Comparative theoretical study of the binding of luciferyl-adenylate and dehydroluciferyl-adenylate to firefly luciferase

• Tipo: Artigo em Revista Científica Internacional
• Data: 2012

Autores

da silva, lp (Autor) Outra; vieira, j (Autor) Outra; da silva, jcge (Autor) FCUP

Revista

Título: Chemical Physics Letters

Vol. 543

Páginas: 137-141

ISSN: 0009-2614

Editora: Elsevier

Indexação

ISI Web of Knowledge - 9 Citações

Scopus - 9 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Química

Outras Informações

ID Authenticus: P-002-6Z8

DOI: 10.1016/j.cplett.2012.06.038

Abstract (EN): This is the first report of a study employing a computational approach to study the binding of (D/L)-luciferyl-adenlyates and dehydroluciferyl-adenylate to firefly luciferase. A semi-empirical/molecular mechanics methodology was used to study the interaction between these ligands and active site molecules. All adenylates are complexed with the enzyme, mostly due to electrostatic interactions with cationic residues. Dehydroluciferyl-adenylate is expected to be a competitive inhibitor of luciferyl-adenylate, as their binding mechanism and affinity to luciferase are very similar. Both luciferyl-adenylates adopt the L-orientation in the active site of luciferase.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 5