<p>(A) This figure corresponds to the simulation of mutant Ala217Ser. The movement of the lids very similar to those in the wild-type lipase. Thus, despite the mutation, the lids are able to close in an aqueous environment.</p> <p>(B) Here, the simulated structure is a mutant in Phe214Ser.</p> <p>Red, lid1 RMSD; blue, lid2 RMSD; black, lid1-lid2 distance.</p
Thermostability remains one of the most desirable traits in many lipases. Numerous studies have reve...
Relationship between stability and activity of enzymes is maintained by underlying conformational fl...
Pancreatic lipase is a soluble globular protein that must undergo structural modifications be...
<p>Both the alanine at 217 and the phenylalanine at 214 were mutated to serines, and the simulation ...
<p>(A) This figure represents the simulation results. The structure on the left (i) is the open form...
Pseudomonas aeruginosa lipase is a 29-kDa protein that, following the determination of its crystal s...
Lipases naturally function at the interface formed between amphiphilic molecules and the aqueous env...
<div><p><i>Pseudomonas aeruginosa</i> lipase is a 29-kDa protein that, following the determination o...
International audienceThe interfacial activation of many lipases at water/lipid interface is mediate...
In nonaqueous organic solvents, lipases can catalyze esterification reactions, which increase their ...
Lid of lipases modulate the specificity of the substrate to the catalytic active site of lipase by ...
Interfacial activation of Rhizomucor miehei lipase is accompanied by a hinge-type motion of a single...
Lipases are enzymes that play fundamental roles in fat digestion and metabolism, and function at the...
<p>Wild-type (grey) and 6B (pink) crystal structures were overlapped. Side chain of active site resi...
Triacylglycerol hydrolases (EC 3.1.1.3) are thought to become activated when they encounter the wate...
Thermostability remains one of the most desirable traits in many lipases. Numerous studies have reve...
Relationship between stability and activity of enzymes is maintained by underlying conformational fl...
Pancreatic lipase is a soluble globular protein that must undergo structural modifications be...
<p>Both the alanine at 217 and the phenylalanine at 214 were mutated to serines, and the simulation ...
<p>(A) This figure represents the simulation results. The structure on the left (i) is the open form...
Pseudomonas aeruginosa lipase is a 29-kDa protein that, following the determination of its crystal s...
Lipases naturally function at the interface formed between amphiphilic molecules and the aqueous env...
<div><p><i>Pseudomonas aeruginosa</i> lipase is a 29-kDa protein that, following the determination o...
International audienceThe interfacial activation of many lipases at water/lipid interface is mediate...
In nonaqueous organic solvents, lipases can catalyze esterification reactions, which increase their ...
Lid of lipases modulate the specificity of the substrate to the catalytic active site of lipase by ...
Interfacial activation of Rhizomucor miehei lipase is accompanied by a hinge-type motion of a single...
Lipases are enzymes that play fundamental roles in fat digestion and metabolism, and function at the...
<p>Wild-type (grey) and 6B (pink) crystal structures were overlapped. Side chain of active site resi...
Triacylglycerol hydrolases (EC 3.1.1.3) are thought to become activated when they encounter the wate...
Thermostability remains one of the most desirable traits in many lipases. Numerous studies have reve...
Relationship between stability and activity of enzymes is maintained by underlying conformational fl...
Pancreatic lipase is a soluble globular protein that must undergo structural modifications be...