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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Structural and kinetic studies of Schistosoma mansoni adenylate kinases

Texto completo
Marques, Ivo de Almeida [1] ; Romanello, Larissa [2] ; DeMarco, Ricardo [2] ; Pereira, Humberto D'Muniz [2]
Número total de Autores: 4
Afiliação do(s) autor(es):
[1] Univ Fed Goias, Inst Fis, BR-74001970 Goiania, Go - Brazil
[2] Univ Sao Paulo, Inst Fis Sao Carlos, BR-13566590 Sao Carlos, SP - Brazil
Número total de Afiliações: 2
Tipo de documento: Artigo Científico
Fonte: Molecular and Biochemical Parasitology; v. 185, n. 2, p. 157-160, OCT 2012.
Citações Web of Science: 10

The human parasite Schistosoma mansoni is totally dependent on the purine salvage pathway in order to supply large quantities of purine precursors for its energy and DNA biosynthetic needs. Adenylate kinase (ADK) is responsible for the conversion of AMP (produced by the adenosine kinase reaction) into ADP, which is subsequently converted into ATP by nucleoside diphosphate kinase (NDPK). ADK and NDPK are the most active enzymes of the pathway, probably reflecting an evolutionary adaptation due to the intense use of the branch in which they participate. However, notwithstanding their importance very little information has been accumulated found regarding these enzymes. In this work two adenylate kinases from S. mansoni were cloned and heterologously expressed in Escherichia coil. The purified products were utilized in activity assays, and displayed kinetic parameters similar to the corresponding human orthologous proteins. The cytosolic S. mansoni ADK was crystallized and its structure solved allowing us to detect a difference in the nucleotide binding site when compared with the human ortholog. (C) 2012 Elsevier B.V. All rights reserved. (AU)

Processo FAPESP: 98/14138-2 - Center for Structural Molecular Biotechnology
Beneficiário:Glaucius Oliva
Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs
Processo FAPESP: 06/60280-3 - Ensaios de inibição enzimática e cristalografia de alvos protéicos de parasitas tropicais
Beneficiário:Humberto D'Muniz Pereira
Linha de fomento: Bolsas no Brasil - Pós-Doutorado