Cloned (Comment) | Organism |
---|---|
gene CYPP4504A11, located on chromosome 7, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time RT PCR enzyme expression analysis, recombinant expression in Escherichia coli | Callithrix jacchus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
microsome | - |
Callithrix jacchus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | in heme | Callithrix jacchus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2 | Callithrix jacchus | - |
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
lauric acid + [reduced NADPH-hemoprotein reductase] + O2 | Callithrix jacchus | - |
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
additional information | Callithrix jacchus | Marmoset CYP4A11 enzyme heterologously expressed in Escherichia coli preferentially catalyzes the omega-hydroxylation of arachidonic acid and lauric acid, similar to enzymes from Macaca fascicularis and Homo sapiens. The lauric acid omega-hydroxylation activity of marmoset CYP4A11 is low compared with those of marmoset liver microsomes | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Callithrix jacchus | A0A1P8NQJ7 | white-tufted-ear marmoset | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
kidney | highest expression level | Callithrix jacchus | - |
liver | - |
Callithrix jacchus | - |
additional information | expression pattern by real-time RT PCR and immunoblottig. No expression in brains, lungs, and small intestines | Callithrix jacchus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2 | - |
Callithrix jacchus | 20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
lauric acid + [reduced NADPH-hemoprotein reductase] + O2 | - |
Callithrix jacchus | 12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
additional information | Marmoset CYP4A11 enzyme heterologously expressed in Escherichia coli preferentially catalyzes the omega-hydroxylation of arachidonic acid and lauric acid, similar to enzymes from Macaca fascicularis and Homo sapiens. The lauric acid omega-hydroxylation activity of marmoset CYP4A11 is low compared with those of marmoset liver microsomes | Callithrix jacchus | ? | - |
? | |
additional information | the enzyme sequence contains consensus sequences of six substrate recognition sites. Marmoset CYP4A11 enzyme heterologously expressed in Escherichia coli preferentially catalyzes the omega-hydroxylation of arachidonic acid and lauric acid, similar to enzymes from Macaca fascicularis and Homo sapiens. The lauric acid omega-hydroxylation activity of marmoset CYP4A11 is low compared with those of marmoset liver microsomes. CYP4A11 hydroxylates fatty acids at their omega and omega-1 positions | Callithrix jacchus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CYP4A11 | - |
Callithrix jacchus |
Fatty acid omega-hydroxylase | - |
Callithrix jacchus |
omega-hydroxylase | - |
Callithrix jacchus |
P450 4A11 | - |
Callithrix jacchus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome P450 | - |
Callithrix jacchus | |
heme | the enzyme contains one heme-binding domain | Callithrix jacchus | |
NADPH | - |
Callithrix jacchus |