Structural and molecular basis for the acidic pH optimum of digestive lysozymes from housefly Musca domestica (2011)
- Authors:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- Subjects: LISOZIMAS; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Febs Journal
- ISSN: 1742-464X
- Volume/Número/Paginação/Ano: v. 278, suppl. 1, p. 117 res. 003.87, 2011
- Conference titles: FEBS Congress of the Biochemistry for Tomorrows Medicine
-
ABNT
MARANA, Sandro Roberto et al. Structural and molecular basis for the acidic pH optimum of digestive lysozymes from housefly Musca domestica. Febs Journal. Malden: Instituto de Química, Universidade de São Paulo. . Acesso em: 23 abr. 2024. , 2011 -
APA
Marana, S. R., Cançado, F. C., Souza, V. P., & Barbosa, J. A. R. G. (2011). Structural and molecular basis for the acidic pH optimum of digestive lysozymes from housefly Musca domestica. Febs Journal. Malden: Instituto de Química, Universidade de São Paulo. -
NLM
Marana SR, Cançado FC, Souza VP, Barbosa JARG. Structural and molecular basis for the acidic pH optimum of digestive lysozymes from housefly Musca domestica. Febs Journal. 2011 ; 278 117 res. 003.87.[citado 2024 abr. 23 ] -
Vancouver
Marana SR, Cançado FC, Souza VP, Barbosa JARG. Structural and molecular basis for the acidic pH optimum of digestive lysozymes from housefly Musca domestica. Febs Journal. 2011 ; 278 117 res. 003.87.[citado 2024 abr. 23 ] - 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
- Role of residue E190 in modulating aglycone specificity of a 'beta'-glycosidase from spodoptera frugiperda (SFBGLI50-AF 052729) of family 1
- In vitro evolution of beta-glucosidase from Spodoptera frugiperda, aiming at second generation ethanol
- Data supporting the hypothesis that contact pathways modulate the substrate specificity of a β-glucosidase
- Mapping of amino acid residues involved in the thermal stability of a beta-glucosidase
- Standardization of a method of In vitro evolution of beta-glycosidases
- The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase
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