A single amino acid residue determines the ratio of hydrolysis to transglycosylation catalyzed by beta-glucosidases (2013)
- Authors:
- Autor USP: MARANA, SANDRO ROBERTO - IQ
- Unidade: IQ
- DOI: 10.2174/092986613804096757
- Subjects: OLIGOSSACARÍDEOS; AMINOÁCIDOS
- Language: Inglês
- Imprenta:
- Source:
- Título: Protein and Peptide Letters
- ISSN: 0929-8665
- Volume/Número/Paginação/Ano: v. 20, n. 1, p. 102-106,
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
-
ABNT
FRUTUOSO, Maria Artischeeff e MARANA, Sandro Roberto. A single amino acid residue determines the ratio of hydrolysis to transglycosylation catalyzed by beta-glucosidases. Protein and Peptide Letters, v. 20, n. 1, p. 102-106, 2013Tradução . . Disponível em: https://doi.org/10.2174/092986613804096757. Acesso em: 27 dez. 2025. -
APA
Frutuoso, M. A., & Marana, S. R. (2013). A single amino acid residue determines the ratio of hydrolysis to transglycosylation catalyzed by beta-glucosidases. Protein and Peptide Letters, 20( 1), 102-106. doi:10.2174/092986613804096757 -
NLM
Frutuoso MA, Marana SR. A single amino acid residue determines the ratio of hydrolysis to transglycosylation catalyzed by beta-glucosidases [Internet]. Protein and Peptide Letters. 2013 ; 20( 1): 102-106.[citado 2025 dez. 27 ] Available from: https://doi.org/10.2174/092986613804096757 -
Vancouver
Frutuoso MA, Marana SR. A single amino acid residue determines the ratio of hydrolysis to transglycosylation catalyzed by beta-glucosidases [Internet]. Protein and Peptide Letters. 2013 ; 20( 1): 102-106.[citado 2025 dez. 27 ] Available from: https://doi.org/10.2174/092986613804096757 - 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
- 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?
- 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
Informações sobre o DOI: 10.2174/092986613804096757 (Fonte: oaDOI API)
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