Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda (2012)
- Authors:
- USP affiliated authors: POLIKARPOV, IGOR - IFSC ; MARANA, SANDRO ROBERTO - IQ
- Unidades: IFSC; IQ
- Subjects: ENZIMAS (ESTUDO); PROTEÍNAS; AMINOÁCIDOS
- Language: Inglês
- Imprenta:
- Publisher: Wiley-Blackwell
- Publisher place: Oxford
- Date published: 2012
- Source:
- Título: FEBS Journal
- ISSN: 1742-464X
- Volume/Número/Paginação/Ano: v. 279, suppl. 1, p. 437, abstr. P 20-98, Sept. 2012
- Conference titles: Congress of the International Union of Biochemistry and Molecular Biology - IUBMB
-
ABNT
TAMAKI, F. K. et al. Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda. FEBS Journal. Oxford: Wiley-Blackwell. . Acesso em: 03 nov. 2024. , 2012 -
APA
Tamaki, F. K., Textor, L. C., Polikarpov, I., & Marana, S. R. (2012). Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda. FEBS Journal. Oxford: Wiley-Blackwell. -
NLM
Tamaki FK, Textor LC, Polikarpov I, Marana SR. Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda. FEBS Journal. 2012 ; 279 437.[citado 2024 nov. 03 ] -
Vancouver
Tamaki FK, Textor LC, Polikarpov I, Marana SR. Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda. FEBS Journal. 2012 ; 279 437.[citado 2024 nov. 03 ] - Sets of co-variant positions in β-glucosidases are involved in modulating the activity and the thermal stability
- Functional sectors involved in thermal stability and activity in beta-glucosidases
- Functional study of amino acid positions presenting coupled frequencies in Spodoptera frujiperda beta-glucosidase
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- Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans
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- Optimum temperature may be a misleading parameter in enzyme characterization and application
- Enzyme optimum temperature: constant or relative parameter?
- Role of the triad N46, S106 and T107 and the surface charges in the determination of the acidic pH optimum of digestive lysozymes from Musca domestica
- Additivity of mutational effects on the catalytic activity of a 'beta'glycosidase
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