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:
    title: D-aminoacylases and dipeptidases within the amidohydrolase superfamily
    sub title: relationship between enzyme structure and substrate specificity
  name:
    name part: Cummings, Jennifer Ann.
    role:
      role term: creator
  name:
    name part: Raushel, Frank M.
    role:
      role term: thesis advisor.
  type of resource: text
  genre: bibliography
  origin info:
    place:
      place term: txu
    date issued: 2012
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: remote
    extent: 1 online resource.
  abstract: Approximately one third of the genes for the completely sequenced bacterial genomes have an unknown, uncertain, or incorrect functional annotation. Approximately 11,000 putative proteins identified from the fully-sequenced microbial genomes are members of the catalytically diverse Amidohydrolase Superfamily. Members of the Amidohydrolase Superfamily separate into 24 Clusters of Orthologous Groups (cogs). Cog3653 includes proteins annotated as N-acyl-D-amino acid deacetylases (DAAs), and proteins within cog2355 are homologues to the human renal dipeptidase. The substrate profiles of three DAAs (Bb3285, Gox1177 and Sco4986) and six microbial dipeptidase (Sco3058, Gox2272, Cc2746, LmoDP, Rsp0802 and Bh2271) were examined with N-acyl-L-, N-acyl-D-, L-Xaa-L-Xaa, L-Xaa-D-Xaa and D-Xaa-L-Xaa substrate libraries. The rates of hydrolysis of the library components were determined by separating the amino acids by HPLC and quantitating the products. Gox1177 and Sco4986 hydrolyzed several N-acyl-D-amino acids, especially those where the amino acid was a hydrophobic residue. Gox1177 hydrolyzed L-Xaa-D-Xaa and N-acetyl-D-amino acids with similar catalytic efficiencies (~10⁴ M⁻¹s⁻¹). The best substrates identified for Gox1177 and Sco4986 were N-acetyl-D-Trp and N-acetyl-D-Phe, respectively. Conversely, Bb3285 hydrolyzed N-acyl-D-Glu substrates (kcat/Km ⁹́⁸ 5 x 10⁶M⁻¹s⁻¹) and, to a lesser extent, L-Xaa-D-Glu dipeptides. The structure of a DAA from A. faecalis did not help explain the substrate specificity of Bb3285. N-methylphosphonate derivatives of D-amino acids were inhibitors of the DAAs examined. The structure of Bb3285 was solved in complex with the N-methylphosphonate derivative of D-Glu or acetate/formate. The specificity of Bb3285 was due to an arginine located on a loop which varied in conformation from the A. faecalis enzyme. In a similar manner, six microbial renal dipeptidase-like proteins were screened with 55 dipeptide libraries. These enzymes hydrolyzed many dipeptid…
  note: by Jennifer Ann Cummings.
  note: "Major Subject: Chemistry"
  note: Electronic resource.
  note: Doctor of Philosophy Texas A&M University 2010 http://hdl.handle.net/1969.1/ETD-TAMU-2010-12-9021
  note: Includes bibliographical references.
  note: Text (Dissertation)
  subject:
    topic: Major chemistry
  subject:
    topic: Clusters of Orthologous Groups
  subject:
    topic: Enzymology
  subject:
    topic: Bh2271
  subject:
    topic: TIM-barrel
  subject:
    topic: Amidohydrolase Superfamily
  subject:
    topic: Sco4986
  subject:
    topic: Jennifer Cummings
  subject:
    topic: Lmo2462
  subject:
    topic: Gox2272
  subject:
    topic: Dipeptides
  subject:
    topic: Alpha-beta barrel
  subject:
    topic: Phosphonate
  subject:
    topic: Cc2746
  subject:
    topic: Bb3285
  subject:
    topic: Rsp_0802
  subject:
    topic: Phosphinate
  subject:
    topic: D-aminoacylase
  subject:
    topic: D-amino acid
  subject:
    topic: Dipeptidase
  identifier: http://hdl.handle.net/1969.1/ETD-TAMU-2010-12-9021
  record info:
    record content source: TXA
    record creation date: 120312
    record change date: 20151202151730.0
    record identifier: in00002742440