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Literature summary extracted from

  • Saam, J.; Ivanov, I.; Walther, M.; Holzhuetter, H.G.; Kuhn, H.
    Molecular dioxygen enters the active site of 12/15-lipoxygenase via dynamic oxygen access channels (2007), Proc. Natl. Acad. Sci. USA, 104, 13319-13324.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.31 L367E site-directed mutagenesis, site-directed mutagenesis, the mutant shows reduced activity with O2 compared to the wild-type enzyme, L367 is involved in oxygen access, overview Oryctolagus cuniculus
1.13.11.31 L367F site-directed mutagenesis, site-directed mutagenesis, the mutant shows reduced activity with O2 compared to the wild-type enzyme, in silico mutagenesis and structural modeling, L367 is involved in oxygen access, overview Oryctolagus cuniculus
1.13.11.31 L367K site-directed mutagenesis, site-directed mutagenesis, the mutant shows reduced activity with O2 compared to the wild-type enzyme, L367 is involved in oxygen access, overview Oryctolagus cuniculus
1.13.11.31 L367W site-directed mutagenesis, site-directed mutagenesis, the mutant shows reduced activity with O2 compared to the wild-type enzyme, L367 is involved in oxygen access, overview Oryctolagus cuniculus
1.13.11.33 L367E site-directed mutagenesis, site-directed mutagenesis, the mutant shows reduced activity with O2 compared to the wild-type enzyme, L367 is involved in oxygen access, overview Oryctolagus cuniculus
1.13.11.33 L367F site-directed mutagenesis, site-directed mutagenesis, the mutant shows reduced activity with O2 compared to the wild-type enzyme, in silico mutagenesis and structural modeling, L367 is involved in oxygen access, overview Oryctolagus cuniculus
1.13.11.33 L367K site-directed mutagenesis, site-directed mutagenesis, the mutant shows reduced activity with O2 compared to the wild-type enzyme, L367 is involved in oxygen access, overview Oryctolagus cuniculus
1.13.11.33 L367W site-directed mutagenesis, site-directed mutagenesis, the mutant shows reduced activity with O2 compared to the wild-type enzyme, L367 is involved in oxygen access, overview Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.31 additional information
-
 additional information free-energy distribution for oxygen inside the substrate-free rabbit 12/15-LOX, containing four nested free-energy isosurfaces with different energy levels, overview Oryctolagus cuniculus
1.13.11.31 0.0052
-
 O2 pH 7.4, wild-type enzyme, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.31 0.007
-
 O2 pH 7.4, mutant L367W, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.31 0.009
-
 O2 pH 7.4, mutant L367E, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.31 0.009
-
 O2 pH 7.4, mutant L367K, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.31 0.0401
-
 O2 pH 7.4, mutant L367F, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.33 additional information
-
 additional information free-energy distribution for oxygen inside the substrate-free rabbit 12/15-LOX, containing four nested free-energy isosurfaces with different energy levels, overview Oryctolagus cuniculus
1.13.11.33 0.0052
-
 O2 pH 7.4, wild-type enzyme, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.33 0.007
-
 O2 pH 7.4, mutant L367W, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.33 0.009
-
 O2 pH 7.4, mutant L367E, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.33 0.009
-
 O2 pH 7.4, mutant L367K, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.33 0.0401
-
 O2 pH 7.4, mutant L367F, with substrate linoleic acid Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.31 arachidonate + O2 Oryctolagus cuniculus
-
 (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate
-
 ?
1.13.11.33 arachidonate + O2 Oryctolagus cuniculus
-
 (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.31 Oryctolagus cuniculus
-
-
-
1.13.11.33 Oryctolagus cuniculus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.31 arachidonate + O2
-
 Oryctolagus cuniculus (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate
-
 ?
1.13.11.31 arachidonate + O2 high oxygen affinity is important for effective catalysis, L367 is involved in oxygen access, channel structure, overview, arachidonic acid closes the substrate-binding pocket for oxygen diffusion but opens a fourth oxygen access channel Oryctolagus cuniculus (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate
-
 ?
1.13.11.31 linoleic acid + O2 reaction of EC 1.13.11.12 Oryctolagus cuniculus ?
-
 ?
1.13.11.31 additional information the bifunctional enzyme also forms (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate, the product of 15-LO activity, EC 1.13.11.33, in a ratio of 9:1 15(S)-HPETE to 12(S)-HPETE Oryctolagus cuniculus ?
-
 ?
1.13.11.33 arachidonate + O2
-
 Oryctolagus cuniculus (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
 ?
1.13.11.33 arachidonate + O2 high oxygen affinity is important for effective catalysis, L367 is involved in oxygen access, channel structure, overview, arachidonic acid closes the substrate-binding pocket for oxygen diffusion but opens a fourth oxygen access channel Oryctolagus cuniculus (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
 ?
1.13.11.33 linoleic acid + O2 reaction of EC 1.13.11.12 Oryctolagus cuniculus ?
-
 ?
1.13.11.33 additional information the bifunctional enzyme also forms (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate, the product of 12-LO activity, EC 1.13.11.31, in a ratio of 9:1 15(S)-HPETE to 12(S)HPETE Oryctolagus cuniculus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.11.31 More structural modeling, overview Oryctolagus cuniculus
1.13.11.33 More structural modeling, overview Oryctolagus cuniculus

Synonyms

EC Number Synonyms Comment Organism
1.13.11.31 12/15-lipoxygenase
-
 Oryctolagus cuniculus
1.13.11.31 12/15-LOX
-
 Oryctolagus cuniculus
1.13.11.33 12/15-lipoxygenase
-
 Oryctolagus cuniculus
1.13.11.33 12/15-LOX
-
 Oryctolagus cuniculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.31 0.3
-
 O2 pH 7.4, mutant L367K, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.31 2.2
-
 O2 pH 7.4, mutant L367E, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.31 4.4
-
 O2 pH 7.4, mutant L367W, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.31 5.6
-
 O2 pH 7.4, mutant L367F, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.31 13.7
-
 O2 pH 7.4, wild-type enzyme, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.33 0.3
-
 O2 pH 7.4, mutant L367K, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.33 2.2
-
 O2 pH 7.4, mutant L367E, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.33 4.4
-
 O2 pH 7.4, mutant L367W, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.33 5.6
-
 O2 pH 7.4, mutant L367F, with substrate linoleic acid Oryctolagus cuniculus
1.13.11.33 13.7
-
 O2 pH 7.4, wild-type enzyme, with substrate linoleic acid Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.31 7.4
-
 assay at Oryctolagus cuniculus
1.13.11.33 7.4
-
 assay at Oryctolagus cuniculus