<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Vasella A</dc:creator>
  <dc:creator>Davies GJ</dc:creator>
  <dc:creator>Böhm M</dc:creator>
  <dc:date>2002</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">The three-dimensional structure of glycosidases and of their complexes and the study of transition-state mimics reveal structural details that correlate with mechanism. Of particular interest are the transition-state conformations harnessed by individual enzymes and the substrate distortion observed in enzyme-ligand complexes. 3D-structure in synergy with transition-state mimicry opens the way for mechanistic interpretation of enzyme inhibition and for the development of therapeutic agents.</dc:description>
  <dc:identifier>https://sonar.ch/global/documents/123440</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/s1367-5931(02)00380-0</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/12413546</dc:relation>
  <dc:source>Current opinion in chemical biology. - 2002</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Catalysis</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Enzyme Inhibitors</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Glycoside Hydrolases</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Hydrolysis</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Ligands</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Molecular Structure</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Mutagenesis</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Protein Conformation</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Stereoisomerism</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Substrate Specificity</dc:subject>
  <dc:title xmlns:ns11="xml" ns11:lang="en">Glycosidase mechanisms.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
