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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
alpha-linolenate + O2
10-hydroperoxy-(6Z,8E,12Z)-octadecatrienoate + 12(13)epoxy-10-hydroxy-(8E,15Z)-octadecadienoate
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
oleate + O2
8-H(P)OME + 10-H(P)OME
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
-
-
?
alpha-linolenate + O2

10-hydroperoxy-(6Z,8E,12Z)-octadecatrienoate + 12(13)epoxy-10-hydroxy-(8E,15Z)-octadecadienoate
-
-
-
?
alpha-linolenate + O2
10-hydroperoxy-(6Z,8E,12Z)-octadecatrienoate + 12(13)epoxy-10-hydroxy-(8E,15Z)-octadecadienoate
-
-
-
?
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-hydroperoxy-8,12-octadecadienoate
-
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
-
?
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
-
-
-
-
?
oleate + O2

8-H(P)OME + 10-H(P)OME
-
-
-
?
oleate + O2
8-H(P)OME + 10-H(P)OME
-
-
-
?
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-hydroperoxy-8,12-octadecadienoate
-
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
-
?
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Jernern, 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
Oliw, E.H.
Linoleate diol synthase related enzymes of the human pathogens Histoplasma capsulatum and Blastomyces dermatitidis
Arch. Biochem. Biophys.
696
108669
2020
Blastomyces dermatitidis
brenda
Oliw, E.; Hamberg, M.
An allene oxide and 12-oxophytodienoic acid are key intermediates in jasmonic acid biosynthesis by Fusarium oxysporum
J. Lipid Res.
58
1670-1680
2017
Fusarium oxysporum (F9FAJ9), Fusarium oxysporum, Fusarium oxysporum Fo5176 (F9FAJ9)
brenda