Information on EC 5.3.3.13 - polyenoic fatty acid isomerase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
5.3.3.13
-
RECOMMENDED NAME
GeneOntology No.
polyenoic fatty acid isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(5Z,8Z,11Z,14Z,17Z)-icosapentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
SYSTEMATIC NAME
IUBMB Comments
(5Z,8Z,11Z,14Z,17Z)-icosapentaenoate DELTA8,11-DELTA7,9-isomerase (trans-double-bond-forming)
The enzyme from the red alga Ptilota filicina catalyses the isomerization of skip dienes (methylene-interrupted double bonds) in a broad range of fatty acids and fatty-acid analogues, such as arachidonate and gamma-linolenate, to yield a conjugated triene.
CAS REGISTRY NUMBER
COMMENTARY hide
159002-84-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexenoate
(4Z,7Z,9E,11E,16Z,19Z)-docosahexenoate
show the reaction diagram
-
excellent substrate
-
-
?
(5Z,8Z,11Z)-eicosatrienoate
?
show the reaction diagram
-
-
-
-
?
(5Z,8Z,11Z,14Z)-eicosatetraenoate
(5Z,7E,9E,14Z)-eicosatetraenoate
show the reaction diagram
(5Z,8Z,11Z,14Z)-eicosatetraenoate
?
show the reaction diagram
arachidonic acid, conversion to the conjugated triene
-
-
?
(5Z,8Z,11Z,14Z)-eicosatetraenoyl methyl ester
(5Z,7E,9E,14Z,17Z)-eicosapentaenoyl methyl ester
show the reaction diagram
-
methyl ester of arachidonate
-
-
?
(5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-ethanolamide
(5Z,7E,9E,14Z)-eicosatetraenoyl-N-ethanolamide
show the reaction diagram
(5Z,8Z,11Z,14Z,17Z)-eicosa-5,8,11,14,17-pentaenoic acid
(5Z,7Z,9Z,14Z,17Z)-eicosa-5,7,9,14,17-pentaenoic acid
show the reaction diagram
-
-
-
-
?
(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate
(5Z,7E,9E,14Z,17Z)-eicosapentaenoate
show the reaction diagram
(6Z,9Z,12Z)-octadecatrienoate
(6Z,8E,10E)-octadecatrienoate
show the reaction diagram
(7Z,10Z,13Z,16Z)-docosatetraenoate
?
show the reaction diagram
-
adrenic acid
-
-
?
(8Z,11Z,14Z)-eicosatrienoate
?
show the reaction diagram
-
dihomo-gamma-linolenic acid, formation of two products: a conjugated triene and a conjugated diene
-
-
?
(9Z,12Z,15Z)-octadecatrienoate
?
show the reaction diagram
linoleic acid
?
show the reaction diagram
-
-
-
-
?
linoleic acid methyl ester
(10E,12Z)-octadeca-10,12-dienoic acid methyl ester
show the reaction diagram
-
-
-
-
?
linoleoyl-CoA
(10Z,12Z)-octadeca-10,12-dienoyl-CoA
show the reaction diagram
-
-
-
-
?
polyenoic fatty acid
?
show the reaction diagram
polyunstaurated fatty acid
?
show the reaction diagram
-
PFI catalyzes the formation of conjugated trienes from a variety of polyunsaturated fatty acid precursors, regio- and stereochemistry, enzyme may recognize the protonated from of the substrate
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate
(5Z,7E,9E,14Z,17Z)-eicosapentaenoate
show the reaction diagram
-
likely the native substrate, biosynthesis of conjugated triene-containing fatty acids
-
-
?
additional information
?
-
Q8W257
PFI may be part of a stress tolerance mechanism
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
additional information
-
no requirement for molecular oxygen
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
not inhibited by EDTA, o-phenanthroline, acetylsalicylic acid, baicalein, dipyridamole, eicosatetraynoic acid, esculetin, indomethacin, naproxen, NDGA or SKF-525A
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019
(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexenoate
-
pH 7, 22C
0.0528
(5Z,8Z,11Z)-eicosatrienoate
-
pH 7, 22C
0.0255 - 0.0399
(5Z,8Z,11Z,14Z)-eicosatetraenoate
0.0152 - 0.0175
(5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-ethanolamide
0.0096 - 0.0328
(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate
0.15
(6Z,9Z,12Z)-octadecatrienoate
0.017
(7Z,10Z,13Z,16Z)-docosatetraenoate
-
pH 7, 22C
0.00482 - 0.0657
linoleic acid
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.6 - 41
(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate
0.16 - 4.37
linoleic acid
additional information
additional information
Propionibacterium acnes
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[11,11-2H2] linoleic acid, 0.83, wild-type PAI; (11S-2H) linoleic acid, 3.51, wild-type PAI
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.06 - 3.5
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pH 7.2, arachidonate as substrate
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
assay at
7.5
-
activity and kinetic assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
-
there is a 30% increase in rate of product formation from pH 8 to 6.5, from pH 6.5 to 4.5 the apparent velocity increases 2.4fold, below pH 4 the activity slowly decreases
additional information
-
pH-dependence profile of PFI, catalytically active over a wide pH-range with (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate as substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
kinetic assay
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
isoelectric focusing
4.9
sequence calculation including the signal peptide; sequence calculation without the signal peptide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
125000
sedimentation equilibrium utracentrifugation
174000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 61000, SDS-PAGE
homodimer
2 * 61000, SDS-PAGE, 2 * 55900, sequence calculation including the signal peptide, 2 * 53600, sequence calculation without the signal peptide
trimer
-
3 * 61000, SDS-PAGE, 3 * 58119, mass spectrometry
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
native PFI is N-glycosylated
proteolytic modification
translation of a preprotein containing a signal peptide of 21 amino acids that is removed during maturation
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
PFI is relatively stable at these pH extremes
649078
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, purified PFI, months, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA, expression in Arabidopsis thaliana
into the vector pGEX-6P-1 for expression in Escherichia coli cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F168G/G169F
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inactive mutant
F168L
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inactive mutant
R88A
-
inactive mutant
R88S/F193A
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mutant