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Literature summary for 1.14.14.80 extracted from

  • Kim, D.; Cha, G.S.; Nagy, L.D.; Yun, C.H.; Guengerich, F.P.
    Kinetic analysis of lauric acid hydroxylation by human cytochrome P450 4A11 (2014), Biochemistry, 53, 6161-6172 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.14.80

Activating Compound

Activating Compound Comment Organism Structure
cytochrome b5 stimulates steady-state lauric acid omega-hydroxylation about 2fold Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
lauric acid + [reduced NADPH-hemoprotein reductase] + O2 + H+ Homo sapiens
-
 12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
additional information Homo sapiens substrate and product binding and release are much faster than overall rates of catalysis. Both the transfer of an electron to the ferrous-O2 complex and C-H bond-breaking limit the rate of P450 4A11 omega-oxidation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q02928
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lauric acid + [reduced NADPH-hemoprotein reductase] + O2 + H+
-
 Homo sapiens 12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
additional information substrate and product binding and release are much faster than overall rates of catalysis. Both the transfer of an electron to the ferrous-O2 complex and C-H bond-breaking limit the rate of P450 4A11 omega-oxidation Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
cytochrome P450 4A11
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
cytochrome P450 reduction of ferric P450 4A11 to ferrous is rapid and not rate-limiting Homo sapiens