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

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dc.contributor.advisor Paige, Mikell
dc.contributor.author Yassa, Jacklin
dc.creator Yassa, Jacklin
dc.date 2019-05-01
dc.date.accessioned 2019-08-28T01:34:48Z
dc.identifier.uri http://hdl.handle.net/1920/11583
dc.description This thesis has been embargoed for 10 years and will not be available until May 2029 at the earliest. en_US
dc.description.abstract The 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. en_US
dc.language.iso en en_US
dc.subject Lys-pNA hydrolysis en_US
dc.subject LTA4H en_US
dc.subject Aminopeptidase activity en_US
dc.subject 4MDM en_US
dc.subject kinetic assay en_US
dc.title Substrate Effect on LTA4H Aminopeptidase Activity in The Presence of 4MDM en_US
dc.type Thesis en_US
thesis.degree.name Master of Science in Biochemistry en_US
thesis.degree.level Master's en_US
thesis.degree.discipline Biochemistry en_US
thesis.degree.grantor George Mason University en_US
dc.description.embargo 2029-05-01


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