G1L8V2 · G1L8V2_AILME
- ProteinCytochrome P450 2E1
- GeneCYP2E1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids494 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids. May be involved in the oxidative metabolism of xenobiotics.
Catalytic activity
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 21-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- (5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = 13-hydroxytetradecanoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxydodecanoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
Cofactor
Activity regulation
The omega-1 hydroxylase activity is stimulated by cytochrome b5.
Pathway
Lipid metabolism; fatty acid metabolism.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | mitochondrial inner membrane | |
Molecular Function | 4-nitrophenol 2-monooxygenase activity | |
Molecular Function | aromatase activity | |
Molecular Function | enzyme binding | |
Molecular Function | heme binding | |
Molecular Function | Hsp70 protein binding | |
Molecular Function | Hsp90 protein binding | |
Molecular Function | iron ion binding | |
Molecular Function | long-chain fatty acid omega-1 hydroxylase activity | |
Biological Process | 4-nitrophenol metabolic process | |
Biological Process | lipid hydroxylation | |
Biological Process | long-chain fatty acid metabolic process | |
Biological Process | monoterpenoid metabolic process | |
Biological Process | steroid metabolic process | |
Biological Process | xenobiotic metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome P450 2E1
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Ursidae > Ailuropoda
Accessions
- Primary accessionG1L8V2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Peripheral membrane protein
Microsome membrane ; Peripheral membrane protein
Mitochondrion inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
Interaction
Subunit
Interacts with chaperones HSP70 and HSP90; this interaction is required for initial targeting to mitochondria.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length494
- Mass (Da)56,556
- Last updated2011-10-19 v1
- Checksum018CEA663B1A2E8B
Keywords
- Technical term