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1.13.11.45: linoleate 11-lipoxygenase

This is an abbreviated version!
For detailed information about linoleate 11-lipoxygenase, go to the full flat file.

Word Map on EC 1.13.11.45

Reaction

linoleate
+
O2
=
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate

Synonyms

13 R -MnLOX, 13R-MnLOX, Cg-MnLOX, CspLOX2, Fo-MnLOX, linoleate dioxygenase, lipoxygenase 2, LOX-1, manganese lipoxygenase, manganese LOX, MGG_08499, Mn-LO, Mn-LOX, MnLOX, Mo-MnLOX

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.45 linoleate 11-lipoxygenase

Engineering

Engineering on EC 1.13.11.45 - linoleate 11-lipoxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L530R
-
site-directed mutagenesis
S348F
-
site-directed mutagenesis, the mutant enzyme shows altered reaction stereospecificity compared to the wild-type enzyme
F337I
-
site-directed mutagenesis, replacement of Phe337 with Ile changes the stereochemistry of the 13-hydroperoxy metabolites of 18:2n-6 and 18:3n-3 (from 100% R to 69-74% S) with little effect on regiospecificity. The abstraction of the pro-S hydrogen of 18:2n-6 is retained, suggesting antarafacial hydrogen abstraction and oxygenation. The mutant shows highly reduced activity compared to the wild-type enzyme
F347A
-
site-directed mutagenesis, the mutant oxidizes octadeca-9,11-dienoic acid to 11-hydroperoxyoctadecadienoate/(13R)-hydroperoxyoctadecadienoate/(9S)-hydroperoxyoctadecadienoate in an initial ratio of 50/42/8 and with almost complete consumption of 11-hydroperoxyoctadecadienoate to a ratio of 2/84/14. The (9E,11Z,15E)-octadeca-9,11,15-trienoic acid is transformed to 11- and (13R)-hydroperoxyoctadecatrienoic acid and to traces of (9S)-hydroperoxyoctadecatrienoic acid, essentially as native 13R-MnLOX
F347L
-
site-directed mutagenesis, (9E,11Z,15E)-octadeca-9,11,15-trienoic acid is oxidized to a 2:3 mixture of (9S)- and (13R)-dihydroxyoctadecatrienoic acid
F347V
-
site-directed mutagenesis
G316A
G316T
catalytically inactive
G316V
catalytically inactive
G332A
-
site-directed mutagenesis, replacement of Gly332 with the larger hydrophobic residue selectively augments dehydration of (9Z,11E,13R,15Z)-13-hydroperoxyoctadeca-9,12,15-trienoic acid and increases the oxidation at C-13 of 18:1n-6
H274Q
-
no enzymic activity, loss of more than 95% of manganese content
H278E
-
no enzymic activity, loss of more than 95% of manganese content
H462E
-
no enzymic activity, loss of more than 95% of manganese content
H463Q
-
no significant change in activity
K52N
-
site-directed mutagenesis
L176K
-
site-directed mutagenesis
L336A
-
site-directed mutagenesis, replacement of Leu336 with the smaller hydrophobic residue shifts the oxygenation from C-13 toward C-9 with formation of 9S- and 9R-hydroperoxy metabolites of 18:2n-6 and 18:3n-3, the mutant shows highly reduced activity compared to the wild-type enzyme
L336F
-
site-directed mutagenesis, replacement of Leu336 with the larger hydrophobic residue selectively augments dehydration of (9Z,11E,13R,15Z)-13-hydroperoxyoctadeca-9,12,15-trienoic acid and increases the oxidation at C-13 of 18:1n-6, the mutant shows highly reduced activity compared to the wild-type enzyme
L336G
-
site-directed mutagenesis, replacement of Leu336 with the smaller hydrophobic residue shifts the oxygenation from C-13 toward C-9 with formation of 9S- and 9R-hydroperoxy metabolites of 18:2n-6 and 18:3n-3, the mutant shows highly reduced activity compared to the wild-type enzyme
L336V
-
site-directed mutagenesis, replacement of Leu336 with the smaller hydrophobic residue shifts the oxygenation from C-13 toward C-9 with formation of 9S- and 9R-hydroperoxy metabolites of 18:2n-6 and 18:3n-3, the mutant shows highly reduced activity compared to the wild-type enzyme
N466L
N466Q
-
no significant change in activity
Q467N
-
no significant change in activity
S469A
-
site-directed mutagenesis, the mutation hardly affects the bis-allylic hydroperoxide rearrangement, the mutant shows the same substrate profile as the wild-type enzyme
Y158C
-
site-directed mutagenesis
A300G
site-directed mutagenesis, structure comparison with wild-type enzyme, enantioselectivity towards formation of 9R- and 13S-hydroperoxyoctadeca-9,12-dienoate is increased compared to the wild-type enzyme
I296A
site-directed mutagenesis, structure comparison with wild-type enzyme, the stereospecificity of the mutant activity is inverted compared to the wild-type enzyme
L258V
site-directed mutagenesis, structure comparison with wild-type enzyme, the mutation only slightly affects the enzyme activity
L502V
site-directed mutagenesis, structure comparison with wild-type enzyme, enantioselectivity towards formation of 9R- and 13S-hydroperoxyoctadeca-9,12-dienoate is increased compared to the wild-type enzyme
L506V
site-directed mutagenesis, structure comparison with wild-type enzyme, the stereospecificity of the mutant activity is inverted compared to the wild-type enzyme
additional information