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Literature summary for 1.14.14.18 extracted from

  • Ding, Y.; McCoubrey, W.K., Jr.; Maines, M.D.
    Interaction of heme oxygenase-2 with nitric oxide donors: is the oxygenase an intracellular sink for NO? (1999), Eur. J. Biochem., 264, 854-861.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type heme oxygenase-1 and 2 and heme oxygenase-2 C264A/C281A double mutant in Escherichia coli Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
3-morpholinosydnonimine NO-donor, 27% inhibition of recombinant heme oxygenase-2 Rattus norvegicus
S-nitroso-N-acetyl-pennicillamine NO-donor, 23% inhibition of recombinant heme oxygenase-2 Rattus norvegicus
sodium nitroprusside NO-donor, 58% inhibition of recombinant heme oxygenase-2 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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-
-

Cofactor

Cofactor Comment Organism Structure
heme hemoprotein, heme is both substrate and cofactor, heme oxygenase-2 binds heme at heme regulatory motifs with a conserved Cys-Pro pair Rattus norvegicus