2012
DOI: 10.1016/j.molcatb.2012.05.012
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Lipase B from Candida antarctica binds to hydrophobic substrate–water interfaces via hydrophobic anchors surrounding the active site entrance

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Cited by 42 publications
(35 citation statements)
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“…7,27,29-31 In this paper we show that CalB is an interfacially activated enzyme and that activation depends both on the hydrophobicity of the interface as well as the overall size of the substrate. In a series of systematic experiments, we have immobilized CalB on a number of supports with varying degrees of hydrophobicity via physical adsorption.…”
Section: Introductionmentioning
confidence: 79%
See 1 more Smart Citation
“…7,27,29-31 In this paper we show that CalB is an interfacially activated enzyme and that activation depends both on the hydrophobicity of the interface as well as the overall size of the substrate. In a series of systematic experiments, we have immobilized CalB on a number of supports with varying degrees of hydrophobicity via physical adsorption.…”
Section: Introductionmentioning
confidence: 79%
“…25 In agreement with these experimental observations, several molecular dynamics studies have shown the important role of the α5 and α10 helices for CalB activity, highlighting that these helices are the most mobile parts of the structure. 13,26-28 In a particularly elegant series of simulations, Pleiss and coworkers 27 have shown that, upon coming into close proximity with a hydrophobic interface, CalB is initially anchored in the bilayer by burial of the α5 helix into the hydrophobic layer. Subsequently, the enzyme reorients and binds to the interface, appropriately positioning its active site.…”
Section: Introductionmentioning
confidence: 99%
“…CalB does not display the common interfacial activation characteristics of lipases . However, the enzyme has a very flexible small loop close to the active site and three hydrophobic anchor residues that bind to oil–water interfaces …”
Section: Resultsmentioning
confidence: 99%
“…This observation is in good agreement with previous studies by Pleiss and co-workers. The authors identified six regions (α-helices α2, α5, α8, α10 and β-strands β1 and β4) of high hydrophobicity that can function as putative membrane interaction sites (studies based on a water-substrate interface system [21]) and three water binding sites at CALB surface (studies based on water-organic solvent binary mixtures [22]). Our study shows that even at high water activity, these six hydrophobic regions are not covered by water molecules and that the hot spot regions on CALB surface identified here are comparable with the water binding sites suggested by Kulschewski and Pleiss [22].…”
Section: Hydration Levelmentioning
confidence: 99%