1993
DOI: 10.1016/s0021-9258(18)31464-9
|View full text |Cite
|
Sign up to set email alerts
|

Insights into interfacial activation from an open structure of Candida rugosa lipase

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

2
155
0
8

Year Published

1996
1996
2021
2021

Publication Types

Select...
7
1
1

Relationship

0
9

Authors

Journals

citations
Cited by 539 publications
(165 citation statements)
references
References 0 publications
2
155
0
8
Order By: Relevance
“…Lipase hyperactivation exhibited after immobilization on hydrophobic supports is caused by lid movements, exposing the active center of the lipase to the medium, which changes the conformational balance between the open and closed form of the lipase [25][26][27][28][29], and fully displaces the equilibrium towards the open active form of the lipase, which is fixed by adsorption on the hydrophobic support through its hydrophobic pocket [17] (Figure 1). This mechanism facilitates the entry of the substrate, resulting in easier enzymatic hydrolysis [16,17,34,73].…”
Section: Immobilization Of Usba-gbx-513 Lipase On Different Supportsmentioning
confidence: 99%
See 1 more Smart Citation
“…Lipase hyperactivation exhibited after immobilization on hydrophobic supports is caused by lid movements, exposing the active center of the lipase to the medium, which changes the conformational balance between the open and closed form of the lipase [25][26][27][28][29], and fully displaces the equilibrium towards the open active form of the lipase, which is fixed by adsorption on the hydrophobic support through its hydrophobic pocket [17] (Figure 1). This mechanism facilitates the entry of the substrate, resulting in easier enzymatic hydrolysis [16,17,34,73].…”
Section: Immobilization Of Usba-gbx-513 Lipase On Different Supportsmentioning
confidence: 99%
“…Lipases are the most used enzymes in biocatalysis due to their high activity, specificity, selectivity, and robustness in a variety of reaction media [14][15][16][17][18][19][20][21][22][23][24]. Lipases have a peculiar catalytic mechanism, called interfacial activation, which is based on the interaction of the lipase with hydrophobic structures, which causes deep conformational changes on the structure of the active site of the lipase and its consequent enzyme activation [25][26][27][28][29], permitting the enzyme to act in the hydrolysis of insoluble drops of oils and be adsorbed on any hydrophobic surface [30][31][32][33][34].…”
Section: Introductionmentioning
confidence: 99%
“…For molecular modeling we used three-dimensional structures of CRL, isoform 1 (LIP1), solved by X-ray diffraction in 'open' and in 'closed' form, PDB entries 1CRL and 1TRH, respectively. 28,29 Structures were checked for missing residues, close contacts and similar in VegaZZ 3.0.5 and water molecules removed. 30 Molecular interaction elds (MIFs) was calculated in GRID 22b, using Ca 2+ probe.…”
Section: Molecular Modelingmentioning
confidence: 99%
“…In particular, interaction of Gly 261 in mAChE subunit A with Trp 286 at the gorge entry of mAChE subunit C mimics the key interaction of Met 33 in mAChE establishes the same van der Waals contacts with Tyr 72 as does Fas2 Leu 35 . Several residues in helix ␣ 1 6,7 of mAChE subunit A also adopt positions similar to residues in bound Fas2: the side chain of Arg 253 in mAChE mimics, in both position and orientation, the side chain of Arg 27 in Fas2, and mAChE Gly 256 forms the same van der Waals contacts with His 287 as Fas2 Leu 48 . Hence, in the tetramer, the loops that arise from two of the subunits appear to occlude substrate access to the catalytic sites of the two other subunits, similar to steric occlusion observed in the Fas2⅐mAChE complex.…”
Section: Comparison Of the Mache And Fas2⅐mache Structuresmentioning
confidence: 99%