rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    non sort: A
    title: structural and functional evaluation of the allosteric response of the Aspartate transcarbamoylase from Serratia marcescens
  name:
    name part: Beck, DeAndra.
    role:
      role term: creator
  name:
    name part: Ippen-Ihler, Karin
    role:
      role term: degree committee member.
  name:
    name part: Pace, Carlos N.
    role:
      role term: degree committee member.
  name:
    name part: Raushel, Frank M.
    role:
      role term: degree committee member.
  name:
    name part: Wild, James R.
    role:
      role term: degree supervisor.
  name:
    name part: Texas A & M University
    role:
      role term: degree granting institution.
  type of resource: text
  genre: bibliography
  genre: Academic theses
  origin info:
    place:
      place term: xx
    date issued: 1990
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: print
    extent: xii, 146 leaves : illustrations ; 29 cm
  abstract: The aspartate transcarbamoylases (E.C.2.1.3.2, ATCase) from enteric bacteria possess structural and functional similarities, although unique differences in homotropic and heterotropic regulation of enzymatic activity exist among divergent species. The ATCase holoenzyme from Escherichia coli is activated by ATP, inhibited by CTP, and synergistically inhibited by CTP in the presence of UTP. The ATCase holoenzyme from Serratia marcescens is activated by ATP and by CTP, while a combination of CTP and UTP counteracts the activation of CTP alone. The genes encoding the catalytic and regulatory polypeptides of the ATCase from S. marcescens, pyrB and pyrI, are arranged as a bicistronic operon with pyrI promoter distal. A comparison of the DNA sequences of pyrI from E. coli and S. marcescens reveals a 75% identity, and the deduced amino acid homology is 77%. The regulatory polypeptide from S. marcescens contains 154 amino acids with a molecular mass of 17,308 Da. In vivo hybrid enzymes have been assembled with catalytic subunits from divergent enteric species and regulatory subunits from S. marcescens. The regulatory dimers of S. marcescens dictate the nature of the allosteric response to the catalytic trimers. In each of the enzymes, the UTP response is either negligible or significantly less than the activation by both ATP and CTP; moreover, a combination of CTP and UTP counteracts the activation of CTP. These observations are consistent with the allosteric response of the native S. marcescens holoenzyme. Chimeric regulatory polypeptides can be made by genetically exchanging the allosteric domain and the zinc domain from E. coli and S. marcescens in both combinations. Using catalytic polypeptides from both species and both chimeric regulatory polypeptides, a series of active chimeric holoenzymes have been assembled in vivo. ATP uniformly activates the chimeric enzymes, but the CTP response is variable, indicating that ATP and CTP exert heterotropic effects through a differ…
  note: by DeAndra Beck.
  note: "Major subject: Biochemistry."
  note: Typescript (photocopy).
  note: Vita.
  note: Ph. D. Texas A & M University 1990
  note: Includes bibliographical references.
  subject:
    topic: Allosteric proteins
  subject:
    topic: Enzymes
    topic: Analysis
  subject:
    topic: Serratia marcescens
  subject:
    topic: Biochemistry
  subject:
    topic: Allosteric proteins
  subject:
    topic: Enzymes
    topic: Analysis
  subject:
    topic: Serratia marcescens
  identifier: http://proxy.library.tamu.edu/login
  identifier: https://hdl.handle.net/1969.1/DISSERTATIONS-1190580
  related item:
    location:
      url: http://proxy.library.tamu.edu/login
  related item:
    location:
      url: https://hdl.handle.net/1969.1/DISSERTATIONS-1190580
  record info:
    record content source: TXA
    record creation date: 910905
    record change date: 20220103134950.0
    record identifier: in00001043020
    language of cataloging:
      language term: eng