EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.13.11.B6 | more |
both the wild type ZmLOX and A562G mutant dioxygenate monolinolenoylglycerol and 2-linoleoyl-sn-glycero-3-phosphorylcholine, the latter being a poor substrate. Both oxidize the monolinolenoylglycerol predominantly into (9S)-hydroperoxide. The oxidation of 2-linoleoyl-sn-glycero-3-phosphorylcholine exhibits limited regio- and stereospecificity: the wild-type ZmLOX produces some predominance of (13S)-hydroperoxide. In contrast, the A562G mutant produces some excess of (9S)-hydroperoxide |
Zea mays |
? |
- |
? |
| 1.13.11.B6 | more |
Bulky polar heads of glycerolipids cannot penetrate into the LOX active site. Both (9S)- and (13S)-hydroperoxides can be produced when the substrate is arranged within LOX active site in the methyl end first orientation. 1-Linoleoyl-snglycero-3-phosphorylcholine is a poor substrate for both wild-type and A562G mutant. No activity of wild-type and mutant with 2-O-alpha-linolenoyl-3-O-beta-D-galactopyranosyl-sn-glycerol, dilinolenoylglycerol, and trilinolenoylglycerol |
Zea mays |
? |
- |
? |
| 1.13.11.B6 | more |
cf. EC 1.13.11.45, LC- and GC-MS analysis product analysis, overview. Authentic (11S)-hydroperoxyoctadecadienoate is rapidly transformed to 9-hydroperoxyoctadecadienoate by 9S-MnLOX, and only traces of 13-hydroperoxyoctadecadienoate. 9S-MnLOX also partly transforms authentic (13R)-hydroperoxyoctadecadienoate to (9S)-hydroperoxyoctadecadienoate |
Nakataea oryzae |
? |
- |
? |
| 1.13.11.B6 | more |
the putative 9R-dioxygenase catalyzes stereospecific removal of the 11R hydrogen followed by suprafacial attack of dioxygen at C-9 |
Lasiodiplodia theobromae |
? |
- |
? |
| 1.13.11.B6 | more |
regio- and stereospecificity analysis of isozyme substrate specificity, recombinant LOX1:Md:1a, LOX1:Md:1c, LOX2:Md:2a and LOX2:Md:2b isozymes show 13/9-LOX, 9-LOX, 13/9-LOX and 13-LOX activity with linoleic acid, respectively. While products of LOX1:Md:1c and LOX2:Md:2b are S-configured, LOX1:Md:1a and LOX2:Md:2a form 13(R)-hydroperoxides as major products. Oxygenation in the carbon backbone of linoleic acid occurs either at carbon atom 9 (9-LOX) or 13 (13-LOX), forming the corresponding hydroperoxy derivatives, respectively. LOX enzymes are not perfectly specific and biocatalysts that produce more than 10% of the alternative regio-isomer are called dual positional specific LOX |
Malus domestica |
? |
- |
? |
| 1.13.11.B6 | more |
the putative 9R-dioxygenase catalyzes stereospecific removal of the 11R hydrogen followed by suprafacial attack of dioxygen at C-9 |
Lasiodiplodia theobromae 2334 |
? |
- |
? |
| 1.13.11.B6 | more |
cf. EC 1.13.11.45, LC- and GC-MS analysis product analysis, overview. Authentic (11S)-hydroperoxyoctadecadienoate is rapidly transformed to 9-hydroperoxyoctadecadienoate by 9S-MnLOX, and only traces of 13-hydroperoxyoctadecadienoate. 9S-MnLOX also partly transforms authentic (13R)-hydroperoxyoctadecadienoate to (9S)-hydroperoxyoctadecadienoate |
Nakataea oryzae CBS 288.54 |
? |
- |
? |
| 1.13.11.B6 | more |
the putative 9R-dioxygenase catalyzes stereospecific removal of the 11R hydrogen followed by suprafacial attack of dioxygen at C-9 |
Lasiodiplodia theobromae CBS 117454 |
? |
- |
? |
| 1.13.11.B6 | more |
the putative 9R-dioxygenase catalyzes stereospecific removal of the 11R hydrogen followed by suprafacial attack of dioxygen at C-9 |
Lasiodiplodia theobromae CBS 122127 |
? |
- |
? |
| 1.13.11.B6 | phosphorylcholine + O2 |
activity with the wild-type enzyme, no activity with mutant A562G |
Zea mays |
? |
- |
? |
