Ontology highlight
ABSTRACT:
SUBMITTER: Booth RE
PROVIDER: S-EPMC368447 | biostudies-literature | 2004
REPOSITORIES: biostudies-literature
Booth Rachell E RE Lovell Simon C SC Misquitta Stephanie A SA Bateman Robert C RC
BMC biology 20040210
<h4>Background</h4>Glutaminyl cyclase (QC) forms the pyroglutamyl residue at the amino terminus of numerous secretory peptides and proteins. We previously proposed the mammalian QC has some features in common with zinc aminopeptidases. We now have generated a structural model for human QC based on the aminopeptidase fold (pdb code 1AMP) and mutated the apparent active site residues to assess their role in QC catalysis.<h4>Results</h4>The structural model proposed here for human QC, deposited in ...[more]