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Kinetic properties and inhibition of the dimeric dUTPase-dUDPase from Leishmania major
Kinetic properties of the dimeric enzyme dUTPase from Leishmania major were studied using a continuous spectrophotometric method. dUTP was the natural substrate and dUMP and PPi the products of the hydrolysis. The trypanosomatid enzyme exhibited a low K(m) value for dUTP (2.11 μM), a k(cat) of 49 s(...
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| Autores principales: | , , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
Cold Spring Harbor Laboratory Press
2001
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2374113/ https://ncbi.nlm.nih.gov/pubmed/11420444 |
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