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Guo, S.* ; Popowicz, G.M. ; Li, D.* ; Yuan, D.* ; Wang, Y.*

Lid mobility in lipase SMG1 validated using a thiol/disulfide redox potential probe.

FEBS Open Bio 6, 477-483 (2016)
Verlagsversion DOI
Open Access Gold
Creative Commons Lizenzvertrag
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter 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
Zeitschrift FEBS Open Bio
Quellenangaben Band: 6, Heft: 5, Seiten: 477-483 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort Cambridge
Begutachtungsstatus Peer reviewed