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Literature summary for 1.6.2.4 extracted from

  • Higashimoto, Y.; Sugishima, M.; Sato, H.; Sakamoto, H.; Fukuyama, K.; Palmer, G.; Noguchi, M.
    Mass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductase (2008), Biochem. Biophys. Res. Commun., 367, 852-858.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.6.2.4

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus the presence of NADPH-cytochrome P450 reductase prevents heme oxygenase-1 from acetylation of lysine residues, Lys149 and Lys153, located in the F-helix. The heme degradation activity of the fully acetylated heme oxygenase-1 in the NADPH/NADPH-cytochrome P450 reductase-supported system is significantly reduced, whereas almost no inactivation is detected in heme oxygenase-1 in the presence of NADPH-cytochrome P450 reductase, which prevents acetylation of Lys149 and Lys153 ?
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus P00388 recombinant
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Source Tissue

Source Tissue Comment Organism Textmining
liver
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 Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the presence of NADPH-cytochrome P450 reductase prevents heme oxygenase-1 from acetylation of lysine residues, Lys149 and Lys153, located in the F-helix. The heme degradation activity of the fully acetylated heme oxygenase-1 in the NADPH/NADPH-cytochrome P450 reductase-supported system is significantly reduced, whereas almost no inactivation is detected in heme oxygenase-1 in the presence of NADPH-cytochrome P450 reductase, which prevents acetylation of Lys149 and Lys153 Rattus norvegicus ?
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Synonyms

Synonyms Comment Organism
CPR
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 Rattus norvegicus
NADPH-cytochrome P450 reductase
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 Rattus norvegicus