Dynamics of the substrate binding pocket in the presence of an inhibitor covalently attached to a fungal lipase.
作者： Günther H. Peters , Morten Ø. Jensen , Robert P. Bywater
DOI: 10.1080/07391102.2001.10506716
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摘要: Abstract To gain insight into the mobility of occupied ligand-binding pocket Rhizomucor miehei lipase we have conducted a rigorous molecular dynamics analysis. The covalently attached inhibitor, ethylhexylphosphonate, was employed as mimic putative tetrahedral intermediate in esterolytic reaction. Our results show that this lipase, ligand recognition is influenced by flexibility binding pocket, feature common to many other enzymes. Several regions around active site were found move significantly adapt inhibitor. These motions are correlated In particular, hexyl chain inhibitor shows considerable mobility, and adjacent residues cleft accommodate flexibility. Pronounced fluctuations induced observed hinge region F79-S82, loop W88-V95 protein P209-F215/H257-Y260. f...
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