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Lid mobility in lipase SMG1 validated using a thiol/disulfide redox potential probe.
FEBS Open Bio 6, 477-483 (2016)
Most lipases possess a lid domain above the catalytic site that is responsible for their activation. Lipase SMG1 from Malassezia globose CBS 7966 (Malassezia globosa LIP1), is a mono- and diacylglycerol lipase with an atypical loop-like lid domain. Activation of SMG1 was proposed to be solely through a gating mechanism involving two residues (F278 and N102). However, through disulfide bond cross-linking of the lid, this study shows that full activation also requires mobility of the lid domain, contrary to a previous proposal. The newly introduced disulfide bond makes lipase SMG1 eligible as a ratiometric thiol/disulfide redox potential probe, when it is coupled with chromogenic substrates. This redox-switch lipase could also be of potential use in cascade biocatalysis.
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2.101
0.612
5
7
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Activation Mechanism ; Disulfide Bond ; Lid ; Redox Potential ; Redox-switch ; Smg1; Green Fluorescent Protein; Molecular-dynamics Simulations; Site-directed Mutagenesis; Malassezia-globosa; Diacylglycerol Lipase; Active-site; Mono; Indicators; Activation; Residues
Language
english
Publication Year
2016
HGF-reported in Year
2016
ISSN (print) / ISBN
2211-5463
Journal
FEBS Open Bio
Quellenangaben
Volume: 6,
Issue: 5,
Pages: 477-483
Publisher
Elsevier
Publishing Place
Cambridge
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Enabling and Novel Technologies
PSP Element(s)
G-503000-003
PubMed ID
27419053
WOS ID
WOS:000375915100011
Scopus ID
84963839225
Erfassungsdatum
2016-05-10