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alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxy-8,12,15-octadecatrienoate
i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
oleate + O2
8-hydroperoxy-9(Z)-octadecenoic acid
-
low activity
-
-
?
palmitoleate + O2
8-hydroperoxy-9(Z)-hexadecenoic acid
-
low activity
-
-
?
additional information
?
-
alpha-linolenate + O2

(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
moderate activity
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
moderate activity
-
-
?
linoleate + O2

(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
the enzyme is involved in biosynthesis of oxylipins
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
abstraction of the pro-S hydrogen at C-8 and antarafacial dioxygenation at C-10 with double bond migration
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
i.e. (9Z,12Z)-octadeca-9,12-dienoate. The enzyme is involved in biosynthesis of oxylipins, which affect sporulation, development, and pathogenicity of Aspergilli
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
i.e. (9Z,12Z)-octadeca-9,12-dienoate. The wild-type enzyme forms 90% (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate, 10% (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate and small amounts of 12S(13R)-epoxy-(10R)-hydroxy-(8E)-octadecenoic acid
-
-
?
linoleate + O2

(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
best substrate
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
-
?
additional information

?
-
recombinant enzyme lacks hydroperoxide isomerase activity, but shows low epoxyalcohol synthase activity with biosynthesis of a novel oxylipin, 12S(13R)-epoxy-(10R)-hydroxy-18:1. The enzyme oxygenates 20:4n-6 (all-cis-5,8,11,14-eicosatetraenoic acid) i.e. by hydrogen abstraction at both C-13 and C-10 with formation of two nonconjugated and four cis-trans-conjugated hydroperoxyeicosatetraenoic acid
-
-
?
additional information
?
-
-
recombinant enzyme lacks hydroperoxide isomerase activity, but shows low epoxyalcohol synthase activity with biosynthesis of a novel oxylipin, 12S(13R)-epoxy-(10R)-hydroxy-18:1. The enzyme oxygenates 20:4n-6 (all-cis-5,8,11,14-eicosatetraenoic acid) i.e. by hydrogen abstraction at both C-13 and C-10 with formation of two nonconjugated and four cis-trans-conjugated hydroperoxyeicosatetraenoic acid
-
-
?
additional information
?
-
-
the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
-
-
?
additional information
?
-
-
assay method optimization for the recombinant enzyme exprssed in Escherichia coli, overview
-
-
?
additional information
?
-
-
the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
-
-
?
additional information
?
-
-
assay method optimization for the recombinant enzyme exprssed in Escherichia coli, overview
-
-
?
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alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
additional information
?
-
alpha-linolenate + O2

(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
-
?
linoleate + O2

(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
the enzyme is involved in biosynthesis of oxylipins
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
i.e. (9Z,12Z)-octadeca-9,12-dienoate. The enzyme is involved in biosynthesis of oxylipins, which affect sporulation, development, and pathogenicity of Aspergilli
-
-
?
linoleate + O2

(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
-
?
additional information

?
-
-
the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
-
-
?
additional information
?
-
-
the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
-
-
?
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L306A
the relative biosynthesis of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate compared to (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate is slightly lowered
L306V
the relative biosynthesis of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate compared to (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate is slightly lowered
L384A
the relative amount of (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate (8-HODE/(10-HODE + 8-HODE)) is 10.4% for the recombinant wild-type enzyme and 53.7% for the mutant enzyme. The L384A mutant changes the stereochemistry at C-8 and C-10. L384A forms the R and S enantiomers of 8-HODE and 10-HODE in a ratio of 3:2, whereas native and recombinant 10R-DOX form both products with 95% R configuration
L384F
increases the relative biosynthesis of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate compared to (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate to 48% (the wild-type enzyme forms 90% (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate and 10% (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate)
L384M
increases the relative biosynthesis of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate compared to (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate with 3-4% units
L384V
the relative amount of (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate (8-HODE/(10-HODE + 8-HODE)) is 10.4% for the recombinant wild-type enzyme and 22.1% for the mutant enzyme
V388F
the wild-type enzyme forms 90% (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate and 10% (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate. The mutation increases the formation of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to 36%
V388L
the wild-type enzyme forms 90% (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate and 10% (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate. The mutation increases the formation of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to 16%
additional information

-
under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization, optimization of concentrations of cells and substrate, pH and temperature, for the production of 10R-hydroxy unsaturated fatty acids, overview. Recombinant enzyme PpoC in Escherichia coli cells is more stable than the purified recombinant PpoC
additional information
-
under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization, optimization of concentrations of cells and substrate, pH and temperature, for the production of 10R-hydroxy unsaturated fatty acids, overview. Recombinant enzyme PpoC in Escherichia coli cells is more stable than the purified recombinant PpoC
-
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synthesis

-
under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization
synthesis
-
under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization
-
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Garscha, U.; Oliw, E.H.
Leucine/valine residues direct oxygenation of linoleic acid by (10R)- and (8R)-dioxygenases: expression and site-directed mutagenesis oF (10R)-dioxygenase with epoxyalcohol synthase activity
J. Biol. Chem.
284
13755-13765
2009
Aspergillus fumigatus (Q4WY82), Aspergillus fumigatus
brenda
Jernerén, F.; Garscha, U.; Hoffmann, I.; Hamberg, M.; Oliw, E.H.
Reaction mechanism of 5,8-linoleate diol synthase, 10R-dioxygenase, and 8,11-hydroperoxide isomerase of Aspergillus clavatus
Biochim. Biophys. Acta
1801
503-507
2010
Aspergillus clavatus (Q4W941), Aspergillus clavatus
brenda
Han, J.E.; Seo, M.J.; Shin, K.C.; Oh, D.K.
Production of 10R-hydroxy unsaturated fatty acids from hempseed oil hydrolyzate by recombinant Escherichia coli cells expressing PpoC from Aspergillus nidulans
Appl. Microbiol. Biotechnol.
100
7933-7944
2016
Aspergillus nidulans, Aspergillus nidulans ATCC 10074
brenda