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Information on EC 1.14.18.4 - phosphatidylcholine 12-monooxygenase
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1.14.18.4 phosphatidylcholine 12-monooxygenaseIUBMB Comments
The enzyme, characterized from the plant Ricinus communis (castor bean), is involved in production of the 12-hydroxylated fatty acid ricinoleate. The enzyme, which shares sequence similarity with fatty-acyl desaturases, requires a cytochrome b5 as the electron donor.
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Word Map
- 1.14.18.4
- triacylglycerols
- ricinus
- communis
- bean
-
desaturase
- purpurea
-
claviceps
- phospholipase
- fendleri
-
oilseed
- linoleate
- lesquerella
-
seed-specific
-
desaturation
-
lesquerolic
- synthesis
-
petrochemical
-
18-carbon
-
condensing
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
fah12, oleoyl-12-hydroxylase, cpfah, cpfah12, oleate 12-hydroxylase, oleate hydroxylase, lfah12, oleate delta12-hydroxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
castor DELTA12-hydroxylase
EC 1.14.13.26
-
-
formerly
-
FAH12
oleate 12-hydroxylase
oleate DELTA12-hydroxylase
oxygenase, oleate DELTA12-mono
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-
-
-
ricinoleic acid synthase
-
-
-
-
oleate DELTA12-hydroxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + 2 ferrocytochrome b5 + O2 + 2 H+ = a 1-acyl-2-[(12R)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + 2 ferricytochrome b5 + H2O
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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,
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SYSTEMATIC NAME
IUBMB Comments
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine,ferrocytochrome-b5:oxygen oxidoreductase (12-hydroxylating)
The enzyme, characterized from the plant Ricinus communis (castor bean), is involved in production of the 12-hydroxylated fatty acid ricinoleate. The enzyme, which shares sequence similarity with fatty-acyl desaturases, requires a cytochrome b5 as the electron donor.
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CAS REGISTRY NUMBER
COMMENTARY
77950-95-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2
1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + ferricytochrome b5
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2
1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
a 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + 2 ferrocytochrome b5 + O2 + 2 H+
a 1-acyl-2-ricinoleoyl-sn-glycero-3-phosphocholine + 2 ferricytochrome b5 + H2O
-
-
-
-
?
a 1-acyl-2-oleoyl-sn-glycero-3-phosphoethanolamine + 2 ferrocytochrome b5 + O2 + 2 H+
a 1-acyl-2-ricinoleoyl-sn-glycero-3-phosphoethanolamine + 2 ferricytochrome b5 + H2O
-
-
-
-
?
cis-linoleic acid + reduced acceptor + O2
densipolic acid + acceptor + H2O
-
-
-
?
eicosenoic acid + reduced acceptor + O2
lesquerolic acid + acceptor + H2O
-
-
-
?
linoleic acid + ferrocytochrome P-450 + O2
linolenic acid + ferricytochrome P-450 + H2O
-
-
-
-
?
oleic acid + 2 ferrocytochrome b5 + O2 + 2 H+
ricinoleic acid + 2 ferricytochrome b5 + H2O
oleic acid esterified to membrane lipid phosphatidylcholine + reduced acceptor + H+ + O2
hydroxy fatty acids in triacylglycerol + acceptor + H2O
D2CPE1
-
-
-
?
palmitoleate + ferrocytochrome P-450 + H+ + O2
12-hydroxypalmitoleate + ferricytochrome P-450 + H2O
-
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2
1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + ferricytochrome b5
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2
1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + ferricytochrome b5
-
-
-
?
cis-oleic acid + reduced acceptor + O2
ricinoleic acid + acceptor + H2O
-
-
-
?
cis-oleic acid + reduced acceptor + O2
ricinoleic acid + acceptor + H2O
-
-
-
?
cis-oleic acid + reduced acceptor + O2
ricinoleic acid + acceptor + H2O
-
-
-
?
cis-oleic acid + reduced acceptor + O2
ricinoleic acid + acceptor + H2O
Ricinus communis OLE-1
-
-
-
?
oleate + ferrocytochrome P-450 + H+ + O2
12-hydroxy-oleate + ferricytochrome P-450 + H2O
-
-
-
-
?
oleate + ferrocytochrome P-450 + H+ + O2
12-hydroxy-oleate + ferricytochrome P-450 + H2O
the enzyme is primarily a fatty acid hydroxylase, rather than a bifunctional oleate 12-hydroxylase-desaturase, involved in ricinoleic acid biosynthesis, overview
-
-
?
oleate + ferrocytochrome P-450 + H+ + O2
12-hydroxy-oleate + ferricytochrome P-450 + H2O
the enzyme is primarily a fatty acid hydroxylase rather than a bifunctional oleate 12-hydroxylase-desaturase, overview
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-
?
oleic acid + 2 ferrocytochrome b5 + O2 + 2 H+
ricinoleic acid + 2 ferricytochrome b5 + H2O
-
-
-
?
oleic acid + 2 ferrocytochrome b5 + O2 + 2 H+
ricinoleic acid + 2 ferricytochrome b5 + H2O
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i.e. 12-hydroxy-octadeca-cis-9-enoic acid
-
?
additional information
?
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-
biosynthesis of ricinoleic acid in Claviceps purpurea is catalyzed by the fungal desaturase-like hydroxylase
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-
?
additional information
?
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the enzyme acts predominantly as a hydroxylase, introducing hydroxyl groups at the 12-position of oleic acid and palmitoleic acid. It also shows DELTA12 desaturase activities on 16C and 18C monounsaturated fatty acids and, to a much lesser extent, omega3 desaturase activities on ricinoleic acid, overview
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-
?
additional information
?
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in Lesquerella fendleri ricinoleic acid is efficiently elongated to lesquerolic acid in a reaction catalyzed by a condensing enzyme specific to hydroxy fatty acids
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-
?
additional information
?
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the activitiy of oleoyl-12-hydroxylase seems unaffected by the fatty acid at the sn-1 position of 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine. 1-acyl-2-ricinoleoyl-sn-glycero-3-phosphocholine is formed mostly by the hydroxylation of 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine, not from the incorporation of ricinoleate into 1-acyl-2-ricinoleoyl-sn-glycero-3-phosphocholine, and 1-acyl-2-oleoyl-sn-glycero-3-phosphoethanolamine is less actively formed than 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2
1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + ferricytochrome b5
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2
1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + ferricytochrome b5 + H2O
-
-
-
-
?
oleate + ferrocytochrome P-450 + H+ + O2
12-hydroxy-oleate + ferricytochrome P-450 + H2O
the enzyme is primarily a fatty acid hydroxylase, rather than a bifunctional oleate 12-hydroxylase-desaturase, involved in ricinoleic acid biosynthesis, overview
-
-
?
oleic acid esterified to membrane lipid phosphatidylcholine + reduced acceptor + H+ + O2
hydroxy fatty acids in triacylglycerol + acceptor + H2O
D2CPE1
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2
1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + ferricytochrome b5
-
-
-
?
1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + ferrocytochrome b5 + O2
1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + ferricytochrome b5
-
-
-
?
cis-oleic acid + reduced acceptor + O2
ricinoleic acid + acceptor + H2O
-
-
-
?
cis-oleic acid + reduced acceptor + O2
ricinoleic acid + acceptor + H2O
-
-
-
?
cis-oleic acid + reduced acceptor + O2
ricinoleic acid + acceptor + H2O
Ricinus communis OLE-1
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-
-
?
additional information
?
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-
biosynthesis of ricinoleic acid in Claviceps purpurea is catalyzed by the fungal desaturase-like hydroxylase
-
-
?
additional information
?
-
in Lesquerella fendleri ricinoleic acid is efficiently elongated to lesquerolic acid in a reaction catalyzed by a condensing enzyme specific to hydroxy fatty acids
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Ricinus communis OLE-1
wild-type and OLE-1 mutant strain i.e. high-oleic castor mutant
SwissProt
brenda
wild-type and OLE-1 mutant strain i.e. high-oleic castor mutant
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
fatty acid profiles during the development of wild-type castor bean seeds and OLE-1 mutant seeds, overview
brenda
Ricinus communis OLE-1
-
fatty acid profiles during the development of wild-type castor bean seeds and OLE-1 mutant seeds, overview
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
an integral membrane protein, proposed topological model, overview
brenda
Ricinus communis OLE-1
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an integral membrane protein, proposed topological model, overview
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
common castor bean seed lipids contain high levels of palmitic and linoleic acid in the initial stages of development. As development proceeds, the ricinoleic acid content constitutes up to 80% of the total fatty acids in mature seeds of the wild-type. In the high-oleic mutant seed, embryos mostly accumulate palmitic, oleic and linoleic in the first stages of development, which is followed by an important accumulation of oleic acid during seed maturation. The ricinoleic acid content remains low in these seeds throughout development
physiological function
Ricinus communis OLE-1
-
common castor bean seed lipids contain high levels of palmitic and linoleic acid in the initial stages of development. As development proceeds, the ricinoleic acid content constitutes up to 80% of the total fatty acids in mature seeds of the wild-type. In the high-oleic mutant seed, embryos mostly accumulate palmitic, oleic and linoleic in the first stages of development, which is followed by an important accumulation of oleic acid during seed maturation. The ricinoleic acid content remains low in these seeds throughout development
-
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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). FAH12_RICCO
387
5
44435
Swiss-Prot
Chloroplast (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
topology predictions for the castor DELTA12-hydroxylase. The RcFAH12 sequence is divided into nine consecutive domains from I through to IX: domain I is the cytosolic N-terminal region, domain II is two transmembrane helices (TM1 and TM2) connected by a short ER luminal loop, domain III is a short cytosolic loop containing the first histidine box that is involved in the catalytic site, domain IV is the first peripheral membrane-associated segment (PMS1), domain V is the second short cytosolic loop containing the second histidine box, domain VI is the second peripheral membrane-associated region (PMS2), domain VII is the third short cytosolic loop, domain VIII is the second group of transmembrane helices (TM3 and TM4) that are connected by a short ER luminal loop, and domain IX is the cytosolic C terminus containing the third histidine motif
additional information
-
topology predictions for the castor DELTA12-hydroxylase. The RcFAH12 sequence is divided into nine consecutive domains from I through to IX: domain I is the cytosolic N-terminal region, domain II is two transmembrane helices (TM1 and TM2) connected by a short ER luminal loop, domain III is a short cytosolic loop containing the first histidine box that is involved in the catalytic site, domain IV is the first peripheral membrane-associated segment (PMS1), domain V is the second short cytosolic loop containing the second histidine box, domain VI is the second peripheral membrane-associated region (PMS2), domain VII is the third short cytosolic loop, domain VIII is the second group of transmembrane helices (TM3 and TM4) that are connected by a short ER luminal loop, and domain IX is the cytosolic C terminus containing the third histidine motif
additional information
Ricinus communis OLE-1
-
topology predictions for the castor DELTA12-hydroxylase. The RcFAH12 sequence is divided into nine consecutive domains from I through to IX: domain I is the cytosolic N-terminal region, domain II is two transmembrane helices (TM1 and TM2) connected by a short ER luminal loop, domain III is a short cytosolic loop containing the first histidine box that is involved in the catalytic site, domain IV is the first peripheral membrane-associated segment (PMS1), domain V is the second short cytosolic loop containing the second histidine box, domain VI is the second peripheral membrane-associated region (PMS2), domain VII is the third short cytosolic loop, domain VIII is the second group of transmembrane helices (TM3 and TM4) that are connected by a short ER luminal loop, and domain IX is the cytosolic C terminus containing the third histidine motif
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
M295L
site-directed mutagenesis, expression of the mutant FAH12gene in yeast does not result in any obvious changes in the ratio of hydroxy and diunsaturated fatty acids accumulating
F49S/V242A/H319Q
additional information
F49S/V242A/H319Q
naturally occuring mutation in the OLE-1 mutant strain i.e. high-oleic castor mutant. Residue F49 is located in domain I, residue V242 in transmembrane domain TM3, and residue H319 in the His box III or domain IX, respectively, In the high-oleic mutant seed, embryos mostly accumulate palmitic, oleic and linoleic in the first stages of development, which is followed by an important accumulation of oleic acid during seed maturation. The ricinoleic acid content remains low in these seeds throughout development, in contrast to the wild-type seeds. Comparison of fatty acid profiles of seeds. The mutant displays a phenotype similar to the control cells that are transformed with the empty pYES2 plasmid. Structural effect of the mutations, overview
F49S/V242A/H319Q
Ricinus communis OLE-1
-
naturally occuring mutation in the OLE-1 mutant strain i.e. high-oleic castor mutant. Residue F49 is located in domain I, residue V242 in transmembrane domain TM3, and residue H319 in the His box III or domain IX, respectively, In the high-oleic mutant seed, embryos mostly accumulate palmitic, oleic and linoleic in the first stages of development, which is followed by an important accumulation of oleic acid during seed maturation. The ricinoleic acid content remains low in these seeds throughout development, in contrast to the wild-type seeds. Comparison of fatty acid profiles of seeds. The mutant displays a phenotype similar to the control cells that are transformed with the empty pYES2 plasmid. Structural effect of the mutations, overview
-
additional information
optimization of the recombinant enzyme from gene FAH12 overexpression in Schizosaccharomyces pombe, overview. The enzyme product is toxic for the yeast cells. Gene plg7, encoding phospholipase A2, acts as a multicopy suppressor restoring the growth defect by removing ricinoleic acid from phospholipids and inducing secretion of a part of the released free ricinoleic acid into culture media. Overexpression of Schizosaccharomyces pombe triglyceride (TG) lipase encoded by gene ptl2, but not the expression of the TG lipases encodd by ptl1 and ptl3, suppresses the growth defect induced by ricinoleic acid production, and the culture grown at 20°C secretes free ricinoleic acid into media like plg7 overexpression. Suppression by ptl2 is independent of plg7, and a large amount of free ricinoleic acid is accumulated in the cells concomitant with the decrease in ricinoleic acid moieties in phospholipids. The suppression by ptl2 is attenuated by bromoenol lactone (BEL), a phospholipase A2 specific inhibitor, suggesting that Ptl2p may have phospholipase activity. Simultaneous overexpression of ptl2 and plg7 in the FAH12 integrant increases secretion and intracellular accumulation of ricinoleic acid 1.2 and 1.3fold, respectively, compared to those with single overexpression of plg7 on day 10 at 20°C. Method optimization and evaluation, overview
additional information
-
optimization of the recombinant enzyme from gene FAH12 overexpression in Schizosaccharomyces pombe, overview. The enzyme product is toxic for the yeast cells. Gene plg7, encoding phospholipase A2, acts as a multicopy suppressor restoring the growth defect by removing ricinoleic acid from phospholipids and inducing secretion of a part of the released free ricinoleic acid into culture media. Overexpression of Schizosaccharomyces pombe triglyceride (TG) lipase encoded by gene ptl2, but not the expression of the TG lipases encodd by ptl1 and ptl3, suppresses the growth defect induced by ricinoleic acid production, and the culture grown at 20°C secretes free ricinoleic acid into media like plg7 overexpression. Suppression by ptl2 is independent of plg7, and a large amount of free ricinoleic acid is accumulated in the cells concomitant with the decrease in ricinoleic acid moieties in phospholipids. The suppression by ptl2 is attenuated by bromoenol lactone (BEL), a phospholipase A2 specific inhibitor, suggesting that Ptl2p may have phospholipase activity. Simultaneous overexpression of ptl2 and plg7 in the FAH12 integrant increases secretion and intracellular accumulation of ricinoleic acid 1.2 and 1.3fold, respectively, compared to those with single overexpression of plg7 on day 10 at 20°C. Method optimization and evaluation, overview
additional information
D2CPE1
fusion enzyme of castor bean oleate 12-hydroxylase and tobacco cytochrome b5
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Arabidopsis thaliana
FAH gene, unrooted phylogenetic analysis, functional expression in Saccharomyces cerevisiae, expression in transgenic Arabidopsis thaliana plants under control of a seed-specific promoter
-
gene FAH12, recombinant overexpression in Schizosaccharomyces pombe strain ARC010-1, RT-PCR enzyme expression analysis. The enzyme product is toxic for the cells. Gene plg7, encoding phospholipase A2, acts as a multicopy suppressor restoring the growth defect by removing ricinoleic acid from phospholipids and inducing secretion of a part of the released free ricinoleic acid into culture media
gene FAH12, subcloning in Escherichia coli strain DH5alpha, expression in Saccharomyces cerevisiae results in the synthesis of ricinoleic acid and very low levels of di-unsaturated fatty acids. Expression of LlinFAH12 in Arabidopsis thaliana seeds results in hydroxy fatty acid accumulation, fatty acid composition in transformed compared to wild-type plants, overview
gene RcFAH12, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative real-time PCR enzyme expression analysis, recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain W303-1A, fatty acid analysis
PCR-amplification, plant transformation by heat shock transformation of Agrobacterium tumefaciens (GV3101) with vector, expression in EMS mutant or T-DNA insertion lines of Arabidopsis thaliana deficient in the production of the enzymes diacylglycerol acyltransferase-1 (DGAT1), phospholipid: diacylglycerol acyltransferase-1 (PDAT1) and the homologue of PDAT1 phospholipid: diacylglycerol acyltransferase-2 (PDAT2)
D2CPE1
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
CpFAH, thet D12 oleate hydroxylase of nonplant origin, is a good candidate for the transgenic production of hydroxyl fatty acids in oilseed crops
synthesis
-
at the normal growth temperature of 30°C, Schizosaccharomyces pombe cells harboring FAH12 expression vector grow poorly when the FAH12 gene expression is induced. At 37°C, there is almost no growth inhibition. After preliminary growth at 37°C followed by a 5-day incubation at 20°C , the level of ricinoleic acid reaches 137.4 microg/ml of culture which corresponds to 52.6% of total fatty acids
synthesis
coexpression of fatty acid hydroxylase FAH and diacylglycerol acyl transferase DGAT1 in Pichia pastoris produces higher lipid contents and ricinoleic acid levels than expression of FAH alone. Coexpression in a mutant haploid strain defective in the DELTA12 desaturase activity results in a higher level of ricinoleic acid than that in the diploid strain. The ricinoleic acid produced is mainly distributed in the neutral lipid fractions, particularly the free fatty acid form, but with little in the polar lipids
synthesis
-
overexpression of multicopy suppressor Plg7, encoding phospholipase A2, in combinantion with oleate DELTA12-hydroxylase gene FAH12 enables Schizosaccharomyces pombe cells to secrete free ricinoleic acid into culture media. The FAH12 integrant in the absence of the overexpressed plg7 reaches 200 microg/ml of intracellular ricinoleic acid and only 69.3 microg/ml in culture media. The FAH12 integrant harboring the plg7 multicopy plasmid secretes ricinoleic acid in the media (184.5 microg/ml) without decreasing the amount in the cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moreau, R.A.; Stumpf, P.K.
Recent studies of the enzymic synthesis of ricinoleic acid by developing castor beans
Plant Physiol.
67
672-676
1981
Ricinus communis
brenda
Van de Loo, F.J.; Broun, P.; Turner, S.; Somerville, C.
An oleate 12-hydroxylase from Ricinus communis L. is a fatty acyl desaturase homolog
Proc. Natl. Acad. Sci. USA
92
6743-6747
1995
Ricinus communis
brenda
Broun, P.; Boddupalli, S.; Somerville, C.
A bifunctional oleate 12-hydroxylase: desaturase from Lesquerella fendleri
Plant J.
13
201-210
1998
Physaria fendleri (O81094), Physaria fendleri
brenda
Lin, J.T.; McKeon, T.A.; Goodrich-Tanrikulu, M.; Stafford, A.E.
Characterization of oleoyl-12-hydroxylase in castor microsomes using the putative substrate, 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine
Lipids
31
571-577
1996
Ricinus communis
brenda
Richards, D.E.; Taylor, R.D.; Murphy, D.J.
Localization and possible substrate requirement of the oleate 12-hydroxylase of developing Ricinus communis seeds
Plant Physiol. Biochem.
31
89-94
1993
Ricinus communis
-
brenda
Smith, M.A.; Moon, H.; Chowrira, G.; Kunst, L.
Heterologous expression of a fatty acid hydroxylase gene in developing seeds of Arabidopsis thaliana
Planta
217
507-516
2003
Physaria fendleri (O81094), Ricinus communis (Q41131), Ricinus communis
brenda
Meesapyodsuk, D.; Qiu, X.
An oleate hydroxylase from the fungus Claviceps purpurea: cloning, functional analysis, and expression in Arabidopsis
Plant Physiol.
147
1325-1333
2008
Claviceps purpurea
brenda
Dauk, M.; Lam, P.; Kunst, L.; Smith, M.A.
A FAD2 homologue from Lesquerella lindheimeri has predominantly fatty acid hydroxylase activity
Plant Sci.
173
43-49
2007
Physaria lindheimeri (A5HB93)
brenda
Dauk, M.; Lam, P.; Smith, M.
The role of diacylglycerol acyltransferase-1 and phospholipid: diacylglycerol acyltransferase-1 and -2 in the incorporation of hydroxy fatty acids into triacylglycerol in Arabidopsis thaliana expressing a castor bean oleate 12-hydroxylase gene
Botany
87
552-560
2009
Ricinus communis (D2CPE1)
-
brenda
Holic, R.; Yazawa, H.; Kumagai, H.; Uemura, H.
Engineered high content of ricinoleic acid in fission yeast Schizosaccharomyces pombe
Appl. Microbiol. Biotechnol.
95
179-187
2012
Claviceps purpurea
brenda
Yazawa, H.; Kumagai, H.; Uemura, H.
Secretory production of ricinoleic acid in fission yeast Schizosaccharomyces pombe
Appl. Microbiol. Biotechnol.
97
8663-8671
2013
Claviceps purpurea
brenda
Meesapyodsuk, D.; Chen, Y.; Ng, S.H.; Chen, J.; Qiu, X.
Metabolic engineering of Pichia pastoris to produce ricinoleic acid, a hydroxy fatty acid of industrial importance
J. Lipid Res.
56
2102-2109
2015
Claviceps purpurea (B4YQU1), Claviceps purpurea
brenda
Lin, J.T.; Chen, J.M.; Chen, P.; Liao, L.P.; McKeon, T.A.
Molecular species of PC and PE formed during castor oil biosynthesis
Lipids
37
991-995
2002
Ricinus communis
brenda
Yazawa, H.; Ogiso, M.; Kumagai, H.; Uemura, H.
Suppression of ricinoleic acid toxicity by ptl2 overexpression in fission yeast Schizosaccharomyces pombe
Appl. Microbiol. Biotechnol.
98
9325-9337
2014
Claviceps purpurea (B4YQU1), Claviceps purpurea
brenda
Venegas-Caleron, M.; Sanchez, R.; Salas, J.J.; Garces, R.; Martinez-Force, E.
Molecular and biochemical characterization of the OLE-1 high-oleic castor seed (Ricinus communis L.) mutant
Planta
244
245-258
2016
Ricinus communis (Q41131), Ricinus communis, Ricinus communis OLE-1 (Q41131)
brenda
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Release 2023.1 (January 2023)
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