{"id":{"repo_id":"unt","oai_identifier":"info:ark/67531/metadc3012"},"canonical_url":"https://search.dev.ndltd.org/etd/unt/info:ark/67531/metadc3012","repository":{"repo_id":"unt","name":"University of North Texas","base_url":"https://digital.library.unt.edu/oai/"},"display":{"title":"Characterization of Moraxella bovis Aspartate Transcarbamoylase","abstract":"Aspartate transcarbamoylase (ATCase) catalyzes the first committed step in the pyrimidine biosynthetic pathway. Bacterial ATCases have been divided into three classes, class A, B, and C, based on their molecular weight, holoenzyme architecture, and enzyme kinetics. Moraxella bovis is a fastidious organism, the etiologic agent of infectious bovine keratoconjunctivitis (IBK). The M. bovis ATCase was purified and characterized for the first time. It is a class A enzyme with a molecular mass of 480 to 520 kDa. It has a pH optimum of 9.5 and is stable at high temperatures. The ATCase holoenzyme is inhibited by CTP > ATP > UTP. The Km for aspartate is 1.8 mM and the Vmax 1.04 µmol per min, where the Km for carbamoylphosphate is 1.05 mM and the Vmax 1.74 µmol per min.","abstract_html":"Aspartate transcarbamoylase (ATCase) catalyzes the first committed step in the pyrimidine biosynthetic pathway. Bacterial ATCases have been divided into three classes, class A, B, and C, based on their molecular weight, holoenzyme architecture, and enzyme kinetics. Moraxella bovis is a fastidious organism, the etiologic agent of infectious bovine keratoconjunctivitis (IBK). The M. bovis ATCase was purified and characterized for the first time. It is a class A enzyme with a molecular mass of 480 to 520 kDa. It has a pH optimum of 9.5 and is stable at high temperatures. The ATCase holoenzyme is inhibited by CTP > ATP > UTP. The Km for aspartate is 1.8 mM and the Vmax 1.04 µmol per min, where the Km for carbamoylphosphate is 1.05 mM and the Vmax 1.74 µmol per min.","abstract_has_math":false,"creators":["Hooshdaran, Sahar"],"institution":"University of North Texas","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Farinha, Mark A.","O'Donovan, Gerard A.","Benjamin, Robert C."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2001,"date_issued":"2001-12","date_published":"2001-12","updated_at":"2026-07-24T05:34:52Z","subjects":["Pyrimidine nucleotides -- Metabolism.","Moraxella.","Moraxella bovis","ATCase","nucleotide effectors","growth curve","growth conditions"],"languages":["English"],"rights":["Use restricted to UNT Community","Copyright","Hooshdaran, Sahar","Copyright is held by the author, unless otherwise noted. All rights reserved."],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["oclc: 51986132","https://digital.library.unt.edu/ark:/67531/metadc3012/","ark: ark:/67531/metadc3012"],"render_values":[{"text":"oclc: 51986132","href":null,"code":true},{"text":"https://digital.library.unt.edu/ark:/67531/metadc3012/","href":"https://digital.library.unt.edu/ark:/67531/metadc3012/","code":true},{"text":"ark: ark:/67531/metadc3012","href":null,"code":true}]}]},"links":{"outbound_url":"https://doi.org/10.12794/metadc3012","outbound_label":"DOI","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Farinha, Mark A.","O'Donovan, Gerard A.","Benjamin, Robert C."]},{"key":"dc:creator","label":"Author","values":["Hooshdaran, Sahar"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2001-12"]},{"key":"dc:publisher","label":"Institution","values":["University of North Texas"]},{"key":"dc:type","label":"Dc Type","values":["Thesis or Dissertation"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Pyrimidine nucleotides -- Metabolism.","Moraxella.","Moraxella bovis","ATCase","nucleotide effectors","growth curve","growth conditions"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]},{"key":"dc:rights","label":"Dc Rights","values":["Use restricted to UNT Community","Copyright","Hooshdaran, Sahar","Copyright is held by the author, unless otherwise noted. All rights reserved."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["oclc: 51986132","doi: 10.12794/metadc3012","https://digital.library.unt.edu/ark:/67531/metadc3012/","ark: ark:/67531/metadc3012"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Aspartate transcarbamoylase (ATCase) catalyzes the first committed step in the pyrimidine biosynthetic pathway. Bacterial ATCases have been divided into three classes, class A, B, and C, based on their molecular weight, holoenzyme architecture, and enzyme kinetics. Moraxella bovis is a fastidious organism, the etiologic agent of infectious bovine keratoconjunctivitis (IBK). The M. bovis ATCase was purified and characterized for the first time. It is a class A enzyme with a molecular mass of 480 to 520 kDa. It has a pH optimum of 9.5 and is stable at high temperatures. The ATCase holoenzyme is inhibited by CTP > ATP > UTP. The Km for aspartate is 1.8 mM and the Vmax 1.04 µmol per min, where the Km for carbamoylphosphate is 1.05 mM and the Vmax 1.74 µmol per min."]},{"key":"dc:format","label":"Dc Format","values":["Text"]},{"key":"dc:title","label":"Title","values":["Characterization of Moraxella bovis Aspartate Transcarbamoylase"]}]}],"canonical_facts":{"dc:contributor":["Farinha, Mark A.","O'Donovan, Gerard A.","Benjamin, Robert C."],"dc:creator":["Hooshdaran, Sahar"],"dc:date":["2001-12"],"dc:description":["Aspartate transcarbamoylase (ATCase) catalyzes the first committed step in the pyrimidine biosynthetic pathway. Bacterial ATCases have been divided into three classes, class A, B, and C, based on their molecular weight, holoenzyme architecture, and enzyme kinetics. Moraxella bovis is a fastidious organism, the etiologic agent of infectious bovine keratoconjunctivitis (IBK). The M. bovis ATCase was purified and characterized for the first time. It is a class A enzyme with a molecular mass of 480 to 520 kDa. It has a pH optimum of 9.5 and is stable at high temperatures. The ATCase holoenzyme is inhibited by CTP > ATP > UTP. The Km for aspartate is 1.8 mM and the Vmax 1.04 µmol per min, where the Km for carbamoylphosphate is 1.05 mM and the Vmax 1.74 µmol per min."],"dc:format":["Text"],"dc:identifier":["oclc: 51986132","doi: 10.12794/metadc3012","https://digital.library.unt.edu/ark:/67531/metadc3012/","ark: ark:/67531/metadc3012"],"dc:language":["English"],"dc:publisher":["University of North Texas"],"dc:rights":["Use restricted to UNT Community","Copyright","Hooshdaran, Sahar","Copyright is held by the author, unless otherwise noted. All rights reserved."],"dc:subject":["Pyrimidine nucleotides -- Metabolism.","Moraxella.","Moraxella bovis","ATCase","nucleotide effectors","growth curve","growth conditions"],"dc:title":["Characterization of Moraxella bovis Aspartate Transcarbamoylase"],"dc:type":["Thesis or Dissertation"]},"updated_at":"2026-07-24T05:34:52Z"}