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Information on EC 2.1.1.15 - fatty-acid O-methyltransferase
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EC Tree
2.1.1.15 fatty-acid O-methyltransferaseIUBMB Comments
Oleic acid is the most effective fatty acid acceptor.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
bp2936, fatty acid methyltransferase, fatty acid methyl-transferase, fatty acid o-methyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BP2936
FAMT
fatty acid methyl-transferase
fatty acid methyltransferase
fatty acid O-methyltransferase
-
-
-
-
FmtB
MMAR_3356
fatty acid methyltransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a fatty acid = S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:fatty-acid O-methyltransferase
Oleic acid is the most effective fatty acid acceptor.
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CAS REGISTRY NUMBER
COMMENTARY
37256-89-6
-
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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
3-hydroxydecanoic acid + S-adenosyl-L-methionine
methyl 3-hydroxydecanoate + S-adenosyl-L-homocysteine
3-hydroxydodecanoic acid + S-adenosyl-L-methionine
methyl 3-hydroxydodecanoate + S-adenosyl-L-homocysteine
-
-
-
-
?
3-hydroxyoctanoic acid + S-adenosyl-L-methionine
methyl 3-hydroxyoctanoate + S-adenosyl-L-homocysteine
dodecanoic acid + S-adenosyl-L-methionine
methyl dodecanoate + S-adenosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
S-adenosyl-L-methionine + oleic acid
S-adenosyl-L-homocysteine + oleic acid methyl ester
-
oleic acid is the most effective fatty acid acceptor, traces of activity with phosphatidylethanolamine and phosphatidylglycerol
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine
-
-
-
?
additional information
?
-
-
traces of activity with methionine, serine and S-adenosylethinonine as methyl donor
-
-
?
3-hydroxydecanoic acid + S-adenosyl-L-methionine
methyl 3-hydroxydecanoate + S-adenosyl-L-homocysteine
-
-
-
-
?
3-hydroxydecanoic acid + S-adenosyl-L-methionine
methyl 3-hydroxydecanoate + S-adenosyl-L-homocysteine
-
-
-
?
3-hydroxydecanoic acid + S-adenosyl-L-methionine
methyl 3-hydroxydecanoate + S-adenosyl-L-homocysteine
-
-
-
?
3-hydroxyoctanoic acid + S-adenosyl-L-methionine
methyl 3-hydroxyoctanoate + S-adenosyl-L-homocysteine
-
-
-
-
?
3-hydroxyoctanoic acid + S-adenosyl-L-methionine
methyl 3-hydroxyoctanoate + S-adenosyl-L-homocysteine
-
-
-
?
3-hydroxyoctanoic acid + S-adenosyl-L-methionine
methyl 3-hydroxyoctanoate + S-adenosyl-L-homocysteine
-
-
-
?
decanoic acid + S-adenosyl-L-methionine
methyl decanoate + S-adenosyl-L-homocysteine
-
-
-
-
?
decanoic acid + S-adenosyl-L-methionine
methyl decanoate + S-adenosyl-L-homocysteine
-
-
-
?
decanoic acid + S-adenosyl-L-methionine
methyl decanoate + S-adenosyl-L-homocysteine
-
-
-
?
octanoic acid + S-adenosyl-L-methionine
methyl octanoate + S-adenosyl-L-homocysteine
-
-
-
-
?
octanoic acid + S-adenosyl-L-methionine
methyl octanoate + S-adenosyl-L-homocysteine
-
-
-
?
octanoic acid + S-adenosyl-L-methionine
methyl octanoate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
-
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
involved in biosynthesis of branched chain fatty acids, mycolic acid, menaquinones and in esterification of fatty acid carboxyl group
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
-
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
oleic acid is the most effective fatty acid acceptor, traces of activity with phosphatidylethanolamine and phosphatidylglycerol
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
synthesis of 10-methylstearic acid
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
involved in biosynthesis of branched chain fatty acids, mycolic acid, menaquinones and in esterification of fatty acid carboxyl group
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
-
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
-
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
involved in biosynthesis of phosphatidylcholine
-
?
S-adenosyl-L-methionine + abietic acid
S-adenosyl-L-homocysteine + methyl abietate
-
-
-
?
S-adenosyl-L-methionine + abietic acid
S-adenosyl-L-homocysteine + methyl abietate
-
-
-
?
S-adenosyl-L-methionine + palmitate
S-adenosyl-L-homocysteine + palmitoyl methyl ester
-
-
-
?
S-adenosyl-L-methionine + palmitate
S-adenosyl-L-homocysteine + palmitoyl methyl ester
-
-
-
?
S-adenosyl-L-methionine + palmitic acid
S-adenosyl-L-homocysteine + methyl palmitate
-
-
-
?
S-adenosyl-L-methionine + palmitic acid
S-adenosyl-L-homocysteine + methyl palmitate
-
-
-
?
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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
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
involved in biosynthesis of branched chain fatty acids, mycolic acid, menaquinones and in esterification of fatty acid carboxyl group
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
synthesis of 10-methylstearic acid
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
involved in biosynthesis of branched chain fatty acids, mycolic acid, menaquinones and in esterification of fatty acid carboxyl group
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
-
-
?
S-adenosyl-L-methionine + a fatty acid
S-adenosyl-L-homocysteine + a fatty acid methyl ester
-
involved in biosynthesis of phosphatidylcholine
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-(6-aminohexyl)-5-chloro-1-naphthalene-sulfonamide
-
W7, very strong inhibition
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Characterization of a Bvg-regulated fatty acid methyl-transferase in Bordetella pertussis.
Whooping Cough
Characterization of a Bvg-regulated fatty acid methyl-transferase in Bordetella pertussis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
expression of BP2936 is regulated in a similar manner as the bona fide virulence genes. Loss of BP2936 gene expression does not appear to affect host-pathogen interaction in cellular and animal models of infection
physiological function
-
expression of BP2936 is regulated in a similar manner as the bona fide virulence genes. Loss of BP2936 gene expression does not appear to affect host-pathogen interaction in cellular and animal models of infection
-
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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). MTF2_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
274
0
31353
Swiss-Prot
-
A8LLB3_DINSH
Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12)
233
0
24325
TrEMBL
-
B2HHT4_MYCMM
Mycobacterium marinum (strain ATCC BAA-535 / M)
368
0
40293
TrEMBL
-
Q7VUX9_BORPE
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
335
0
37265
TrEMBL
-
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q154A
17fold increaseof the KM with octanoate as a substrate, and 5fold increase of the KM for 3-hydroxydecanoate
Q154A
-
17fold increaseof the KM with octanoate as a substrate, and 5fold increase of the KM for 3-hydroxydecanoate
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of BP2936 is regulated in a similar manner as the bona fide virulence genes
expression of BP2936 is regulated in a similar manner as the bona fide virulence genes
expression of BP2936 is regulated in a similar manner as the bona fide virulence genes
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Akamatsu, Y.; Law, J.H.
The enzymatic synthesis of fatty acid methyl esters by carboxyl group alkylation
J. Biol. Chem.
245
709-713
1970
Mycolicibacterium phlei
brenda
Orpiszewski, J.; Hebda, C.; Szykula, J.; Powls, R.; Clasper, S.; Rees, H.H.
Multiple forms of O-methyltransferase involved in the microbial conversion of abietic acid into methyl abietate by Mycobacterium sp
FEMS Microbiol. Lett.
82
233-236
1991
Mycobacterium sp., Mycolicibacterium phlei
-
brenda
Safayhi, H.; Anazodo, M.I.; Ammon, H.P.T.
Calmodulin- and calcium-insensitive fatty acid methyltransferase from RINm5F cells. Inhibition by trifluoperazine and W7
Int. J. Biochem.
23
769-772
1991
Rattus norvegicus
brenda
Sastry, B.V.R.; Vidaver, P.S.; Janson, V.E.; Franks, J.J.
S-Adenosyl-L-methionine-mediated enzymic methylations in the rat retinal membranes
J. Ocul. Pharmacol.
10
253-263
1994
Rattus norvegicus
brenda
Nawabi, P.; Bauer, S.; Kyrpides, N.; Lykidis, A.
Engineering Escherichia coli for biodiesel production utilizing a bacterial fatty acid methyltransferase
Appl. Environ. Microbiol.
77
8052-8061
2011
Mycobacterium marinum
brenda
Petronikolou, N.; Nair, S.K.
Biochemical studies of mycobacterial fatty acid methyltransferase: A catalyst for the enzymatic production of biodiesel
Chem. Biol.
22
1480-1490
2015
Mycobacterium marinum (B2HHT4), Mycobacterium marinum, Mycobacterium marinum ATCC BAA-535 (B2HHT4)
brenda
Rivera-Millot, A.; Lesne, E.; Solans, L.; Coutte, L.; Bertrand-Michel, J.; Froguel, P.; Dhennin, V.; Hot, D.; Locht, C.; Antoine, R.; Jacob-Dubuisson, F.
Characterization of a Bvg-regulated fatty acid methyl-transferase in Bordetella pertussis
PLoS One
12
e0176396
2017
Bordetella pertussis (Q7VUX9), Bordetella pertussis, Bordetella pertussis ATCC BAA-589 (Q7VUX9)
brenda
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