1.13.11.B6: linoleate 9/13-lipoxygenase
This is an abbreviated version!
For detailed information about linoleate 9/13-lipoxygenase, go to the full flat file.
Word Map on EC 1.13.11.B6
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1.13.11.B6
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jasmonate
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polyunsaturated
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epoxy
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cucumber
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magnaporthe
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apple
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lipoxygenases
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hydroperoxidation
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9s-hpode
- 1.13.11.B6
- jasmonate
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polyunsaturated
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epoxy
- cucumber
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magnaporthe
- apple
- lipoxygenases
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hydroperoxidation
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9s-hpode
Reaction
Synonyms
13/9 lipoxygenase, 13/9-LOX, 9-/13-LOXN2, 9-lipoxygenase, 9-LOX, 9/13-lipoxygenase, 9/13-LOX, Ca-LOC-1, dual positional specific LOX, linoleate 9 S-lipoxygenase, linoleate oxygen oxidoreductase, linolenate 9R-dioxygenase, lipoxygenase, LOX, lox1-St-2, LOX1-Zm1, LOX1:Md:1a, LOX1a, LOX2:Md:2a, LOX2a, manganese 9S-lipoxygenase, MoLOX1, OsLOX1, PnLOX1, S-LOX
ECTree
Advanced search results
Engineering
Engineering on EC 1.13.11.B6 - linoleate 9/13-lipoxygenase
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G567A
I578L
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis
R268A
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis
V582F
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis
Q599F
the wild-type enzyme is a linoleate 13-LOX above pH 7.5, below this value it functions as a linoleate 9-LOX. The mutant loses its 13-LOX activity at higher pH-values. At pH-values above 7.5 a rather unspecific product pattern (1:1 ratio of 13-hydroperoxy-(10E,12Z)-octadecadienoate and 9-hydroperoxy-(10E,12Z)-octadecadienoate) is observed with the mutant enzyme. The unspecific oxygenation reaction is also indicated by the R/S-ratio (4:6) of the major reaction products
Q599H
the mutation converts the enzyme to a linoleate 13-LOX lacking any pH sensitivity. The pH optimum remains unaffected, and the major product isomers are in the S-configuration
L350M
F580A
I437L
KM-value for linoleate is 114% of wild-type value, kcat/Km for linoleate is 83% of wild-type value. Positional specificity 13-hydroperoxy-(10E,12Z)-octadecadienoate/9-hydroperoxy-(10E,12Z)-octadecadienoate is 0.7 (compared to 0.8 in reaction with wild-type enzyme)
V570I
KM-value for linoleate is 61% of wild-type value, kcat/Km for linoleate is 367% of wild-type value. Positional specificity 13-hydroperoxy-(10E,12Z)-octadecadienoate/9-hydroperoxy-(10E,12Z)-octadecadienoate is 0.6 (compared to 0.8 in reaction with wild-type enzyme)
V580F
KM-value for linoleate is 384% of wild-type value, kcat/Km for linoleate is 4% of wild-type value. Positional specificity 13-hydroperoxy-(10E,12Z)-octadecadienoate/9-hydroperoxy-(10E,12Z)-octadecadienoate is 0.9 (compared to 0.8 in reaction with wild-type enzyme)
A562G
additional information
site-directed mutagenesis, the mutant converts the dual positional specific LOX1:Md:1a to an enzyme with a high specificity for 9(S)-hydroperoxide formation
G567A
site-directed mutagenesis, the mutant converts the dual positional specific LOX1:Md:1a to an enzyme with a high specificity for 9(S)-hydroperoxide formation, mutant substrate specificity compared to the wild-type enzyme, chiral analysis
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site-directed mutagenesis, the mutant shows increased specificity for 13S-lipoxygenation, EC 1.13.11.12, altered substrate specificity/regiospecific activity, overview
L350M
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site-directed mutagenesis, the mutant shows increased specificity for 13S-lipoxygenation, EC 1.13.11.12, altered substrate specificity/regiospecific activity, overview
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site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
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
mutants Arg268Ala, Gly567Ala, Ile578Leu and Val582Phe show high substrate conversion rates of linoleate, linolenate and arachidonate (60%-100% of wild-type LOX1:Md:1a activity with linoleate). Substrate specificity of mutants, overview
additional information
mutants Arg268Ala, Gly567Ala, Ile578Leu and Val582Phe show high substrate conversion rates of linoleate, linolenate and arachidonate (60%-100% of wild-type LOX1:Md:1a activity with linoleate). Substrate specificity of mutants, overview
additional information
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mutants Arg268Ala, Gly567Ala, Ile578Leu and Val582Phe show high substrate conversion rates of linoleate, linolenate and arachidonate (60%-100% of wild-type LOX1:Md:1a activity with linoleate). Substrate specificity of mutants, overview
additional information
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replacement Leu350 in 9S-MnLOX and changes the regiospecific oxidation of 18:2 n-6 in a consistent way, but the n-3 double bond of 18:3 n-3 can reduce this effect
additional information
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replacement Leu350 in 9S-MnLOX and changes the regiospecific oxidation of 18:2 n-6 in a consistent way, but the n-3 double bond of 18:3 n-3 can reduce this effect
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