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Volumn 46, Issue 1, 2010, Pages 1-8

A functional comparison of the TET aminopeptidases of P. furiosus and B. subtilis with a protein-engineered variant recombining the former's structure with the latter's active site

Author keywords

Active site transplantation; Enzyme characterization; Enzyme engineering; Protein engineering

Indexed keywords

ACTIVE SITE; ACTIVE SITE TRANSPLANTATION; AMINO PEPTIDASE; BACILLUS SUBTILIS; ENZYME CHARACTERIZATION; ENZYME ENGINEERING; GUIDED MUTATION; OPTIMAL FUNCTION; PROTEIN ENGINEERING; PYROCOCCUS FURIOSUS; SUBTILIS;

EID: 70350127725     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2009.09.003     Document Type: Article
Times cited : (6)

References (6)
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  • 2
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  • 3
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    • Russo, S.1    Baumann, U.2
  • 4
    • 0031722406 scopus 로고    scopus 로고
    • Purification and application of a novel N-terminal deblocking aminopeptidase (DAP) from Pyrococcus furiosus
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  • 5
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  • 6
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    • Replacement of the active surface of a thermophile protein by that of a homologous mesophile protein through structure-guided 'protein surface grafting'
    • Kapoor D., Kumar V., Chandrayan S.K., Ahmed S., Sharma S., Datt M., et al. Replacement of the active surface of a thermophile protein by that of a homologous mesophile protein through structure-guided 'protein surface grafting'. Biochim Biophys Acta 1784 (2007) 1771-1776
    • (2007) Biochim Biophys Acta , vol.1784 , pp. 1771-1776
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.