Substrate Effect on LTA4H Aminopeptidase Activity in The Presence of 4MDM

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dc.contributor.advisorPaige, Mikell
dc.contributor.authorYassa, Jacklin
dc.creatorYassa, Jacklin
dc.date2019-05-01
dc.date.accessioned2019-08-28T01:34:48Z
dc.descriptionThis thesis has been embargoed for 10 years and will not be available until May 2029 at the earliest.
dc.description.abstractThe leukotriene A4 hydrolase (LTA4H) protein is a zinc-containing bifunctional enzyme with epoxide hydrolase (EH) activity and aminopeptidase (AP) activity. LTA4H has long been regarded as an anti-inflammatory target since it controls the rate-limiting step in the biosynthesis of the inflammatory mediator leukotriene B4 (LTB4). In addition to the EH activity, LTA4H is an aminopeptidase which has a broad substrates specificity. It is proposed that the LTA4H aminopeptidase activity may have an important role in the processing of peptides related to inflammation. The small molecule 4- methoxydiphenylmethane (4MDM) was reported previously to selectively augment the LTA4H aminopeptidase activity without affecting the bioproduction of LTB4 in vivo. Thus, this thesis aims to determine the mechanism of LTA4H-mediated hydrolysis of peptidyl substrates in the presence of 4MDM.
dc.description.embargo2029-05-01
dc.identifier.urihttps://hdl.handle.net/1920/11583
dc.language.isoen
dc.subjectLys-pNA hydrolysis
dc.subjectLTA4H
dc.subjectAminopeptidase activity
dc.subject4MDM
dc.subjectKinetic assay
dc.titleSubstrate Effect on LTA4H Aminopeptidase Activity in The Presence of 4MDM
dc.typeThesis
thesis.degree.disciplineBiochemistry
thesis.degree.grantorGeorge Mason University
thesis.degree.levelMaster's
thesis.degree.nameMaster of Science in Biochemistry

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