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Volumn 25, Issue 11, 2012, Pages 781-788

Engineering catalytic properties and thermal stability of plant formate dehydrogenase by single-point mutations

Author keywords

modeling; rational design; site directed mutagenesis; soya Glycine max; structure

Indexed keywords

AMINO ACID SUBSTITUTION; ARABIDOPSIS THALIANA; AZIDE ION; CANDIDA BOIDINII; CATALYTIC CONSTANTS; CATALYTIC PROPERTIES; COMPUTER MODELING; ENZYME ACTIVE SITES; FORMATE DEHYDROGENASE; GLYCINE MAX; RATIONAL DESIGN; SINGLE-POINT MUTATION; SITE DIRECTED MUTAGENESIS; TERNARY COMPLEX; THERMAL INACTIVATION; WILD-TYPE ENZYMES;

EID: 84868608812     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzs084     Document Type: Conference Paper
Times cited : (28)

References (26)
  • 11
    • 11144245250 scopus 로고    scopus 로고
    • NAD+-dependent formate dehydrogenase. from a model enzyme to a versatile biocatalyst
    • Uversky, V. N. (ed) . Research Signpost, Kerala, India, ISBN: 81-7736-177-5
    • Popov, V. O. and Tishkov, V. I. (2003) In Uversky,, V. N. (ed), NAD+-dependent formate dehydrogenase. From a model enzyme to a versatile biocatalyst. in Protein Structures: Kaleidoscope of Structural Properties and Functions. Research Signpost, Kerala, India, ISBN: 81-7736-177-5, pp. 441-473
    • (2003) Protein Structures: Kaleidoscope of Structural Properties and Functions , pp. 441-473
    • Popov, V.O.1    Tishkov, V.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.