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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Structural studies of Old Yellow Enzyme of Leishmania braziliensis in solution

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Author(s):
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]
Total Authors: 6
Affiliation:
[1] Univ Sao Paulo, Sao Carlos Inst Chem, POB 780, BR-13560970 Sao Carlos, SP - Brazil
Total Affiliations: 1
Document type: Journal article
Source: Archives of Biochemistry and Biophysics; v. 661, p. 87-96, JAN 2019.
Web of Science Citations: 1
Abstract

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)

FAPESP's process: 11/23110-0 - Using isothermal titration calorimetry for the determination of thermodynamic properties of protein-ligand and protein-protein interactions
Grantee:Julio Cesar Borges
Support Opportunities: Regular Research Grants
FAPESP's process: 14/07206-6 - Studies of the mitochondrial HSP70 of human and protozoa: structural and functional approaches
Grantee:Julio Cesar Borges
Support Opportunities: Regular Research Grants
FAPESP's process: 17/07335-9 - Studies of human HSP70 isoforms residing in the cytoplasm and mitochondria and their high molecular weight oligomers: interaction with co-chaperones and client proteins
Grantee:Julio Cesar Borges
Support Opportunities: Regular Research Grants