Literature summary extracted from
Mishra, V.K.; Mishra, S.
Flipped regiospecificity in L434F mutant of 8-lipoxygenase (2020), Phys. Chem. Chem. Phys., 22, 16013-16022 .
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.13.11.40 |
L434F |
mutation alters the regio- and stereospecificity of the final products, with a product ratio of 66 : 34 for 8R- and 12S-hydroperoxide, respectively. In the closed conformation, the phenyl group of Phe434 shields the C8 site of the substrate, preventing access of the oxygen molecule to this site, which leads to a quenching of the 8R-product. Both closed and open conformations of Phe434 allow the oxygen molecule to approach the pro-S face of the C12 site of the substrate, which enhances the propensity of the 12S-hydroperoxide |
Plexaura homomalla |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.13.11.40 |
Plexaura homomalla |
O16025 |
bifunctional allene oxide synthase-lipoxygenase protein |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.13.11.40 |
allene oxide synthase-lipoxygenase protein |
- |
Plexaura homomalla |