Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta(DE3)pLysS | Zea mays |
Protein Variants | Comment | Organism |
---|---|---|
A562G | site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme | Zea mays |
A562G | the mutation does not affect the relative yield of 13-hydroperoxide, but increases the proportion of (13R)-enantiomer compared to the wild-type enzyme | Zea mays |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
linoleate + O2 | Zea mays | - |
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate | - |
? | |
linoleate + O2 | Zea mays | - |
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate | - |
? | |
additional information | Zea mays | 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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | - |
- |
- |
Zea mays | Q9AXG8 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2 | - |
Zea mays | ? | - |
? | |
1,2-di-O-alpha-linolenoyl-3-O-beta-D-galactopyranosyl-sn-glycerol + O2 | low activity with the wild-type enzyme, no activity with mutant A562G | Zea mays | ? | - |
? | |
2-linoleoyl-sn-glycero-3-phosphorylcholine + O2 | low activity of wild-type and A562G mutant. The wild-type enzyme predominantly produces (13S)-hydroperoxide. The A562G mutant form possesses lesser regio- and stereospecificity during the dioxygenation of lysoPC. It produces 28% of (10E,12Z)-9-hydroperoxide and 30% of (9Z,11E)-13-hydroperoxide along with 41% of (all-E)-hydroperoxides. While 9-hydroperoxide is present mainly (61%) as S-enantiomer, (9Z,11E)-13-hydroperoxide is nearly racemic | Zea mays | ? | - |
? | |
2-linoleoyl-sn-glycero-3-phosphorylcholine + O2 | the wild-type ZmLOX produces predominantly (13S)-hydroperoxide. In contrast, the A562G mutant produces excessively (9S)-hydroperoxide. The oxidation of 2-linoleoyl-sn-glycero-3-phosphorylcholine exhibits the limited regio- and stereospecificity. But the A562G mutant form possesses lesser regio- and stereospecificity | Zea mays | ? | - |
? | |
linoleate + O2 | - |
Zea mays | (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate | - |
? | |
linoleate + O2 | - |
Zea mays | (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate | - |
? | |
linoleate + O2 | - |
Zea mays | (9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate | - |
? | |
monolinolenoylglycerol + O2 | isolated from flax leaves, both the wild-type ZmLOX and A562G mutant dioxygenate monolinolenoylglycerol. Both oxidize the monolinolenoylglycerol predominantly into (9S)-hydroperoxide. The A562G mutation does not affect the relative yield of 13-hydroperoxide, but increases the proportion of (13R)-enantiomer | Zea mays | ? | - |
? | |
monolinolenoylglycerol + O2 | wild-type enzyme and mutant A562G predominantly produce (9S)-hydroperoxide | Zea mays | ? | - |
? | |
additional information | 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 | ? | - |
? | |
additional information | 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 | ? | - |
? | |
phosphorylcholine + O2 | activity with the wild-type enzyme, no activity with mutant A562G | Zea mays | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
9-lipoxygenase | - |
Zea mays |
9-LOX | - |
Zea mays |
LOX | - |
Zea mays |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Zea mays |
General Information | Comment | Organism |
---|---|---|
additional information | 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 | Zea mays |