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

• Type: Article in International Scientific Journal
• Date: 2012

Authors

da silva, lp (Author) Other; vieira, j (Author) Other; da silva, jcge (Author) FCUP

Journal

Title: Chemical Physics Letters

Vol. 543

Pages: 137-141

ISSN: 0009-2614

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 9 Citations

Scopus - 9 Citations

Scientific classification

FOS: Natural sciences > Chemical sciences

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 5