<p>Both the alanine at 217 and the phenylalanine at 214 were mutated to serines, and the simulation was carried out in an aqueous medium. The lids do not close in an aqueous environment. Thus, by mutating the key contact residues to serines, the hydrophobicity of lid2 is lost, and it is unable to function as a trigger for the lids to converge and close.</p> <p>Red, lid1 RMSD; blue, lid2 RMSD; black, lid1-lid2 distance.</p
Lip 42 lipase, isolated from Bacillus sp. strain 42 was previously shown to be stable in polar organ...
AbstractThe effect of solvent hydrophobicity on activation of Candida rugosa lipase (CRL) was invest...
Pseudomonas fluorescens AMS8 lipase lid 1 structure is rigid and holds unclear roles due to the abse...
<p>(A) This figure corresponds to the simulation of mutant Ala217Ser. The movement of the lids very ...
Lipases naturally function at the interface formed between amphiphilic molecules and the aqueous env...
Pseudomonas aeruginosa lipase is a 29-kDa protein that, following the determination of its crystal s...
<p>(A) This figure represents the simulation results. The structure on the left (i) is the open form...
<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...
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...
In nonaqueous organic solvents, lipases can catalyze esterification reactions, which increase their ...
Lipases are enzymes that play fundamental roles in fat digestion and metabolism, and function at the...
Pancreatic lipase is a soluble globular protein that must undergo structural modifications be...
AbstractRhizomuor miehei Lipase (RmL) is a type of lipase that has a single lid segment playing impo...
Lip 42 lipase, isolated from Bacillus sp. strain 42 was previously shown to be stable in polar organ...
AbstractThe effect of solvent hydrophobicity on activation of Candida rugosa lipase (CRL) was invest...
Pseudomonas fluorescens AMS8 lipase lid 1 structure is rigid and holds unclear roles due to the abse...
<p>(A) This figure corresponds to the simulation of mutant Ala217Ser. The movement of the lids very ...
Lipases naturally function at the interface formed between amphiphilic molecules and the aqueous env...
Pseudomonas aeruginosa lipase is a 29-kDa protein that, following the determination of its crystal s...
<p>(A) This figure represents the simulation results. The structure on the left (i) is the open form...
<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...
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...
In nonaqueous organic solvents, lipases can catalyze esterification reactions, which increase their ...
Lipases are enzymes that play fundamental roles in fat digestion and metabolism, and function at the...
Pancreatic lipase is a soluble globular protein that must undergo structural modifications be...
AbstractRhizomuor miehei Lipase (RmL) is a type of lipase that has a single lid segment playing impo...
Lip 42 lipase, isolated from Bacillus sp. strain 42 was previously shown to be stable in polar organ...
AbstractThe effect of solvent hydrophobicity on activation of Candida rugosa lipase (CRL) was invest...
Pseudomonas fluorescens AMS8 lipase lid 1 structure is rigid and holds unclear roles due to the abse...