Active serine involved in the stabilization of the active site loop in the Humicola lanuginosa lipase

We have investigated the binding properties of and dynamics in Humicola lanuginosa lipase (Hll) and the inactive mutant S146A (active Ser146 substituted with Ala) using fluorescence spectroscopy and molecular dynamics simulations, respectively. Hll and S146A show significantly different binding beha...

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Veröffentlicht in:	Biochemistry (Easton) 1998-09, Vol.37 (36), p.12375-12383
Hauptverfasser:	Peters, G.H. (University of Copenhagen, Copenhagen, Denmark.), Svendsen, A, Langberg, H, Vind, J, Patkar, S.A, Toxvaerd, S, Kinnunen, P.K.J
Format:	Artikel
Sprache:	eng
Schlagworte:	Alanine - genetics BINDING SITES Binding Sites - genetics Dimyristoylphosphatidylcholine - chemistry Dimyristoylphosphatidylcholine - metabolism Enzyme Stability HUMICOLA Humicola lanuginosa Lipase - chemistry Lipase - genetics Lipase - metabolism Liposomes - chemistry Liposomes - metabolism Mitosporic Fungi - enzymology Mitosporic Fungi - genetics Models, Molecular Mutagenesis, Site-Directed Phosphatidylglycerols - chemistry Phosphatidylglycerols - metabolism Protein Structure, Secondary SERINA SERINE Serine - genetics Serine - metabolism Spectrometry, Fluorescence Thermodynamics TRIACILGLICEROL LIPASA TRIACYLGLYCEROL LIPASE
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