| Texto completo | |
| Autor(es): |
Walbert Veloso-Silva, Laudimir Leonardo
[1]
;
Dores-Silva, Paulo Roberto
[1]
;
Bertolino-Reis, Dayane Eliara
[1]
;
Moreno-Oliveira, Louis Fellipe
[1]
;
Libardi, Silvia Helena
[1]
;
Borges, Julio Cesar
[1]
Número total de Autores: 6
|
| Afiliação do(s) autor(es): | [1] Univ Sao Paulo, Sao Carlos Inst Chem, POB 780, BR-13560970 Sao Carlos, SP - Brazil
Número total de Afiliações: 1
|
| Tipo de documento: | Artigo Científico |
| Fonte: | Archives of Biochemistry and Biophysics; v. 661, p. 87-96, JAN 2019. |
| Citações Web of Science: | 1 |
| Resumo | |
First described in yeast in 1932 by Christian \& Warburg, the Old Yellow Enzyme (OYE) (EC 1.6.99.1) has aroused the interest of the scientific community regarding its high ability to catalyze stereoselective reactions of alpha/beta-unsaturated carbonyl compounds with important industrial applications. In addition, the OYE family of proteins has been found in different organisms, such as plants, bacteria and protozoa, but not in mammals, which makes it an excellent candidate for a functional and molecular study aimed at more effective therapies with fewer undesirable side effects. Several OYE orthologues have been characterized; however, the real physiological role for most members of this family of proteins remains a mystery. In this paper, we present the structural studies of the OYE of Leishmania braziliensis. The findings are discussed in comparison with OYE of Trypanosoma cruzi, revealing some biophysical differences. The main differences are related to their chemical and thermal stabilities and behavior in solution. In addition, the L. braziliensis OYE shape is more elongated than that of the T. cruzi orthologue. Despite this, the active sites of these enzymes do not appear to have major differences, since their interactions with the substrate menadione occur with an affinity of the same order of magnitude, revealing that the binding sites in both proteins are essentially similar. (AU) | |
| Processo FAPESP: | 11/23110-0 - Uso da calorimetria de titulação isotérmica para a determinação de propriedades termodinâmicas de interação de proteína-ligante e proteína-proteína |
| Beneficiário: | Julio Cesar Borges |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |
| Processo FAPESP: | 14/07206-6 - Estudos da HSP70 mitocondrial de humanos e de protozoários: abordagem estrutural e funcional |
| Beneficiário: | Julio Cesar Borges |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |
| Processo FAPESP: | 17/07335-9 - Estudos das isoformas da HSP70 humana residentes no citoplasma e mitocôndria e de seus oligômeros de alta massa molecular: interação com co-chaperonas e proteínas clientes |
| Beneficiário: | Julio Cesar Borges |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |