Q8RNT4 · LOX_PSEAI
- ProteinLinoleate 9/13-lipoxygenase
- Genelox
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids685 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
In presence of oxygen, converts linoleate into (9S)-hydroperoxy-10,12-octadecenoate (9HPOD), which spontaneously decomposes to the corresponding 9-hydroxy-10,12-octadecenoate (9HOD), and into 13-hydroperoxy-9,11-octadecenoate (13HPOD) which spontaneously decomposes to the corresponding 13-hydroxy-9,11-octadecenoate (13HOD). Also active on linolenate. To a lesser extent, is also able to convert oleate into (10S)-hydroperoxy-8E-octadecenoate, which spontaneously decomposes to the corresponding 10-hydroxy-8E-octadecenoate. Is almost not active on arachidonate.
Miscellaneous
In vitro, under anaerobic conditions, does not transform linoleate or oleate into the corresponding hydroxy derivative.
Catalytic activity
- (9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-octadecadienoate
Cofactor
Note: Binds 1 Fe cation per subunit.
Activity regulation
Inhibited by Ba2+, Zn2+ and Fe3+.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
78.9 μM | linoleate (Ref.4) | |||||
0.74 mM | oleate | |||||
0.66 mM | linoleate | |||||
0.73 mM | linolenate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.246 μmol/min/mg | with oleate as substrate | ||||
81.75 μmol/min/mg | with linoleate as substrate (Ref.4) |
kcat is 96 sec-1 with linoleate as substrate (Ref.4).
pH Dependence
Optimum pH is 7 with linoleate as substrate, and 8.5-9.0 with oleate as substrate.
Temperature Dependence
Optimum temperature is 25-30 degrees Celsius. Active up to 45 degrees Celsius, less active after 50 degrees Celsius and completely inactive at 70 degrees Celsius.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 377 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 382 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 555 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 559 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Binding site | 685 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: I |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
Molecular Function | linoleate 13S-lipoxygenase activity | |
Molecular Function | linoleate 9S-lipoxygenase activity | |
Molecular Function | metal ion binding | |
Biological Process | lipid oxidation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLinoleate 9/13-lipoxygenase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ8RNT4
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MKRRSVLLSGVALSGTALA | ||||||
Chain | PRO_0000018330 | 20-685 | Linoleate 9/13-lipoxygenase | |||
Sequence: NDSIFFSPLKYLGAEQQRSIDASRSLLDNLIPPSLPQYDNLAGKLARRAVLTSKKLVYVWTENFANVKGVPMARSVPLGELPNVDWLLKTAGVIVELIVNFVASLPASAAAQFERIAAGLSGDLEAARQVHEALLEEAKNDPAAAGSLLLRFTELQTRVIALLTRVGLLVDDILKSASNLVTQGGQGDGLNRFRAVFGTLRLPEVADSFRDDEAFAYWRVAGPNPLLIRRVDALPANFPLGEEQFRRVMGADDSLLEAAASRRLYLLDYAELGKLAPSGAVDKLLTGTGFAYAPIALFALGKDRAGLLPVAIQCGQDPATHPMFVRPAESESDLYWGWQMAKTVVQVAEENYHEMFVHLAQTHLVSEAFCLATQRTLAPSHPLHVLLAPHFEGTLFINEGAARILLPSAGFIDVMFAAPIQDTQATAGGNRLGFDFYRGMLPESLKARNVDDPAALPDYPYRDDGLLVWNAIRQWAADYVAVYYASDGDVTADVELAAWVGEVIGSGKVAGFRPITGRSQLVEVLTMVIFTASAQHAAVNFPQPSMMTYAPAICAMSAAPAPDSPSGKSEADWLKMMPPTLVALEKVNIYHLLGSVYHGRLGDYRQTGFPYAPVFSDRRVTASGGPLERFQARLKEVEATIRTRNQARRKPYEYLLPSRIPASTNI |
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 122-685 | Lipoxygenase | ||||
Sequence: ASLPASAAAQFERIAAGLSGDLEAARQVHEALLEEAKNDPAAAGSLLLRFTELQTRVIALLTRVGLLVDDILKSASNLVTQGGQGDGLNRFRAVFGTLRLPEVADSFRDDEAFAYWRVAGPNPLLIRRVDALPANFPLGEEQFRRVMGADDSLLEAAASRRLYLLDYAELGKLAPSGAVDKLLTGTGFAYAPIALFALGKDRAGLLPVAIQCGQDPATHPMFVRPAESESDLYWGWQMAKTVVQVAEENYHEMFVHLAQTHLVSEAFCLATQRTLAPSHPLHVLLAPHFEGTLFINEGAARILLPSAGFIDVMFAAPIQDTQATAGGNRLGFDFYRGMLPESLKARNVDDPAALPDYPYRDDGLLVWNAIRQWAADYVAVYYASDGDVTADVELAAWVGEVIGSGKVAGFRPITGRSQLVEVLTMVIFTASAQHAAVNFPQPSMMTYAPAICAMSAAPAPDSPSGKSEADWLKMMPPTLVALEKVNIYHLLGSVYHGRLGDYRQTGFPYAPVFSDRRVTASGGPLERFQARLKEVEATIRTRNQARRKPYEYLLPSRIPASTNI |
Sequence similarities
Belongs to the lipoxygenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length685
- Mass (Da)74,519
- Last updated2010-06-15 v2
- Checksum4F56EFE0780295FA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF479686 EMBL· GenBank· DDBJ | AAL85880.2 EMBL· GenBank· DDBJ | Genomic DNA |