biochem. J , vol.80 , pp. 324-332
    • Wilkinson, G.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.