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
5.3.3.13
-
RECOMMENDED NAME
GeneOntology No.
polyenoic fatty acid isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(5Z,8Z,11Z,14Z,17Z)-icosapentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate
show the reaction diagram
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-
-
-
(5Z,8Z,11Z,14Z,17Z)-icosapentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate
show the reaction diagram
regio- and stereochemistry of the isomerization reaction, mechanism
-
(5Z,8Z,11Z,14Z,17Z)-icosapentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate
show the reaction diagram
mechansim of hydrogen transfers in the isomerization reaction including a diene intermediate
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
isomerization
-
-
-
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
eicosapentaenoate cis-DELTA5,8,11,14,17-eicosapentaenoate cis-DELTA5-trans-DELTA7,9-cis-D14,17 isomerase
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-
-
-
PFI
-
-
-
-
polyunsaturated fatty acid double bond isomerase
-
-
polyunsaturated fatty acid double bond isomerase
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-
polyunsaturated fatty acid isomerase
-
-
PUFA double bond isomerases
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-
CAS REGISTRY NUMBER
COMMENTARY
159002-84-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
; Oregon red marine alga
-
-
Manually annotated by BRENDA team
; temperate red alga from the Oregon coast
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
arachidonate, next best substrate after (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate, the C11 olefinic position becomes protonated by a solvent-derived proton, mechanism
-
-
?
(5Z,8Z,11Z,14Z)-eicosatetraenoate
(5Z,7E,9E,14Z)-eicosatetraenoate
show the reaction diagram
-
arachidonic acid
-
-
?
(5Z,8Z,11Z,14Z)-eicosatetraenoate
?
show the reaction diagram
Q8W257
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
-
anandamide
-
-
?
(5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-ethanolamide
(5Z,7E,9E,14Z)-eicosatetraenoyl-N-ethanolamide
show the reaction diagram
-
anandamide
conjugated triene anandamide, cannabimimetic substance
-
?
(5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-ethanolamide
(5Z,7E,9E,14Z)-eicosatetraenoyl-N-ethanolamide
show the reaction diagram
-
anandamide
termed CTA, i.e. conjugated triene anandamide, cannabimimetic substance
-
?
(5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-ethanolamide
(5Z,7E,9E,14Z)-eicosatetraenoyl-N-ethanolamide
show the reaction diagram
-
arachidonylethanolamide
-
-
?
(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
-
-
-
-
?
(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, best substrate, likely the native substrate, mechanism
-
-
?
(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate
(5Z,7E,9E,14Z,17Z)-eicosapentaenoate
show the reaction diagram
Q8W257
the preferred substrates are highly unsaturated free fatty acids such as eicosapentaenoic acid
-
-
?
(6Z,9Z,12Z)-octadecatrienoate
(6Z,8E,10E)-octadecatrienoate
show the reaction diagram
-
gamma-linolenate, PFI intramolecularly transfers the bis-allylic pro-S hydrogen from the C11 position to the C13 position, the bis-allylic pro-R hydrogen at C8 in gamma-linolenate is lost to the solvent
-
-
?
(6Z,9Z,12Z)-octadecatrienoate
(6Z,8E,10E)-octadecatrienoate
show the reaction diagram
-
gamma-linolenic acid
-
-
?
(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
-
alpha-linolenate, one-fifth as fast as gamma-linolenate
-
-
?
(9Z,12Z,15Z)-octadecatrienoate
?
show the reaction diagram
-
alpha-linolenic acid
-
-
?
linoleic acid
?
show the reaction diagram
-
-
-
-
?
linoleic acid methyl ester
(10E,12Z)-octadeca-10,12-dienoic acid methyl ester
show the reaction diagram
-
-
-
-
?
polyenoic fatty acid
?
show the reaction diagram
Q8W257
PFI catalyzes the isomerization of a wide range of substrates containing three or more methylene interrupted olefins into a Z,E,E conjugated triene functionality
-
-
?
polyenoic fatty acid
?
show the reaction diagram
-
PFI is capable of isomerizing the methylene interrupted olefins of a wide range of polyenoic fatty acids into a conjugated triene functionality
-
-
?
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
-
-
?
linoleoyl-CoA
(10Z,12Z)-octadeca-10,12-dienoyl-CoA
show the reaction diagram
-
-
-
-
?
additional information
?
-
Q8W257
PFI may be part of a stress tolerance mechanism
-
-
-
additional information
?
-
-
not: linoleic acid
-
-
-
additional information
?
-
-
substrate binding site, PFI preferentially orients the substrate in the catalytic site with respect to the methyl terminus and likely reacts, preferentially, with the protonated form of the substrate, not: linoleic acid
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
flavin
Q8W257
bound to PFI, cDNA contains a flavin-binding motif near the mature N-terminus
additional information
-
no requirement for molecular oxygen
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INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by EDTA, o-phenanthroline, acetylsalicylic acid, baicalein, dipyridamole, eicosatetraynoic acid, esculetin, indomethacin, naproxen, NDGA or SKF-525A
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0019
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(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexenoate
-
pH 7, 22C
0.0528
-
(5Z,8Z,11Z)-eicosatrienoate
-
pH 7, 22C
0.0255
-
(5Z,8Z,11Z,14Z)-eicosatetraenoate
-
pH 7, 22C
0.0399
-
(5Z,8Z,11Z,14Z)-eicosatetraenoate
-
pH 7.2
0.0152
-
(5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-ethanolamide
-
pH 9, 22C
0.0175
-
(5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-ethanolamide
-
pH 7, 22C
0.0096
-
(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate
-
pH 7, 22C
0.0328
-
(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate
-
pH 7.2
0.15
-
(6Z,9Z,12Z)-octadecatrienoate
-
pH 7.2
0.15
-
(6Z,9Z,12Z)-octadecatrienoate
-
-
0.017
-
(7Z,10Z,13Z,16Z)-docosatetraenoate
-
pH 7, 22C
0.00482
-
linoleic acid
-
wild-type PAI
0.02577
-
linoleic acid
-
mutant R88S/F193A
0.03794
-
linoleic acid
-
mutant F193A
0.0657
-
linoleic acid
-
mutant R88S
additional information
-
additional information
-
study of the effect of the pH on kinetic parameters with several substrates
-
additional information
-
additional information
-
[11,11-2H2] linoleic acid, 0.00228, wild-type PAI; (11S-2H) linoleic acid, 0.00408, wild-type PAI
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
11.6
-
(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate
-
assuming one catalytic site per enzyme molecule
41
-
(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate
-
pH 7.2, assuming one catalytic site per enzyme molecule
0.16
-
linoleic acid
-
mutant R88S/F193A
0.33
-
linoleic acid
-
mutant F193A
2.93
-
linoleic acid
-
mutant R88S
4.37
-
linoleic acid
-
wild-type PAI
additional information
-
additional information
-
[11,11-2H2] linoleic acid, 0.83, wild-type PAI; (11S-2H) linoleic acid, 3.51, wild-type PAI
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.06
3.5
-
pH 7.2, arachidonate as substrate
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
below
6.5
-
-
assay at
7.2
-
Q8W257
assay at
7.5
-
-
activity and kinetic assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at
22
-
Q8W257
assay at
25
-
-
kinetic assay
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
isoelectric focusing
4.9
-
Q8W257
sequence calculation including the signal peptide; sequence calculation without the signal peptide
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
125000
-
Q8W257
sedimentation equilibrium utracentrifugation
174000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 61000, SDS-PAGE
homodimer
Q8W257
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 ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
Q8W257
native PFI is N-glycosylated
proteolytic modification
Q8W257
translation of a preprotein containing a signal peptide of 21 amino acids that is removed during maturation
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
10
-
PFI is relatively stable at these pH extremes
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, purified PFI, months, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
into the vector pGEX-6P-1 for expression in Escherichia coli cells
-
cDNA, expression in Arabidopsis thaliana
Q8W257
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
F168G/G169F
-
inactive mutant
F168L
-
inactive mutant
R88A
-
inactive mutant
R88S/F193A
-
mutant