Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Frydman, R.B.; Tomaro, M.L.; Buldain, G.; Awruch, J.; Diaz, L.; Frydman, B.
    Specificity of heme oxygenase: a study with synthetic hemins (1981), Biochemistry, 20, 5177-5182.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.18 Porphyrins protoporphyrin IX, Zn-protoporphyrin IX, 2,4-diacetyldeuteroporphyrin IX, deuteroporphyrin IX, coproporphyrin II, III and IV Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.14.18 microsome
-
 Rattus norvegicus
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.18 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.14.18 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.18 heme + electron donor + O2 overview, substrate specificity Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
 ?
1.14.14.18 heme + electron donor + O2 synthetic hemins XIII and III and iron porphyrin are better substrates than the natural substrate hemin IX, 83 and 86% of hemin IX activity with mesohemin IX and hematohemin IX respectively Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
 ?