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Literature summary extracted from

  • van der Kamp, M.W.; Sirirak, J.; ?urek, J.; Allemann, R.K.; Mulholland, A.J.
    Conformational change and ligand binding in the aristolochene synthase catalytic cycle (2013), Biochemistry, 52, 8094-8105.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.3.9 molecular dynamics simulations based on structure PDB entry 2OA6. The substrate farnesyl diphosphate binds first, followed by three magnesium ions in sequence, and, after reaction, the release of aristolochene and two magnesium ions followed by the final magnesium ion and diphosphate. Binding of farnesyl diphosphate leads to an increased level of sampling of open conformations, allowing the first two magnesium ions to bind. The closed enzyme conformation is maintained with a diphosphate moiety and two magnesium ions bound. The open-to-closed transition reduces flexibility around the active site entrance, partly through a lid closing over it Aspergillus terreus

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.9 Aspergillus terreus Q9UR08
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