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 (2010)
- Authors:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- DOI: 10.1016/j.cbpb.2010.01.001
- Subjects: LISOZIMAS; ENZIMAS HIDROLÍTICAS
- Language: Inglês
- Imprenta:
- Source:
- Título: Comparative Biochemistry and Physiology, Part B
- ISSN: 1096-4959
- Volume/Número/Paginação/Ano: v. 155, n. 4, p. 387-395, 2010
- Este periódico é de assinatura
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: hybrid
- Licença: unspecified-oa
-
ABNT
CANÇADO, Fabiane Chaves e BARBOSA, João Alexandre Ribeiro Gonçalves e MARANA, Sandro Roberto. 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. Comparative Biochemistry and Physiology, Part B, v. 155, n. 4, p. 387-395, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.cbpb.2010.01.001. Acesso em: 28 dez. 2025. -
APA
Cançado, F. C., Barbosa, J. A. R. G., & Marana, S. R. (2010). 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. Comparative Biochemistry and Physiology, Part B, 155( 4), 387-395. doi:10.1016/j.cbpb.2010.01.001 -
NLM
Cançado FC, Barbosa JARG, Marana SR. 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 [Internet]. Comparative Biochemistry and Physiology, Part B. 2010 ; 155( 4): 387-395.[citado 2025 dez. 28 ] Available from: https://doi.org/10.1016/j.cbpb.2010.01.001 -
Vancouver
Cançado FC, Barbosa JARG, Marana SR. 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 [Internet]. Comparative Biochemistry and Physiology, Part B. 2010 ; 155( 4): 387-395.[citado 2025 dez. 28 ] Available from: https://doi.org/10.1016/j.cbpb.2010.01.001 - Single mutations outside the active site affect the substrate specificity in a ß-glycosidade
- Structural and molecular basis for the acidic pH optimum of digestive lysozymes from housefly Musca domestica
- Characterization of '(β/α)'IND. 8'-barrel β-glycosidase
- A single amino acid residue determines the ratio of hydrolysis to transglycosylation catalyzed by beta-glucosidases
- Using the amino acid network to modulate the hydrolytic activity of beta-Glycosidases
- Protein thermal stability modulated by Hub residues
- Optimum temperature may be a misleading parameter in enzyme characterization and application
- Enzyme optimum temperature: constant or relative parameter?
- 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
Informações sobre o DOI: 10.1016/j.cbpb.2010.01.001 (Fonte: oaDOI API)
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
