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Volumn 318, Issue 2, 2002, Pages 443-453

Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 α-amylase 1 (TVAI) at 1.6 Å resolution and α-amylase 2 (TVAII) at 2.3 Å resolution

Author keywords

Cyclodextrin; Enzymatic glucoside hydrolysis; Thermostability; X ray structure; amylase

Indexed keywords

AMYLASE 1; AMYLASE 2; BACTERIAL ENZYME; CYCLODEXTRIN; UNCLASSIFIED DRUG;

EID: 0036304348     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00111-0     Document Type: Article
Times cited : (55)

References (45)
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    • Studies on the hydrolyzing mechanism for cyclodextrins of Thermoactinomyces vulgaris R-47 a-amylase 2 (TVAII). X-ray structure of mutant E354A complexed with β-cyclodextrin, and kinetic analyses on cyclodextrins
    • (2001) J. Biochem. , vol.129 , pp. 423-428
    • Kondo, S.1    Ohtaki, A.2    Tonozuka, T.3    Sakano, Y.4    Kamitori, S.5
  • 15
    • 0035823414 scopus 로고    scopus 로고
    • Role of Phe286 in the cyclodextrin-recognition mechanism of Thermoactinomyces vulgaris R-47 α-amylase 2 (TVAII). X-ray structures of the TVAII-mutants F286A and F286Y, and kinetic analyses of the Phe286-replaced TVAII-mutants
    • (2001) Carbohydr. Res. , vol.334 , pp. 309-313
    • Ohtaki, A.1    Kondo, S.2    Tonozuka, T.3    Sakano, Y.4    Kamitori, S.5
  • 21
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnot, M.L.1
  • 44
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.