Kinetic and Crystallographic Studies on Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma cruzi in Complex with Iodoacetate
Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
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Data(s) |
20/10/2012
20/10/2012
2009
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Resumo |
Kinetic and crystallographic studies on the formation of the complex between iodoacetate and the enzyme glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi were conducted in order to investigate the mechanistic and structural basis underlying enzyme inactivation. The crystallographic complex reveal important structural features useful for the design of novel inhibitors. Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) FAPESP (The State of Sao Paulo Research Foundation) CNPq (The National Council for Scientific and Technological Development), Brazil Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) |
Identificador |
LETTERS IN DRUG DESIGN & DISCOVERY, v.6, n.3, p.210-214, 2009 1570-1808 |
Idioma(s) |
eng |
Publicador |
BENTHAM SCIENCE PUBL LTD |
Relação |
Letters in Drug Design & Discovery |
Direitos |
restrictedAccess Copyright BENTHAM SCIENCE PUBL LTD |
Palavras-Chave | #Parasitic infections #Trypanosoma cruzi #Inhibitors #Enzyme #Glyceraldehyde-3-phosphate dehydrogenase #X-ray crystallography #D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE #SELECTIVE-INHIBITION #CRYSTAL-STRUCTURE #DESIGN #GLYCOLYSIS #ANALOG #QSAR #Chemistry, Medicinal |
Tipo |
article original article publishedVersion |