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Literature summary for 2.5.1.10 extracted from

  • Huang, C.H.; Gabelli, S.B.; Oldfield, E.; Amzel, L.M.
    Binding of nitrogen-containing bisphosphonates (N-BPs) to the Trypanosoma cruzi farnesyl diphosphate synthase homodimer (2010), Proteins, 78, 888-899.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with substrate isopentenyl diphosphate and five nitrogen-containing bisphosphonate inhibitors. The C1-hydroxyl and the nitrogen-containing groups of the inhibitors alter the binding of isopentenyl diphosphate and the conformation of residues Y94 and Q167. binding of the inhibitors changes the binding properties of the second site of the dimer Trypanosoma cruzi

Organism

Organism UniProt Comment Textmining
Trypanosoma cruzi Q8WS25
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Subunits

Subunits Comment Organism
dimer crystallization data Trypanosoma cruzi