2018
DOI: 10.1016/j.ijbiomac.2018.07.158
|View full text |Cite
|
Sign up to set email alerts
|

Elucidation of lid open and orientation of lipase activated in interfacial activation by amphiphilic environment

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
4
1

Citation Types

0
30
0
4

Year Published

2019
2019
2024
2024

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 47 publications
(34 citation statements)
references
References 41 publications
0
30
0
4
Order By: Relevance
“…107 This mechanism is based on the existence of a large hydrophobic pocket surrounding the active center. [108][109][110][111][112][113][114][115] An enzyme molecule with this large hydrophobic pocket will be very unstable and will have low solubility in aqueous media. However, this problem is avoided because this hydrophobic pocket it is covered by a polypeptide chain called lid, which generally isolates the active center from the reaction medium (in this "closed" form, the lipase is inactive).…”
Section: Lipases In Biocatalysismentioning
confidence: 99%
See 1 more Smart Citation
“…107 This mechanism is based on the existence of a large hydrophobic pocket surrounding the active center. [108][109][110][111][112][113][114][115] An enzyme molecule with this large hydrophobic pocket will be very unstable and will have low solubility in aqueous media. However, this problem is avoided because this hydrophobic pocket it is covered by a polypeptide chain called lid, which generally isolates the active center from the reaction medium (in this "closed" form, the lipase is inactive).…”
Section: Lipases In Biocatalysismentioning
confidence: 99%
“…The lid also has an internal hydrophobic face that interacts with the hydrophobic areas of the active center and a hydrophilic external face, which interacts with the reaction medium. [108][109][110][111][112][113][114][115] This lid can move, and when it is shifted, it forms a huge hydrophobic pocket exposing the active center to the medium, resulting in the "open" and active form of the lipase, with the hydrophilic phase of the lid interacting with the protein surface. Both conformational lipase forms are in equilibrium, but in the presence of oil drops, the open form becomes adsorbed on the hydrophobic surface of the drops, shifting the conformational equilibrium towards the open form of the lipase and permitting the attack of the glycerides by the enzyme [108][109][110][111][112][113][114][115] (Fig.…”
Section: Lipases In Biocatalysismentioning
confidence: 99%
“…Most lipases present their active center isolated from the medium by a polypeptide chain called lid. The internal face of the lid is hydrophobic and interacts with the hydrophobic surroundings of the active center [77][78][79][80][81][82][83][84]. This "closed" form is in equilibrium with an "open" form of the lipase that is the active one, where the lid is shifted and exposes the active center.…”
Section: Lipases In Biocatalysismentioning
confidence: 99%
“…This "closed" form is in equilibrium with an "open" form of the lipase that is the active one, where the lid is shifted and exposes the active center. However, the large hydrophobic pocket is unstable under these conditions and the enzyme is mainly in the closed form in saline aqueous homogenous media [77][78][79][80][81][82][83][84]. In the presence of a hydrophobic surface, like drops of oil, this lipase form may be adsorbed and stabilized, and for this reason they can operate at the interface of the oil drops [77][78][79][80][81][82][83][84].…”
Section: Lipases In Biocatalysismentioning
confidence: 99%
“…lipid activated lids to the active site of lipases, also help dene substrate type. 34 These structures endow enzymes with exquisite chemo-, regio-and most importantly stereo-selectivity. 35 Engineering of these channels is a developing area of research.…”
Section: Enzyme Structure Functions Mechanisms and Scope In Organicmentioning
confidence: 99%