EC Number   |
General Information |
Reference |
|---|
   1.13.11.B6 | evolution |
9S-LOX contains catalytic manganese, and its sequence can be aligned with 77% identity to 13R-LOX with catalytic manganese lipoxygenase of the Take-all fungus. Alterations in the Sloane determinant of 9S-LOX and 13R-MnLOX with larger and smaller hydrophobic residues interconvert the regiospecifi c oxidation of 18:2 n-6, presumably by altering the substrate position in relation to oxygen insertion |
-, 725658 |
| 1.13.11.B6 | evolution |
DNA and amino acid sequence determination and analysis of LOX1 and LOX2 isozymes, phylogenetic analysis, only LOX1:Md:1a exhibits a glycine residue (Gly567) responsible for dual positional specificity and (R)-LOX activity |
742627 |
| 1.13.11.B6 | metabolism |
the enzyme is involved in the LOX pathway, overview |
742627 |
| 1.13.11.B6 | more |
9S-MnLOX catalyzes hydrogen abstraction at C-11 and oxygenation at C-9 and C-11 in a suprafacial manner in analogy with 13R-MnLOX, EC 1.13.11.45 |
-, 725658 |
| 1.13.11.B6 | more |
fatty acid composition of Lasiodiplodia theobromae determined by GC-MS analysis after hydrolysis, overview |
-, 725856 |
| 1.13.11.B6 | more |
fatty acid composition ofLasiodiplodia theobromae determined by GC-MS analysis after hydrolysis, overview |
-, 725856 |
| 1.13.11.B6 | more |
structure homology modeling |
742627 |
| 1.13.11.B6 | more |
the bulky polar heads of glycerolipids like monolinolenoylglycerol and 2-linoleoyl-sn-glycero-3-phosphorylcholine cannot penetrate into the LOX active site. Thus, both (9S)- and (13S)-hydroperoxides can be produced when substrate is arranged within LOX active site in the methyl end first orientation |
724736 |
| 1.13.11.B6 | physiological function |
lipoxygenase (LOX) is an important contributor to the formation of aroma-active C6 aldehydes in apple (Malus3domestica) fruit upon tissue disruption, role in autonomously produced aroma volatiles from intact tissue, overview. The genetic association with a quantitative trait locus for fruit ester and the remarkable agreement in regio- and stereoselectivity of the LOX1:Md:1a reaction with the overall LOX activity found in mature apple fruits, suggest a major physiological function of LOX1:Md:1a during climacteric ripening of apples. While isozymes LOX1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b may contribute to aldehyde production in immature fruit upon cell disruption isozyme, LOX1:Md:1a probably regulates the availability of precursors for ester production in intact fruit tissue. Both 9- and 13-hydroperoxides can be catabolized to aroma-active volatile aldehydes by hydroperoxide lyase. Only 13-LOX activity contributes to the apple aroma due to the formation of precursors of C6 volatile compounds. The dioxygenation of PUFAs by 9- and 13-LOX activity forms precursors for important phytooxylipins with functions in plant defense, wound signaling, senescence and fruit ripening |
742627 |
| 1.13.11.B6 | physiological function |
LOXN2 may be involved in late mechanisms of host resistance |
706289 |
