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Literature summary for extracted from

  • Glynn, S.E.; Baker, P.J.; Sedelnikova, S.E.; Davies, C.L.; Eadsforth, T.C.; Levy, C.W.; Rodgers, H.F.; Blackburn, G.M.; Hawkes, T.R.; Viner, R.; Rice, D.W.
    Structure and mechanism of imidazoleglycerol-phosphate dehydratase (2005), Structure, 13, 1809-1817.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals belong to space group R3 with cell parameters a = 157.9 A, b = 157.9 A, c = 480 A, alpha = beta = 90°, gamma = 120°. Structure of manganese assembled, active form of the enzyme at 3.0 A resolution Arabidopsis thaliana


Metals/Ions Comment Organism Structure
Mn the manganese cluster is critical in converting the inactive trimeric state of the enzyme into its biologically active 24-mer and also forms the active site. The substrate is bound to the manganese cluster as an imidazole moiety that subsequently collapse to yield a diazafulvene intermediate Arabidopsis thaliana


Organism UniProt Comment Textmining
Arabidopsis thaliana


Synonyms Comment Organism
Arabidopsis thaliana