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Literature summary for 1.13.99.1 extracted from

  • Thorsell, A.G.; Persson, C.; Voevodskaya, N.; Busam, R.D.; Hammarstroem, M.; Graeslund, S.; Graeslund, A.; Hallberg, B.M.
    Structural and biophysical characterization of human myo-inositol oxygenase (2008), J. Biol. Chem., 283, 15209-15216.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with myo-inosose-1 bound in a terminal mode to the enzyme's diiron cluster site. The N-terminus is important, through coordination of a set of loops covering the active site, in shielding the active site during catalysis. Role of residue K127 in governing the access o the diiron cluster Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Iron diiron cluster Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
myo-Inositol + O2 = D-glucuronate + H2O the N-terminus is important, through coordination of a set of loops covering the active site, in shielding the active site during catalysis. Role of residue K127 in governing the access o the diiron cluster Homo sapiens