Any feedback?
No. of entries
Information on EC 1.13.11.61 - linolenate 9R-lipoxygenase
for references in articles please use BRENDA:EC1.13.11.61
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
1.13.11 With incorporation of two atoms of oxygen
1.13.11.61 linolenate 9R-lipoxygenase
IUBMB Comments
In cyanobacteria the enzyme is involved in oxylipin biosynthesis. The enzyme also converts linoleate to (9R,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.13.11.61
-
linoleic
- diol
- ala
-
dioxygenation
- lipoxygenases
-
polyunsaturated
- nostoc
-
cyanobacterial
-
regio
- hydroperoxides
-
aspergilli
-
homolytic
-
allene
- terreus
-
stereochemistry
Reaction Schemes
showSynonyms
9r-lox, 9r-lipoxygenase, linoleate 9r-dioxygenase, (9r)-lox, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(9R)-LOX
9R-lipoxygenase
9R-LOX
NspLOX
NspLOX
-
NspLOX C-terminal portion exhibits activity as a inoleate 9R-lipoxygenase
NspLOX
-
NspLOX C-terminal portion exhibits activity as a inoleate 9R-lipoxygenase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-linolenate + O2 = (9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate
-
-
-
-
alpha-linolenate + O2 = (9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate
the LOX reaction is always catalyzed at a 1Z,4Z-pentadiene system of a polyunsaturated fatty acid. In the initial step, a hydrogen atom is abstracted from the central bis-allylic methylene group by the non-heme iron or in few cases manganese in the active site. During this rate-limiting step, Fe(III) is reduced to Fe(II) in the former case and a substrate radical is formed which rapidly delocalizes over the five carbon unit. Addition of dioxygen yields a peroxyl radical, which is finally reduced to the hydroperoxide product
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
acylceramide biosynthesis and processing
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
alpha-linolenate:oxygen (9R)-oxidoreductase
In cyanobacteria the enzyme is involved in oxylipin biosynthesis. The enzyme also converts linoleate to (9R,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-linolenic acid + O2
(9Z,12E,15Z)-9R-hydroxy-9,12,15-octadecatrienoic acid
-
Substrates: -
Products: -
Products: -
?
gamma-linolenic acid + O2
(6Z,10E,12Z)-9R-hydroxy-6,10,12-octadecatrienoic acid
-
Substrates: -
Products: -
Products: -
?
linoleic acid + O2
(10E,12Z)-9R-hydroxy-10,12-octadecadienoic acid
-
Substrates: -
Products: -
Products: -
?
alpha-linolenate + O2
(9R,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
Substrates: i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
Products: -
Products: -
?
alpha-linolenate + O2
(9R,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
Substrates: i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
Products: -
Products: -
?
alpha-linolenate + O2
(9R,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
Substrates: i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate. Preferred substrate
Products: -
Products: -
?
alpha-linolenate + O2
(9R,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
Substrates: i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
Products: -
Products: -
?
alpha-linolenate + O2
(9R,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
Substrates: i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate. Preferred substrate
Products: -
Products: -
?
alpha-linolenate + O2
(9R,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
Substrates: i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
Products: -
Products: -
?
alpha-linolenic acid + O2
(9R,10E,12Z,15Z)-9-hydroxy-10,12,15-octadecatrienoic acid
-
Substrates: -
Products: -
Products: -
?
alpha-linolenic acid + O2
(9R,10E,12Z,15Z)-9-hydroxy-10,12,15-octadecatrienoic acid
-
Substrates: -
Products: -
Products: -
?
alpha-linolenic acid + O2
(9R,10E,12Z,15Z)-9-hydroxy-octadeca-10,12,15-trienoic acid
-
Substrates: optimal reaction conditions are pH 8.5, 15Ā°C, 5% v/v acetone, 0.2% w/v Tween 80, 40 g/l alpha-linolenic acid, and 1 g/l enzyme, assay method optimization
Products: -
Products: -
?
alpha-linolenic acid + O2
(9R,10E,12Z,15Z)-9-hydroxy-octadeca-10,12,15-trienoic acid
-
Substrates: optimal reaction conditions are pH 8.5, 15Ā°C, 5% v/v acetone, 0.2% w/v Tween 80, 40 g/l alpha-linolenic acid, and 1 g/l enzyme, assay method optimization
Products: -
Products: -
?
gamma-linolenic acid + O2
(6Z,9R,10E,12Z)-9-hydroxy-octadeca-6,10,12-trienoic acid
-
Substrates: -
Products: -
Products: -
?
gamma-linolenic acid + O2
(6Z,9R,10E,12Z)-9-hydroxy-octadeca-6,10,12-trienoic acid
-
Substrates: -
Products: -
Products: -
?
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: i.e. (9Z,12Z)-octadeca-9,12-dienoate. (9R,10EZ,12Z)-9-Hydroperoxy-10,12-octadecadienoate is formed by antarafacial hydrogen abstraction and oxygenation
Products: -
Products: -
?
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: i.e. (9Z,12Z)-octadeca-9,12-dienoate
Products: configuration of the 9-hydroperoxide is primarily R (93%). (13S)-Hydroperoxy octadecadienoic acid is detected in small amounts as by-product
Products: configuration of the 9-hydroperoxide is primarily R (93%). (13S)-Hydroperoxy octadecadienoic acid is detected in small amounts as by-product
?
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: the enzyme is involved in oxylipin biosyntesis
Products: -
Products: -
?
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: i.e. (9Z,12Z)-octadeca-9,12-dienoate, the C-terminal portion of NspLOX is identified as a linoleate linoleate (9R)-lipoxygenase. 42% of the activity with alpha-linolenic acid
Products: -
Products: -
?
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: the enzyme is involved in oxylipin biosyntesis
Products: -
Products: -
?
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: i.e. (9Z,12Z)-octadeca-9,12-dienoate, the C-terminal portion of NspLOX is identified as a linoleate linoleate (9R)-lipoxygenase. 42% of the activity with alpha-linolenic acid
Products: -
Products: -
?
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: i.e. (9Z,12Z)-octadeca-9,12-dienoate
Products: configuration of the 9-hydroperoxide is primarily R (93%). (13S)-Hydroperoxy octadecadienoic acid is detected in small amounts as by-product
Products: configuration of the 9-hydroperoxide is primarily R (93%). (13S)-Hydroperoxy octadecadienoic acid is detected in small amounts as by-product
?
linoleate + O2
(9Z,11R,12Z)-11-hydroperoxyoctadeca-9,12-dienoate
-
Substrates: -
Products: -
Products: -
?
linoleate + O2
(9Z,11R,12Z)-11-hydroperoxyoctadeca-9,12-dienoate
-
Substrates: analysis of substrate conformation and environment, overview
Products: -
Products: -
?
linoleic acid + O2
(9R,10E,12Z)-9-hydroxy-octadeca-10,12-dienoic acid
-
Substrates: -
Products: -
Products: -
?
linoleic acid + O2
(9R,10E,12Z)-9-hydroxy-octadeca-10,12-dienoic acid
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: selective production of 9R-hydroxy-10E,12Z,15Z-octadecatrienoic acid from alpha-linolenic acid in Perilla seed oil hydrolyzate by the enzyme from Nostoc sp. strain SAG 25.82, heterologously expressed in Escherichia coli. The specific activity of the enzyme followed the descending order linoleic acid > alpha-linolenic acid > gamma-linolenic acid. Product determination by LC-MS/MS analysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: selective production of 9R-hydroxy-10E,12Z,15Z-octadecatrienoic acid from alpha-linolenic acid in Perilla seed oil hydrolyzate by the enzyme from Nostoc sp. strain SAG 25.82, heterologously expressed in Escherichia coli. The specific activity of the enzyme followed the descending order linoleic acid > alpha-linolenic acid > gamma-linolenic acid. Product determination by LC-MS/MS analysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: CspLOX1 only produces conjugated hydroperoxyoctadeca-9,12-dienoate in a way that it imitates CspLOX2 and forms 11-hydroperoxyoctadeca-9,12-dienoate
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
linoleate + O2
(9Z,11R,12Z)-11-hydroperoxyoctadeca-9,12-dienoate
-
Substrates: -
Products: -
Products: -
?
alpha-linolenate + O2
(9R,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
Substrates: i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
Products: -
Products: -
?
alpha-linolenate + O2
(9R,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
Substrates: i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
Products: -
Products: -
?
alpha-linolenic acid + O2
(9R,10E,12Z,15Z)-9-hydroxy-10,12,15-octadecatrienoic acid
-
Substrates: -
Products: -
Products: -
?
alpha-linolenic acid + O2
(9R,10E,12Z,15Z)-9-hydroxy-10,12,15-octadecatrienoic acid
-
Substrates: -
Products: -
Products: -
?
gamma-linolenic acid + O2
(6Z,9R,10E,12Z)-9-hydroxy-octadeca-6,10,12-trienoic acid
-
Substrates: -
Products: -
Products: -
?
gamma-linolenic acid + O2
(6Z,9R,10E,12Z)-9-hydroxy-octadeca-6,10,12-trienoic acid
-
Substrates: -
Products: -
Products: -
?
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: the enzyme is involved in oxylipin biosyntesis
Products: -
Products: -
?
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: the enzyme is involved in oxylipin biosyntesis
Products: -
Products: -
?
linoleic acid + O2
(9R,10E,12Z)-9-hydroxy-octadeca-10,12-dienoic acid
-
Substrates: -
Products: -
Products: -
?
linoleic acid + O2
(9R,10E,12Z)-9-hydroxy-octadeca-10,12-dienoic acid
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18.4
5.4
6.3
18.4
-
native enzyme, with linoleic acid as substrate, at pH 7.0 and 25Ā°C
5.4
-
native enzyme, with gamma-linolenic acid as substrate, at pH 7.0 and 25Ā°C
6.3
-
native enzyme, with alpha-linolenic acid as substrate, at pH 7.0 and 25Ā°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
structure-activity analysis, overview. Crucial residues in the direct environment of the narrow active site that form a clamp-like structure include Tyr360, Gly401 Ile617, Ile379, Leu405, and Leu621. Molecular dynamics simulations support a major role of steric shielding of active site clamp. Structure-activity analysis, modeling, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LILIP_NOSS1
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
773
0
87860
Swiss-Prot
-
A0A2G9HN56_9LAMI
747
3
83344
TrEMBL
other Location (Reliability: 4)
A0A8J7DB11_9CYAN
385
0
43794
TrEMBL
-
A0A2G9I1B0_9LAMI
869
5
96952
TrEMBL
other Location (Reliability: 5)
A0A8J7D5Y9_9CYAN
430
0
48376
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotrimer
homotrimer
-
3 * 52000, recombinant His-tagged enzyme, SDS-PAGE, 3 * 52300, about, sequence calculation
homotrimer
-
3 * 52000, recombinant His-tagged enzyme, SDS-PAGE, 3 * 52300, about, sequence calculation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type enzyme CspLOX2, sitting drop vapor diffusion method, from well solution of 10% PEG 4000, 0.1 M MES/imidazole pH 6.5, 20% glycerol and 0.02% alcohols (1,6-hexanediol, 1-butanol, 1,2-propanediol, 2-propanol, 1,4-butanediol, and 1,3-propanediol), 10 days, purified recombinant CspLOX2 mutant enzymes by hanging drop vapour diffusion method, from well solution of 12.5-15 PEG 4000, 8-12% glycerol, 0.1 M MES/imidazole pH 6.1, and 0-600 mM NaCl, X-ray diffraction structure determination and analysis at 1.8 A resolution. Crystals of a CspLOX2 substrate complex are not obtained
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A162G
-
the recombinant carboxy-terminal domain of the wild-type enzyme and of mutant enzyme A162G produce primarily (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate from linoleate. The stereochemistry of the hydroperoxide is almost exclusively R (93-94%)
A162I
-
the recombinant carboxy-terminal domain of the mutant enzyme A162I produces almost exlusively (13S)-hydroperoxy octadecadienoic acid (90%)
A162V
-
the recombinant carboxy-terminal domain of the mutant enzyme A162V converts linoleate primarily to (13S)-hydroperoxy octadecadienoic acid (64%) and to a lesser extent to (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate (36%)
A162G
-
the recombinant carboxy-terminal domain of the wild-type enzyme and of mutant enzyme A162G produce primarily (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate from linoleate. The stereochemistry of the hydroperoxide is almost exclusively R (93-94%)
-
A162I
-
the recombinant carboxy-terminal domain of the mutant enzyme A162I produces almost exlusively (13S)-hydroperoxy octadecadienoic acid (90%)
-
A162V
-
the recombinant carboxy-terminal domain of the mutant enzyme A162V converts linoleate primarily to (13S)-hydroperoxy octadecadienoic acid (64%) and to a lesser extent to (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate (36%)
-
G401A
-
site-directed mutagenesis, the mutaant shows increased formation of 11-hydroperoxyoctadeca-9,12-dienoate compared to the wild-type enzyme
I617L
-
site-directed mutagenesis, the mutaant shows increased formation of 11-hydroperoxyoctadeca-9,12-dienoate compared to the wild-type enzyme
additional information
-
Decreasing the channel size of a 9R-lipoxygenase (CspLOX1) can in turn induce formation of the bis-allylic 11R-hydroperoxide
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-Trap column chromatography and Superdex 200 gel filtration
-
recombinant carboxy-terminal domain is purified after expression in Escherichia coli
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 Star by nickel affinity chromatography, gel filtration, and ultrafiltration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of separate domains of NspLOX and the entire protein in Escherichia coli
-
recombinant carboxy-terminal domain is purified after expression in Escherichia coli
-
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Star
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lang, I.; Goebel, C.; Porzel, A.; Heilmann, I.; Feussner, I.
A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120
Biochem. J.
410
347-357
2008
Nostoc sp., Nostoc sp. PCC 7120
brenda
Jernerén, F.; Hoffmann, I.; Oliw, E.H.
Linoleate 9R-dioxygenase and allene oxide synthase activities of Aspergillus terreus
Arch. Biochem. Biophys.
495
67-73
2010
Aspergillus terreus
brenda
Andreou, A.Z.; Vanko, M.; Bezakova, L.; Feussner, I.
Properties of a mini 9R-lipoxygenase from Nostoc sp. PCC 7120 and its mutant forms
Phytochemistry
69
1832-1837
2008
Nostoc sp., Nostoc sp. PCC 7120
brenda
Kim, K.R.; An, J.U.; Lee, S.H.; Oh, D.K.
Selective production of 9R-hydroxy-10E,12Z,15Z-octadecatrienoic acid from alpha-linolenic acid in Perilla seed oil hydrolyzate by a lipoxygenase from Nostoc sp. SAG 25.82
PLoS ONE
10
e0137785
2015
Nostoc sp., Nostoc sp. SAG 25.82
brenda
Newie, J.; Neumann, P.; Werner, M.; Mata, R.A.; Ficner, R.; Feussner, I.
Lipoxygenase 2 from Cyanothece sp. controls dioxygen insertion by steric shielding and substrate fixation
Sci. Rep.
7
2069
2017
Rippkaea orientalis PCC 8801
brenda
Kim, S.; Kim, T.; Kim, M.; Oh, D.
Production of 11R-hydroxyeicosatetraenoic acid from arachidonic acid by Escherichia coli cells expressing arachidonate 11R-lipoxygenase from Nostoc sp.
J. Am. Oil Chem. Soc.
2021
1-9
2021
Nostoc sp. PCC 7120 = FACHB-418
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.13.11.61)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
