Information on EC 3.1.1.67 - fatty-acyl-ethyl-ester synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.1.67
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RECOMMENDED NAME
GeneOntology No.
fatty-acyl-ethyl-ester synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a long-chain-fatty-acyl ethyl ester + H2O = a long-chain-fatty acid + ethanol
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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-
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SYSTEMATIC NAME
IUBMB Comments
long-chain-fatty-acyl-ethyl-ester acylhydrolase
The reaction, forms ethyl esters from fatty acids and ethanol in the absence of coenzyme A or ATP. Best substrates are unsaturated octadecanoic acids; palmitate, stearate and arachidonate also act, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
90119-16-7
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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
arachidonate + ethanol
ethyl arachidonate + H2O
show the reaction diagram
cholesteryl oleate + H2O
oleate + cholesterol
show the reaction diagram
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180 kDa high molecular weight protein, only hydrolysis, no synthetic activity for cholesterol oleate
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-
ir
cocaine + ethanol
cocaethylene + methanol
show the reaction diagram
fatty acid + 2-chloroethanol
fatty acyl 2-chloroethyl ester + H2O
show the reaction diagram
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long-chain fatty acids, 180 kDa high molecular weight protein
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?
fatty acid + ethanol
fatty acyl ethyl ester + H2O
show the reaction diagram
linoleate + ethanol
ethyl linoleate + H2O
show the reaction diagram
monoacylglycerol + H2O
fatty acid + glycerol
show the reaction diagram
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hydrolysis, susceptibilities of substrates increase with decreasing acyl chain length of the fatty acid moiety
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-
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oleate + 1-butanol
1-butyl oleate + H2O
show the reaction diagram
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63.2% of the activity with 1-propanol
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-
?
oleate + 1-propanol
1-propyl oleate + H2O
show the reaction diagram
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highest activity with 1-propanol
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-
?
oleate + 2-chloroethanol
2-chloroethyl oleate + H2O
show the reaction diagram
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180 kDa high molecular weight protein
-
?
oleate + aniline
oleyl anilide + H2O
show the reaction diagram
oleate + ethanol
ethyl oleate + H2O
show the reaction diagram
oleate + methanol
methyl oleate + H2O
show the reaction diagram
oleic acid + ethanol
ethyl oleate
show the reaction diagram
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-
-
-
?
p-nitrophenyl butyrate + H2O
butyrate + p-nitrophenol
show the reaction diagram
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hydrolysis
-
-
?
palmitate + ethanol
ethyl palmitate + H2O
show the reaction diagram
stearate + ethanol
ethyl stearate + H2O
show the reaction diagram
triacylglycerol + H2O
?
show the reaction diagram
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hydrolysis, susceptibilities of substrates increase with decreasing acyl chain length of the fatty acid moiety
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-
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triolein + H2O
?
show the reaction diagram
additional information
?
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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
cocaine + ethanol
cocaethylene + methanol
show the reaction diagram
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enzyme may be responsible for a portion of cocaethylene synthesis in vivo
product enhances cocaine toxicity
?
fatty acid + ethanol
fatty acyl ethyl ester + H2O
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butanol
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at concentrations greater than 5times Km
1-propanol
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at concentrations greater than 5times Km
2-(o-cresyl)-4H-1:3:2-benzodioxaphosphoran-2-one
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di-p-tolyl-o-(alpha-hydroxy)tolylphosphate
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diisopropylfluorophosphate
NaCl
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inhibits hydrolysis of triglycerides, e.g. triolein
tri-o-tolyl phosphate
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Colipase
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stimulates hydrolysis of triglycerides, e.g. triolein
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
70
1-butanol
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pH 7.2, 37C, cosubstrate oleate
530
1-propanol
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pH 7.2, 37C, cosubstrate oleate
0.13 - 0.2
arachidonate
0.41 - 1100
ethanol
0.2
linoleate
1300
methanol
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pH 7.2, 37C, cosubstrate oleate, value above
0.02 - 0.8
oleate
0.24
oleic acid
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37C
0.18 - 0.2
palmitate
0.12 - 0.2
stearate
additional information
additional information
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thermodynamic parameters relevant to the kinetics and equilibria of the reaction
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024 - 0.285
oleate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0003
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pH 7.2, 37C
0.0006
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native FAEES-III and mutants G32Q, C39W, H72S
0.0028
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pH 7.4, 37C, liver microsomes
0.011 - 0.012
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liver microsomal FAEES activity, at 100 mM ethanol
0.0111
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60 kDa low molecular weight protein from liver microsomes with pI 5.3
0.0112
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pH 7.2, 37C
0.0115
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60 kDa low molecular weight protein from liver microsomes with pI 6.5
0.0125
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60 kDa low molecular weight protein from liver microsomes with pI 5.0
0.0133
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60 kDa low molecular weight protein from liver microsomes with pI 5.6
0.015
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pH 7, 37C
0.025 - 0.026
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liver cytosolic FAEES activity, at 100 mM ethanol
0.0335
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pH 7.4, 37C, 180 kDa high molecular weight protein from liver microsomes, FAEES activity
0.035
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60 kDa low molecular weight protein from liver microsomes with pI 5.8
0.04
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pH 7.2, 37C
0.04433
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major enzyme form
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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optimum and assay at
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
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myocardial FAEES-III
5
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one of five 60 kDa low molecular weight proteins in liver microsomes with FAEES activity, isoelectric focusing
5.3
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one of five 60 kDa low molecular weight proteins in liver microsomes with FAEES activity, isoelectric focusing
5.6 - 5.9
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one of five 60 kDa low molecular weight proteins in liver microsomes with FAEES activity, isoelectric focusing
5.8
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one of five 60 kDa low molecular weight proteins in liver microsomes with FAEES activity, isoelectric focusing
6.1
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180 kDa high molecular weight protein from liver microsomes, isoelectric focusing
6.5
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one of five 60 kDa low molecular weight proteins in liver microsomes with FAEES activity, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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FAEES activity is increased 4fold in the choroid of alcohol-treated rats compared with controls
Manually annotated by BRENDA team
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substantially lower activity in erythrocytes than in leukocytes
Manually annotated by BRENDA team
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ventricular, low activity
Manually annotated by BRENDA team
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substantially lower activity in erythrocytes than in leukocytes
Manually annotated by BRENDA team
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FAEES-III mRNA expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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both cytosolic and membrane-bound
Manually annotated by BRENDA team
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enzyme with FAEES/carboxylesterase activity from heart
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23307
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x * 23307, FAEES-III, calculated from the amino acid sequence
24000
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x * 24000, FAEES-III, SDS-PAGE
50000 - 55000
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gel filtration
50000
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gel filtration under nondenaturing conditions
54000
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gel filtration under nondenaturing conditions
62000
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x * 62000, enzyme with FAEES/carboxylesterase activity from heart, SDS-PAGE
84000
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x * 84000, FAEES from plasma, Western blot analysis
180000
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high molecular weight major protein fraction in liver microsomes with FAEES activity, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
trimer
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3 * 60000, high molecular weight major protein fraction, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1200fold
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5 distinct 60 kDa low molecular weight proteins, 10.2-32.5fold; from liver microsomes, 180 kDa high molecular weight major protein fraction and 60 kDa low molecular weight minor protein fraction
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8867fold, major enzyme form, synthase I
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9000fold
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copurification of FAEES, 2-chloroethyl ester synthase and carboxylesterase activity during each step of purification, FAEES activity: 30.9fold; from liver microsomes, 180 kDa high molecular weight major protein fraction and 60 kDa low molecular weight minor protein fraction
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from adipose tissue, 2 enzyme forms
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from pancreas
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partial, separation of 2 cytosolic enzymes: 26fold and 30fold
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA encoding FAEES-III is cloned from heart, sequenced and expressed in MCF-7 and COS-7 cells, 210 amino acid sequence
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native and mutant forms of FAEES-III cDNA are cloned and expressed in COS-7 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C39W
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mutation does not affect FAEES activity
G32Q
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mutation does not affect FAEES activity
H72S
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mutation does not affect FAEES activity, less than 9% of control glutathione S-transferase activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine