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Literature summary for 1.14.14.18 extracted from

  • Matasek, P.; Solangi, K.; Goodman, A.I.; Levere, R.D.; Chernick, R.J.; Abraham, N.G.
    Properties of human kidney heme oxygenase: inhibition by synthetic heme analogues and metalloporphyrins (1988), Biochem. Biophys. Res. Commun., 157, 480-487.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Co-protoporphyrin 0.005 mM, 82.5% inhibition of kidney heme oxygenase Homo sapiens
Fe-deuteroporphyrin IX 2,4-bisglycol 0.01 mM, 46.8% inhibition of kidney heme oxygenase Homo sapiens
Porphyrins Zn-deuteroporphyrin IX 2,4-bis glycol, synthetic metal porphyrins Homo sapiens
Sn-protoporphyrin 0.005 mM, complete inhibition of kidney heme oxygenase Homo sapiens
Zn-deuteroporphyrin IX 2,4-bisglycol 0.002 mM, complete inhibition of kidney heme oxygenase Homo sapiens
Zn-protoporphyrin 0.005 mM, 93.4% inhibition of kidney heme oxygenase Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Homo sapiens
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
x * 32000, kidney heme oxygenase, immunoblot Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00000625
-
activity in kidney microsomes, micromol bilirubin/min/mg Homo sapiens

Subunits

Subunits Comment Organism
? x * 32000, kidney heme oxygenase, immunoblot Homo sapiens