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
-
1.13.11.45
-
oxylipins
-
graminis
-
bis-allylic
-
gaeumannomyces
-
suprafacial
-
take-all
-
antarafacial
-
atlox2
-
lipoxygenation
-
hydroperoxy
- 1.13.11.45
- oxylipins
- graminis
-
bis-allylic
-
gaeumannomyces
-
suprafacial
-
take-all
-
antarafacial
-
atlox2
-
lipoxygenation
-
hydroperoxy
Reaction
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
Advanced search results
Engineering
Engineering on EC 1.13.11.45 - linoleate 11-lipoxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
G316A
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
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
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
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
catalytically active, 7-8% of hydroperoxide isomerase activity
G316A
-
site-directed mutagenesis, the mutant changes the the position of lipoxygenation toward the carboxyl group of 20:2n-6 and 20:3n-3 and prevents the bis-allylic hydroperoxide of 20:3n-3 but not of 20:2n-6to interact with the catalytic metall
G316A
-
site-directed mutagenesis, the mutant MnIII-LO G316A oxygenates mainly 16:3n-3 at positions n-7 and n-6, 19:3n-3 at n-10, n-8, and n-6, and 20:3n-3 at n-10 and n-8
N466L
-
site-directed mutagenesis, the mutation hardly affects the bis-allylic hydroperoxide rearrangement
-
replacement of a single amino acid in the active site of LOXs can alter the product profile
additional information
-
V602 deletion mutant, no enzymic activity, loss of more than 95% of manganese content
additional information
-
hydrophobic replacements of Leu336 can modify the hydroperoxide configurations at C-9 with little effect on the R configuration at C-13 of the 18:2n-6 and 18:3n-3 metabolites
additional information
-
replacement Phe347 in 13R-MnLOX and changes the regiospecific oxidation of 18:2 n-6 in a consistent way, but the n-3 double bond of 18:3n-3 can reduce this effect. Mutations are designed to convert the pentamer motif to a hexamer motif to mimic FeLOX, but the mutants with the His-Val-Leu-Phe-Thr-His and His-Val-Leu-Phe-Gly-His motives are inactive, overview
additional information
modulating the cavity volume around the pentadiene system of linoleic acid shifts the product formation towards 9S-, 9R-, 13S- or 13R-hydroperoxides in correlation with the site of mutation, thus decreasing the amount of the bis-allylic 11R-hydroperoxide