Q8RNT4 · LOX_PSEAI

  • Protein
    Linoleate 9/13-lipoxygenase
  • Gene
    lox
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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.

Caution

The biochemical characterization done in PubMed:15028873 is devoted to oleic acid, however, the preferred substrate of the enzyme is linoleic acid.

Catalytic activity

Cofactor

Fe cation (UniProtKB | Rhea| CHEBI:24875 )

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 μMlinoleate (Ref.4)
0.74 mMoleate
0.66 mMlinoleate
0.73 mMlinolenate
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
0.246 μmol/min/mgwith oleate as substrate
81.75 μmol/min/mgwith 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.

TypeIDPosition(s)Description
Binding site377Fe cation (UniProtKB | ChEBI); catalytic
Binding site382Fe cation (UniProtKB | ChEBI); catalytic
Binding site555Fe cation (UniProtKB | ChEBI); catalytic
Binding site559Fe cation (UniProtKB | ChEBI); catalytic
Binding site685Fe cation (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentperiplasmic space
Molecular Functionlinoleate 13S-lipoxygenase activity
Molecular Functionlinoleate 9S-lipoxygenase activity
Molecular Functionmetal ion binding
Biological Processlipid oxidation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Linoleate 9/13-lipoxygenase
  • EC number
  • Alternative names
    • Oleate 10S-lipoxygenase (EC:1.13.11.77
      ) . EC:1.13.11.77 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      lox

Organism names

  • Taxonomic identifier
  • Strain
    • 42A2 / NCIMB 40045
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    Q8RNT4

Subcellular Location

Periplasm

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_000001833020-685Linoleate 9/13-lipoxygenase

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain122-685Lipoxygenase

Sequence similarities

Belongs to the lipoxygenase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    685
  • Mass (Da)
    74,519
  • Last updated
    2010-06-15 v2
  • Checksum
    4F56EFE0780295FA
MKRRSVLLSGVALSGTALANDSIFFSPLKYLGAEQQRSIDASRSLLDNLIPPSLPQYDNLAGKLARRAVLTSKKLVYVWTENFANVKGVPMARSVPLGELPNVDWLLKTAGVIVELIVNFVASLPASAAAQFERIAAGLSGDLEAARQVHEALLEEAKNDPAAAGSLLLRFTELQTRVIALLTRVGLLVDDILKSASNLVTQGGQGDGLNRFRAVFGTLRLPEVADSFRDDEAFAYWRVAGPNPLLIRRVDALPANFPLGEEQFRRVMGADDSLLEAAASRRLYLLDYAELGKLAPSGAVDKLLTGTGFAYAPIALFALGKDRAGLLPVAIQCGQDPATHPMFVRPAESESDLYWGWQMAKTVVQVAEENYHEMFVHLAQTHLVSEAFCLATQRTLAPSHPLHVLLAPHFEGTLFINEGAARILLPSAGFIDVMFAAPIQDTQATAGGNRLGFDFYRGMLPESLKARNVDDPAALPDYPYRDDGLLVWNAIRQWAADYVAVYYASDGDVTADVELAAWVGEVIGSGKVAGFRPITGRSQLVEVLTMVIFTASAQHAAVNFPQPSMMTYAPAICAMSAAPAPDSPSGKSEADWLKMMPPTLVALEKVNIYHLLGSVYHGRLGDYRQTGFPYAPVFSDRRVTASGGPLERFQARLKEVEATIRTRNQARRKPYEYLLPSRIPASTNI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF479686
EMBL· GenBank· DDBJ
AAL85880.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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