Literature summary for 1.13.11.B6 extracted from

Chechetkin, I.R.; Osipova, E.V.; Antsygina, L.L.; Gogolev, Y.V.; Grechkin, A.N.
Oxidation of glycerolipids by maize 9-lipoxygenase and its A562G mutant (2011), Chem. Phys. Lipids, 164, 216-220.

Search for more literature for 1.13.11.B6

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta(DE3)pLysS	Zea mays

Protein Variants

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/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Zea mays	-	-	-
Zea mays	Q9AXG8	-	-

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
9-lipoxygenase	-	Zea mays
9-LOX	-	Zea mays
LOX	-	Zea mays

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	-	Zea mays

General Information

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)