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Literature summary for extracted from

  • Zhu, G.; Koszelak-Rosenblum, M.; Malkowski, M.G.
    Crystal structures of alpha-dioxygenase from Oryza sativa insights into substrate binding and activation by hydrogen peroxide (2013), Protein Sci., 22, 1432-1438 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of wild-type in complex with H2O2, and the catalytically inactive Y379F mutant in complex with palmitic acid. PA binds within the active site cleft of alpha-DOX such that the carboxylate forms ionic interactions with residues His311 and Arg559. Thr316 aids in the positioning of carbon-2 for hydrogen abstraction. The binding of H2O2 at the distal face of the heme displaces residues His157, Asp158, and Trp159 about 2.5 A from their positions in the wild type structure Oryza sativa


Organism UniProt Comment Textmining
Oryza sativa Q9M5J1