Protein Variants | Comment | Organism |
---|---|---|
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 |
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 |
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 |
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] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
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 | |
0.0052 | - |
O2 | pH 7.4, wild-type enzyme, with substrate linoleic acid | Oryctolagus cuniculus | |
0.007 | - |
O2 | pH 7.4, mutant L367W, with substrate linoleic acid | Oryctolagus cuniculus | |
0.009 | - |
O2 | pH 7.4, mutant L367E, with substrate linoleic acid | Oryctolagus cuniculus | |
0.009 | - |
O2 | pH 7.4, mutant L367K, with substrate linoleic acid | Oryctolagus cuniculus | |
0.0401 | - |
O2 | pH 7.4, mutant L367F, with substrate linoleic acid | Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
arachidonate + O2 | Oryctolagus cuniculus | - |
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
arachidonate + O2 | - |
Oryctolagus cuniculus | (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate | - |
? | |
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 | - |
? | |
linoleic acid + O2 | reaction of EC 1.13.11.12 | Oryctolagus cuniculus | ? | - |
? | |
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 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | structural modeling, overview | Oryctolagus cuniculus |
Synonyms | Comment | Organism |
---|---|---|
12/15-lipoxygenase | - |
Oryctolagus cuniculus |
12/15-LOX | - |
Oryctolagus cuniculus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.3 | - |
O2 | pH 7.4, mutant L367K, with substrate linoleic acid | Oryctolagus cuniculus | |
2.2 | - |
O2 | pH 7.4, mutant L367E, with substrate linoleic acid | Oryctolagus cuniculus | |
4.4 | - |
O2 | pH 7.4, mutant L367W, with substrate linoleic acid | Oryctolagus cuniculus | |
5.6 | - |
O2 | pH 7.4, mutant L367F, with substrate linoleic acid | Oryctolagus cuniculus | |
13.7 | - |
O2 | pH 7.4, wild-type enzyme, with substrate linoleic acid | Oryctolagus cuniculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Oryctolagus cuniculus |