title: Lid mobility in lipase SMG1 validated using a thiol/disulfide redox potential probe.
abstract: 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.
authors.affiliation: School of Light Industry and Engineering South China University of Technology Guangzhou China.
authors.forename: Shaohua
authors.initials: S
authors.lastname: Guo
authors.affiliation: Institute of Structural Biology Helmholtz Zentrum München Deutsches Forschungszentrum für Gesundheit und Umwelt (GmbH) Neuherberg Germany.
authors.forename: Grzegorz Maria
authors.initials: GM
authors.lastname: Popowicz
authors.affiliation: School of Light Industry and Engineering South China University of Technology Guangzhou China.
authors.forename: Daoming
authors.initials: D
authors.lastname: Li
authors.affiliation: School of Light Industry and Engineering South China University of Technology Guangzhou China.
authors.forename: Dongjuan
authors.initials: D
authors.lastname: Yuan
authors.affiliation: School of Light Industry and Engineering South China University of Technology Guangzhou China.
authors.forename: Yonghua
authors.initials: Y
authors.lastname: Wang
keywords: SMG1; activation mechanism; disulfide bond; lid; redox potential; redox‐switch