Information on EC 2.1.1.15 - fatty-acid O-methyltransferase

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

EC NUMBER
COMMENTARY hide
2.1.1.15
-
RECOMMENDED NAME
GeneOntology No.
fatty-acid O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a fatty acid = S-adenosyl-L-homocysteine + a fatty acid methyl ester
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:fatty-acid O-methyltransferase
Oleic acid is the most effective fatty acid acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
37256-89-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxydecanoic acid + S-adenosyl-L-methionine
methyl 3-hydroxydecanoate + S-adenosyl-L-homocysteine
show the reaction diagram
3-hydroxydodecanoic acid + S-adenosyl-L-methionine
methyl 3-hydroxydodecanoate + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
-
?
3-hydroxyoctanoic acid + S-adenosyl-L-methionine
methyl 3-hydroxyoctanoate + S-adenosyl-L-homocysteine
show the reaction diagram
decanoic acid + S-adenosyl-L-methionine
methyl decanoate + S-adenosyl-L-homocysteine
show the reaction diagram
dodecanoic acid + S-adenosyl-L-methionine
methyl dodecanoate + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
-
?
octanoic acid + S-adenosyl-L-methionine
methyl octanoate + S-adenosyl-L-homocysteine
show the reaction diagram
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
show the reaction diagram
S-adenosyl-L-methionine + abietic acid
S-adenosyl-L-homocysteine + methyl abietate
show the reaction diagram
S-adenosyl-L-methionine + oleic acid
S-adenosyl-L-homocysteine + oleic acid methyl ester
show the reaction diagram
-
oleic acid is the most effective fatty acid acceptor, traces of activity with phosphatidylethanolamine and phosphatidylglycerol
-
?
S-adenosyl-L-methionine + palmitic acid
S-adenosyl-L-homocysteine + methyl palmitate
show the reaction diagram
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
show the reaction diagram
-
-
-
?
additional information
?
-
-
traces of activity with methionine, serine and S-adenosylethinonine as methyl donor
-
-
-
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
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-(6-aminohexyl)-5-chloro-1-naphthalene-sulfonamide
-
W7, very strong inhibition
S-adenosylhomocysteine
Trifluoperazine
-
very strong inhibition
unsaturated fatty acids
-
-
-
additional information
-
Ca2+, EGTA and calmodulin have no effect
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.099 - 1.03
3-hydroxydecanoic acid
-
0.129
3-hydroxydodecanoic acid
-
pH 7.8, 37C
-
0.196 - 2.039
3-hydroxyoctanoic acid
0.0082 - 0.046
Decanoic acid
0.103
dodecanoic acid
-
pH 7.8, 37C
0.077 - 5.24
Octanoic acid
1.3
oleic acid
-
-
0.0255
S-adenosyl-L-methionine
wild-type, pH 7.8, 37C
0.025
S-adenosylmethionine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.042 - 1600
3-hydroxydecanoic acid
-
1346
3-hydroxydodecanoic acid
Mycobacterium marinum
-
pH 7.8, 37C
-
0.488 - 358
3-hydroxyoctanoic acid
0.244 - 489
Decanoic acid
1165
dodecanoic acid
Mycobacterium marinum
-
pH 7.8, 37C
0.147 - 510
Octanoic acid
0.598
S-adenosyl-L-methionine
Mycobacterium marinum
B2HHT4
wild-type, pH 7.8, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0031 - 16100
3-hydroxydecanoic acid
42166
10400
3-hydroxydodecanoic acid
Mycobacterium marinum
-
pH 7.8, 37C
42167
0.239 - 1820
3-hydroxyoctanoic acid
26050
29.76 - 10600
Decanoic acid
2551
11300
dodecanoic acid
Mycobacterium marinum
-
pH 7.8, 37C
2019
0.0014 - 6600
Octanoic acid
1649
0.824 - 23.45
S-adenosyl-L-methionine
24
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000018
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
membrane
Manually annotated by BRENDA team
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the cocrystal structure of with S-adenosyl-L-homocysteine and octanoate shows that the substrate-binding site is largely localized within the alpha-helical domain that caps the Rossmann-like fold domain. Aliphatic and aromatic residues encircle the acyl chain of the fatty acid substrate, including Trp155, Met214, Phe222, Tyr224, Val256, Phe311, and Leu316. In the cocrystal structure with 3-hydroxydecanoate, only the S enantiomer is bound in the active site
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
20% loss of activity within 5 min
100
-
90% loss of activity within 10 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+)
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)(pLysS)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q154A
17fold increaseof the KM with octanoate as a substrate, and 5fold increase of the KM for 3-hydroxydecanoate
Q31A
complete loss of activtiy
W155F
near 1000fold decrease in catalytic efficiency
Y24F
30fold decrease in catalytic efficiency
Q154A
-
17fold increaseof the KM with octanoate as a substrate, and 5fold increase of the KM for 3-hydroxydecanoate
-
Q31A
-
complete loss of activtiy
-
W155F
-
near 1000fold decrease in catalytic efficiency
-
Y24F
-
30fold decrease in catalytic efficiency
-