CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
4 | Few Secondary Structures |
|
4.10 | Irregular |
|
4.10.375 | Lipoxygenase-1; domain 2 |
|
4.10.375.10 | Lipoxygenase-1; Domain 2 |
Domain Context
CATH Clusters
| Superfamily | Lipoxygenase-1; Domain 2 |
| Functional Family | Lipoxygenase |
Enzyme Information
| 1.13.11.58 |
Linoleate 9S-lipoxygenase.
based on mapping to UniProt P09186
Linoleate + O(2) = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate.
-!- A common plant lipoxygenase that oxidizes linoleate and alpha- linolenate, the two most common polyunsaturated fatty acids in plants, by inserting molecular oxygen at the C(9) position with (S)- configuration. -!- The enzyme plays a physiological role during the early stages of seedling growth. -!- The enzyme from Arabidopsis thaliana shows comparable activity toward linoleate and linolenate. -!- EC 1.13.11.12 catalyzes a similar reaction at another position of these fatty acids.
|
UniProtKB Entries (1)
| P09186 |
LOX3_SOYBN
Glycine max
Seed linoleate 9S-lipoxygenase-3
|
PDB Structure
| PDB | 1RRL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Effect of crystal freezing and small-molecule binding on internal cavity size in a large protein: X-ray and docking studies of lipoxygenase at ambient and low temperature at 2.0 A resolution.
Acta Crystallogr.,Sect.D
|
