Subsites of trypsin active site favor catalysis or substrate binding (2002)
- Authors:
- USP affiliated authors: MARANA, SANDRO ROBERTO - IQ ; TERRA, CLELIA FERREIRA - IQ ; TERRA, WALTER RIBEIRO - IQ
- Unidade: IQ
- DOI: 10.1006/bbrc.2001.6172
- Subjects: CATÁLISE; REAÇÕES QUÍMICAS
- Language: Inglês
- Imprenta:
- Source:
- Título: Biochemical and Biophysical Research Communications
- ISSN: 0006-291X
- Volume/Número/Paginação/Ano: v. 290, n. 1, p. 494-497, 2002
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
-
ABNT
MARANA, Sandro Roberto et al. Subsites of trypsin active site favor catalysis or substrate binding. Biochemical and Biophysical Research Communications, v. 290, n. 1, p. 494-497, 2002Tradução . . Disponível em: https://doi.org/10.1006/bbrc.2001.6172. Acesso em: 11 fev. 2026. -
APA
Marana, S. R., Lopes, A. R., Juliano, L., Juliano, M. A., Ferreira, C., & Terra, W. R. (2002). Subsites of trypsin active site favor catalysis or substrate binding. Biochemical and Biophysical Research Communications, 290( 1), 494-497. doi:10.1006/bbrc.2001.6172 -
NLM
Marana SR, Lopes AR, Juliano L, Juliano MA, Ferreira C, Terra WR. Subsites of trypsin active site favor catalysis or substrate binding [Internet]. Biochemical and Biophysical Research Communications. 2002 ; 290( 1): 494-497.[citado 2026 fev. 11 ] Available from: https://doi.org/10.1006/bbrc.2001.6172 -
Vancouver
Marana SR, Lopes AR, Juliano L, Juliano MA, Ferreira C, Terra WR. Subsites of trypsin active site favor catalysis or substrate binding [Internet]. Biochemical and Biophysical Research Communications. 2002 ; 290( 1): 494-497.[citado 2026 fev. 11 ] Available from: https://doi.org/10.1006/bbrc.2001.6172 - The active site of a midgut trehalase from Tenebrio molitor larvae
- Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis
- Subsite of trypsin active site favor catalysis or substrate binding
- The role of residues R97 and Y331 in modulating the pH optimum of an insect 'beta'-glycosidase of family 1
- Crystallization, data collection and phasing of two digestive lysozymes from Musca domestica
- Site-directed mutagenesis of amino acid residues involved in the determination of the substrate specificity in a beta-glycosidase
- Expression, purification and crystallization of a recombinant digestive lysozyme from Musca domestica (diptera - insecta)
- Purification and molecular cloning of an intestinal trehalase from Tenebrio molitor larvae
- Papel da R97 e da Y331 na determinação do pH ótimo em uma beta-glicosidase
- Cloning and sequencing lysozyme genes from Musca domestica
Informações sobre o DOI: 10.1006/bbrc.2001.6172 (Fonte: oaDOI API)
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