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Literature summary for 1.6.2.4 extracted from

  • Brignac-Huber, L.; Reed, J.R.; Backes, W.L.
    Organization of NADPH-cytochrome P450 reductase and CYP1A2 in the endoplasmic reticulum - microdomain localization affects monooxygenase function (2011), Mol. Pharmacol., 79, 549-557.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum 68% of the enzyme resides in detergent-resistant lipid microdomains of the endoplasmic reticulum. The unique lipid components of these domains enhance CYP1A2 substrate metabolism through greater efficiency in CPR/CYP1A2 binding, lipid composition analysis, overview. Lipid composition of purified lipid vesicles affects CYP1A2 substrate metabolism and CPR-CYP1A2 binding Oryctolagus cuniculus 5783
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membrane colocalization with cytochromes P450 Oryctolagus cuniculus 16020
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microsome
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Oryctolagus cuniculus
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Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
extraction of native enzyme from liver microsomes by Brij 98 solubilization and isolation of detergent-resistant membranes by sucrose gradient centrifugation Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
liver
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Oryctolagus cuniculus
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Synonyms

Synonyms Comment Organism
CPR
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Oryctolagus cuniculus
NADPH-cytochrome P450 reductase
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Oryctolagus cuniculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Oryctolagus cuniculus

General Information

General Information Comment Organism
additional information interaction analysis of membrane-located enzyme CPR with cytochrome P450 CYP1A2, overview Oryctolagus cuniculus