(Received: August 7, 2008; Accepted for publication: December 4, 2008)
Firefly luciferase is a well-known enzyme that participates in the bioluminescence reaction. Recently, it was reported that this enzyme also exhibits enantioselective thioester formation activity of 2-arylpropanoic acid such as ketoprofen. However, the enantiodifferential mechanism was still unknown. Therefore to clarify the reason of enantioselective thioester formation toward ketoprofen, we have performed molecular dynamics (MD) simulations for three kinds of firefly luciferase / acyl-AMP intermediate analogue complexes. Targeted substrates were N-acylsulfamate derivatives of R-ketoprofen, S-ketoprofen and 3-benzoylphenylacetic acids. Our results show that the dynamic behavior of Ser200 and Ser201 around the asymmetric carbon atom in the complexes is quite different.
Keywords: Firefly luciferase, Ketoprofen, Thioesterification, Enantioselectivity, Molecular dynamics
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