Abstract
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.
Keywords: Parasitic infections, Trypanosoma cruzi, Inhibitors, Enzyme, Glyceraldehyde-3-phosphate dehydrogenase, X-ray crystallography
Letters in Drug Design & Discovery
Title: Kinetic and Crystallographic Studies on Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma cruzi in Complex with Iodoacetate
Volume: 6 Issue: 3
Author(s): Rafael V.C. Guido, Tatiane L. Balliano, Adriano D. Andricopulo and Glaucius Oliva
Affiliation:
Keywords: Parasitic infections, Trypanosoma cruzi, Inhibitors, Enzyme, Glyceraldehyde-3-phosphate dehydrogenase, X-ray crystallography
Abstract: 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.
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Cite this article as:
Guido V.C. Rafael, Balliano L. Tatiane, Andricopulo D. Adriano and Oliva Glaucius, Kinetic and Crystallographic Studies on Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma cruzi in Complex with Iodoacetate, Letters in Drug Design & Discovery 2009; 6 (3) . https://dx.doi.org/10.2174/157018009787847774
DOI https://dx.doi.org/10.2174/157018009787847774 |
Print ISSN 1570-1808 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-628X |
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