Home
Deutsch
Advanced Search
Browse by ...
Publication overview
Contact persons
Help
Publ. Version/Full Text
DOI
PMC
 |
Open Access Gold |
|
as soon as is submitted to ZB.
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.
Altmetric
Additional Metrics?
Edit extra informations
Login
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
ISSN (print) / ISBN
2211-5463
Journal
FEBS Open Bio
Quellenangaben
Volume: 6,
Issue: 5,
Pages: 477-483
Publisher
Elsevier
Publishing Place
Cambridge
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)