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Literature summary extracted from

  • Cooper, C.E.; Davies, N.A.; Psychoulis, M.; Canevari, L.; Bates, T.E.; Dobbie, M.S.; Casley, C.S.; Sharpe, M.A.
    Nitric oxide and peroxynitrite cause irreversible increases in the K(m) for oxygen of mitochondrial cytochrome oxidase: in vitro and in vivo studies (2003), Biochim. Biophys. Acta, 1607, 27-34.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.9 CO competitive and reversible Bos taurus
7.1.1.9 nitric oxide competitive and reversible. Nanomolar levels inhibit the enzyme by competing with oxygen at the enzyme‘s heme-copper active site. This raises the Km for cellular respiration into the physiological range Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.9 mitochondrion
-
Bos taurus 5739
-

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.9 Bos taurus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.1.1.9 heart
-
Bos taurus
-