{"id":{"repo_id":"gmu","oai_identifier":"oai:MARS:1920/11583"},"canonical_url":"https://search.dev.ndltd.org/etd/gmu/oai:MARS:1920/11583","repository":{"repo_id":"gmu","name":"George Mason University","base_url":"https://mars.gmu.edu/server/oai/request"},"display":{"title":"Substrate Effect on LTA4H Aminopeptidase Activity in The Presence of 4MDM","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.","abstract_html":"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.","abstract_has_math":false,"creators":["Yassa, Jacklin"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":null,"date_issued":"","date_published":null,"updated_at":"2026-07-27T19:51:48Z","subjects":["Lys-pNA hydrolysis","LTA4H","Aminopeptidase activity","4MDM","Kinetic assay"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["hdl:1920/11583"],"render_values":[{"text":"hdl:1920/11583","href":null,"code":true}]}]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:type","label":"Dc Type","values":["Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Lys-pNA hydrolysis","LTA4H","Aminopeptidase activity","4MDM","Kinetic assay"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["hdl:1920/11583"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.other","label":"Dc Description Other","values":["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."]},{"key":"dc:title","label":"Title","values":["Substrate Effect on LTA4H Aminopeptidase Activity in The Presence of 4MDM"]}]}],"canonical_facts":{"dc:description.other":["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."],"dc:identifier":["hdl:1920/11583"],"dc:subject":["Lys-pNA hydrolysis","LTA4H","Aminopeptidase activity","4MDM","Kinetic assay"],"dc:title":["Substrate Effect on LTA4H Aminopeptidase Activity in The Presence of 4MDM"],"dc:type":["Thesis"]},"updated_at":"2026-07-27T19:51:48Z"}