Literature summary for 1.14.14.1 extracted from

Connick, J.P.; Reed, J.R.; Cawley, C.F.; Backes, W.L.
Heteromeric complex formation between human cytochrome P450 CYP1A1 and heme oxygenase-1 (2021), Biochem. J., 478, 377-388 .

Search for more literature for 1.14.14.1

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0001	-	7-ethoxyresorufin	complex POR-CYP1A1, pH 7.5, 37°C	Homo sapiens
0.0012	-	7-ethoxyresorufin	complex POR-CYP1A1, presence of heme oxygenase, pH 7.5, 37°C	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P04798	isoform CYP1A1	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2	-	Homo sapiens	resorufin + ethanol + [oxidized NADPH-hemoprotein reductase] + H2O	-	?

Synonyms

Synonyms	Comment	Organism
CYP1A1	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	heme oxygenase HO-1 and CYP1A1 form a stable complex that is further stabilized in the presence of NADPH-cytochrome P450 reductase POR. The POR-CYP1A1 complex is readily disrupted by the addition of HO-1. CYP1A1 also is able to affect the POR-HO-1 complex. The interaction between CYP1A1 and HO-1 affects function, the presence of CYP1A1 inhibits HO-1-mediated bilirubin formation by increasing the Km of POR-HO-1 without affecting the Vmax. HO-1 inhibits CYP1A1-mediated 7-ethoxyresorufin dealkylation by increasing the Km of POR-CYP1A1	Homo sapiens

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Release 2023.1 (January 2023)