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	Provedor de dados BJMBR (1) Electron. J. Biotechnol. (1) J. Venom. Anim. Toxins incl. Trop. Dis. (1) Autor Chioato,Lucimara (1) Cury,Yara (1) Gonçalves,L.M. (1) Guo,Yiming (1) Gutierrez,Vanessa Pacciari (1) Kumar,Ashok (1) Liu,Ziduo (1) Marana,S.R. (1) Rozenfeld,J.H.K. (1) Tomassi,M.H. (1) Ward,Richard John (1) Wu,Gaobing (1) Zambelli,Vanessa Olzon (1) Zhan,Tao (1) Mais... Palavra-chave Site-directed mutagenesis (3) Bacillus cereus (1) Edema (1) Error-prone PCR (1) Glycine oxidase (1) Hyperalgesia (1) Lys49-Phospholipase A2 (1) Membrane damage (1) Myotoxic effect (1) Spodoptera frugiperda (1) Substrate affinity (1) Substrate specificity (1) Β-glycosidase (1) Mais... Tipo do documento Info:eu-repo/semantics/article (1) Info:eu-repo/semantics/other (1) Journal article (1) Ano 2017 (1) 2016 (1) 2010 (1) País Brazil (2) Chile (1) Idioma Inglês (3)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 3 Primeira ... 1 ... Última Characterization of the interdependency between residues that bind the substrate in a β-glycosidase BJMBR Tomassi,M.H.; Rozenfeld,J.H.K.; Gonçalves,L.M.; Marana,S.R.. The manner by which effects of simultaneous mutations combine to change enzymatic activity is not easily predictable because these effects are not always additive in a linear manner. Hence, the characterization of the effects of simultaneous mutations of amino acid residues that bind the substrate can make a significant contribution to the understanding of the substrate specificity of enzymes. In the β-glycosidase from Spodoptera frugiperda (Sfβgly), both residues Q39 and E451 interact with the substrate and this is essential for defining substrate specificity. Double mutants of Sfβgly (A451E39, S451E39 and S451N39) were prepared by site-directed mutagenesis, expressed in bacteria and purified using affinity chromatography. These enzymes were characterized... Tipo: Info:eu-repo/semantics/other Palavras-chave: Β-glycosidase; Substrate specificity; Site-directed mutagenesis; Spodoptera frugiperda. Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2010000100002 Asn336 is involved in the substrate affinity of glycine oxidase from Bacillus cereus Electron. J. Biotechnol. Wu,Gaobing; Zhan,Tao; Guo,Yiming; Kumar,Ashok; Liu,Ziduo. Background: Glycine oxidase (GO), a type of D-amino acid oxidase, is of biotechnological interest for its potential in several fields. In our previous study, we have characterized a new glycine oxidase (BceGO) from Bacillus cereus HYC-7. Here, a variant of N336K with increased the affinity against all the tested substrate was obtained by screening a random mutant library of BceGO. It is observed that the residue N336 is invariable between its homogeneous enzymes. This work was aimed to explore the role of the residue N336 in glycine oxidase by site-directed mutagenesis, kinetic assay, structure modeling and substrate docking. Results: The results showed that the affinity of N336H, N336K and N336R increased gradually toward all the substrates, with increase... Tipo: Journal article Palavras-chave: Bacillus cereus; Error-prone PCR; Glycine oxidase; Site-directed mutagenesis; Substrate affinity. Ano: 2016 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000400004 Structural determinants of the hyperalgesic activity of myotoxic Lys49-phospholipase A2 J. Venom. Anim. Toxins incl. Trop. Dis. Zambelli,Vanessa Olzon; Chioato,Lucimara; Gutierrez,Vanessa Pacciari; Ward,Richard John; Cury,Yara. Abstract Background Bothropstoxin-I (BthTx-I) is a Lys49-phospholipase A2 (Lys49-PLA2) from the venom of Bothrops jararacussu, which despite of the lack of catalytic activity induces myotoxicity, inflammation and pain. The C-terminal region of the Lys49-PLA2s is important for these effects; however, the amino acid residues that determine hyperalgesia and edema are unknown. The aim of this study was to characterize the structural determinants for the Lys49-PLA2-induced nociception and inflammation. Methods Scanning alanine mutagenesis in the active-site and C-terminal regions of BthTx-I has been used to study the structural determinants of toxin activities. The R118A mutant was employed as this substitution decreases PLA2 myotoxicity. In addition, K115A... Tipo: Info:eu-repo/semantics/article Palavras-chave: Lys49-Phospholipase A2; Hyperalgesia; Site-directed mutagenesis; Myotoxic effect; Edema; Membrane damage. Ano: 2017 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100304 Registros recuperados: 3 Primeira ... 1 ... Última

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