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Information on EC 2.3.1.268 - ethanol O-acetyltransferase
for references in articles please use BRENDA:EC2.3.1.268
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.268 ethanol O-acetyltransferase
IUBMB Comments
The enzyme, characterized from the yeast Wickerhamomyces anomalus, is responsible for most ethyl acetate synthesis in known ethyl acetate-producing yeasts. It is only distantly related to enzymes classified as EC 2.3.1.84, alcohol O-acetyltransferase. The enzyme also possesses thioesterase and esterase activities, which are inhibited by high ethanol concentrations.
The enzyme appears in viruses and cellular organisms
showSynonyms
ethanol acetyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAT
alcohol acetyltransferase
alcohol O-acetyltransferase 1
alcohol O-acetyltransferase 2
ATF1
ATF2
eat1
eath
ethanol acetyltransferase
ethanol acetyltransferase 1
Wanomala_5543
additional information
eat1
-
-
-
-
ethanol acetyltransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ethanol + acetyl-CoA = ethyl acetate + CoA
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:ethanol O-acetyltransferase
The enzyme, characterized from the yeast Wickerhamomyces anomalus, is responsible for most ethyl acetate synthesis in known ethyl acetate-producing yeasts. It is only distantly related to enzymes classified as EC 2.3.1.84, alcohol O-acetyltransferase. The enzyme also possesses thioesterase and esterase activities, which are inhibited by high ethanol concentrations.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-penten-3-ol + acetyl-CoA
1-penten-3-yl acetate + CoA
Substrates: -
Products: -
Products: -
r
2-ethyl-1-butanol + acetyl-CoA
2-ethyl-1-butyl acetate + CoA
Substrates: -
Products: -
Products: -
r
2-methyl-1-butanol + acetyl-CoA
2-methyl-1-butyl acetate + CoA
Substrates: -
Products: -
Products: -
r
anisyl alcohol + acetyl-CoA
? + CoA
Substrates: -
Products: -
Products: -
r
butanol + acetyl-CoA
butyl acetate + CoA
Substrates: -
Products: -
Products: -
r
cinnamyl alcohol + acetyl-CoA
? + CoA
Substrates: -
Products: -
Products: -
r
decanol + acetyl-CoA
decyl acetate + CoA
Substrates: -
Products: -
Products: -
r
ethanol + decanoyl-CoA
ethyl decanoate + CoA
-
Substrates: -
Products: -
Products: -
r
ethanol + hexanoyl-CoA
ethyl hexanoate + CoA
-
Substrates: -
Products: -
Products: -
r
ethanol + octanoyl-CoA
ethyl octanoate + CoA
-
Substrates: -
Products: -
Products: -
r
ethyl mercaptan + acetyl-CoA
? + CoA
Substrates: -
Products: -
Products: -
r
ethylene glycol + acetyl-CoA
ethylene glycol acetate + CoA
Substrates: -
Products: -
Products: -
r
furfuryl alcohol + acetyl-CoA
? + CoA
Substrates: -
Products: -
Products: -
r
glycerol + acetyl-CoA
glyceryl acetate + CoA
Substrates: -
Products: -
Products: -
r
heptanol + acetyl-CoA
heptyl acetate + CoA
Substrates: -
Products: -
Products: -
r
hexanol + acetyl-CoA
hexyl acetate + CoA
Substrates: -
Products: -
Products: -
r
isoamyl alcohol + acetyl-CoA
3-methyl-1-butyl acetate + CoA
Substrates: -
Products: -
Products: -
r
isobutanol + acetyl-CoA
isobutyl acetate + CoA
Substrates: -
Products: -
Products: -
r
isopropanol + acetyl-CoA
isopropyl acetate + CoA
Substrates: -
Products: -
Products: -
r
methanol + acetyl-CoA
methyl acetate + CoA
Substrates: -
Products: -
Products: -
r
nonanol + acetyl-CoA
nonyl acetate + CoA
Substrates: -
Products: -
Products: -
r
octanol + acetyl-CoA
octyl acetate + CoA
Substrates: -
Products: -
Products: -
r
pentanol + acetyl-CoA
pentyl acetate + CoA
Substrates: -
Products: -
Products: -
r
phenylethyl alcohol + acetyl-CoA
phenyl ethyl acetate + CoA
Substrates: -
Products: -
Products: -
r
propanol + acetyl-CoA
propyl acetate + CoA
Substrates: -
Products: -
Products: -
r
propylene glycol + acetyl-CoA
propylene glycol acetate + CoA
Substrates: -
Products: -
Products: -
r
tert-butanol + acetyl-CoA
tert-butyl acetate + CoA
Substrates: -
Products: -
Products: -
r
4-nitrophenyl acetate + CoA
4-nitrophenol + acetyl-CoA
Substrates: -
Products: -
Products: -
r
4-nitrophenyl acetate + CoA
4-nitrophenol + acetyl-CoA
Substrates: -
Products: -
Products: -
r
4-nitrophenyl acetate + CoA
4-nitrophenol + acetyl-CoA
-
Substrates: -
Products: -
Products: -
r
4-nitrophenyl butyrate + CoA
4-nitrophenol + butyryl-CoA
Substrates: -
Products: -
Products: -
r
4-nitrophenyl butyrate + CoA
4-nitrophenol + butyryl-CoA
Substrates: -
Products: -
Products: -
r
4-nitrophenyl butyrate + CoA
4-nitrophenol + butyryl-CoA
-
Substrates: -
Products: -
Products: -
r
4-nitrophenyl hexanoate + CoA
4-nitrophenol + hexanoyl-CoA
Substrates: -
Products: -
Products: -
r
4-nitrophenyl hexanoate + CoA
4-nitrophenol + hexanoyl-CoA
Substrates: -
Products: -
Products: -
r
4-nitrophenyl hexanoate + CoA
4-nitrophenol + hexanoyl-CoA
-
Substrates: -
Products: -
Products: -
r
acetyl-CoA + ethanol
CoA + ethyl acetate
Substrates: -
Products: -
Products: -
r
acetyl-CoA + ethanol
CoA + ethyl acetate
Substrates: -
Products: -
Products: -
r
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?, r
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?, r
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
-
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
-
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: recombinant enzyme EatH prefers short-chain acyl substrates, but has a broad alcohol substrate spectrum from short-chain primary alcohols to aromatic alcohols
Products: -
Products: -
-
additional information
?
-
-
Substrates: Eat1 can also function as a thioesterase hydrolyzing acetyl-CoA and as esterase hydrolizing ethyl acetate
Products: -
Products: -
?
additional information
?
-
Substrates: Eat1 can also function as a thioesterase hydrolyzing acetyl-CoA and as esterase hydrolizing ethyl acetate
Products: -
Products: -
?
additional information
?
-
Substrates: Eat1 can also function as a thioesterase hydrolyzing acetyl-CoA and as esterase hydrolizing ethyl acetate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is specific for ethanol as well as fused alcohols and acetyl-CoA as substrates producing ethyl acetate and other acetate esters as products. EAT1 shows alcohol acyltransferase and thioesterase, as well as esterase activties, overview
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme is specific for ethanol and short to medium-chain length fatty acid-CoA as substrates. EHT1 shows alcohol acyltransferase and thioesterase, as well as esterase activties, overview
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
-
Substrates: -
Products: -
Products: -
?
ethanol + acetyl-CoA
ethyl acetate + CoA
-
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no effect on enzyme activity by EDTA
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no effect on enzyme activity by EDTA
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.16
4-nitrophenyl acetate
recombinant wild-type enzyme, pH 7.5, 35°C
1.18
4-nitrophenyl butyrate
recombinant wild-type enzyme, pH 7.5, 35°C
0.19
4-nitrophenyl hexanoate
recombinant wild-type enzyme, pH 7.5, 35°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
33.68
4-nitrophenyl acetate
recombinant wild-type enzyme, pH 7.5, 35°C
8.32
4-nitrophenyl butyrate
recombinant wild-type enzyme, pH 7.5, 35°C
0.79
4-nitrophenyl hexanoate
recombinant wild-type enzyme, pH 7.5, 35°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
29.03
4-nitrophenyl acetate
recombinant wild-type enzyme, pH 7.5, 35°C
7.05
4-nitrophenyl butyrate
recombinant wild-type enzyme, pH 7.5, 35°C
4.16
4-nitrophenyl hexanoate
recombinant wild-type enzyme, pH 7.5, 35°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate 2-ethyl-1-butanol
10.23
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate hexanol
10.75
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate isopropanol
10.76
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate heptanol
10.79
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate furfuryl alcohol
10.99
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate butanol
11
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate methanol
11.06
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate cinnamyl alcohol
11.46
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate 2-methyl-1-butanol
12.63
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate nonanol
12.89
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate decanol
13.84
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate pentanol
13.99
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate ethylene glycol
14.27
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate tert-butanol
14.4
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate isobutanol
14.85
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate octanol
15.01
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate propanol
18.71
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate ethanol
6.18
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate isoamyl alcohol
6.98
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate anisyl alcohol
8.58
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate ethyl mercaptan
8.76
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate glycerol
9.54
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate 1-penten-3-ol
9.56
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate phenylethyl alcohol
9.75
purified recombinant wild-type enzyme, pH 7.5, 35°C, substrate propylene glycol
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
activity range, over 90% activity at pH 7.0-8.0, 70% activity remaining at pH 9.5, inactivation above pH 10.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the N-terminal domain of enzyme Eat1 is responsible for targeting
brenda
-
the N-terminal domain of enzyme Eat1 is responsible for targeting
-
brenda
-
the N-terminal domain of enzyme Eat1 is responsible for targeting
-
brenda
-
the N-terminal domain of enzyme Eat1 is responsible for targeting
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the alpha/beta-hydrolase family (PF00561)
malfunction
metabolism
physiological function
additional information
malfunction
modulation of expression of the TCA cycle and electron transport chain genes using a highly multiplexed CRISPRi approach, simultaneous knockdown of ACO2b, SDH2, RIP1, and MSS51 results in a 3.8fold increase in ethyl acetate productivity over the already high natural capacity
malfunction
catalytic mechanism analysis of enzyme mutants, overview
malfunction
-
modulation of expression of the TCA cycle and electron transport chain genes using a highly multiplexed CRISPRi approach, simultaneous knockdown of ACO2b, SDH2, RIP1, and MSS51 results in a 3.8fold increase in ethyl acetate productivity over the already high natural capacity
-
malfunction
-
modulation of expression of the TCA cycle and electron transport chain genes using a highly multiplexed CRISPRi approach, simultaneous knockdown of ACO2b, SDH2, RIP1, and MSS51 results in a 3.8fold increase in ethyl acetate productivity over the already high natural capacity
-
malfunction
-
modulation of expression of the TCA cycle and electron transport chain genes using a highly multiplexed CRISPRi approach, simultaneous knockdown of ACO2b, SDH2, RIP1, and MSS51 results in a 3.8fold increase in ethyl acetate productivity over the already high natural capacity
-
malfunction
-
catalytic mechanism analysis of enzyme mutants, overview
-
metabolism
the enzyme is involved in the the primary pathways of precursor and acetate ester biosynthesis
metabolism
-
Wickerhamomyces subpelliculosus produces a variety of volatile flavor compounds, leading to the identification of the alcohol acyltransferase (AATase) family of genes comprising 7 genes encoding alcohol-O-acetyltransferases (ATFs) and ethanol acetyltransferase 1 (EAT1) for acetate ester formation, along with ethanol hexanoyl transferase 1 (EHT1) for ethyl ester formation
metabolism
-
the enzyme is involved in the the primary pathways of precursor and acetate ester biosynthesis
-
metabolism
-
the enzyme is involved in the the primary pathways of precursor and acetate ester biosynthesis
-
metabolism
-
the enzyme is involved in the the primary pathways of precursor and acetate ester biosynthesis
-
physiological function
the alcohol acetyltransferase Eat1 is the critical enzyme for ethyl, isoamyl, and phenylethyl acetate production. Ethyl acetate is formed from the condensation of ethanol and acetyl-CoA. Mitochondrial localization of Eat1 is necessary for high ethyl acetate production
physiological function
expression in Saccharomyces cerevisiae and Escherichia coli results in high ethyl acetate production
physiological function
-
enzyme WsEAT1 catalyzes the production of ethyl acetate via its AATase activity. Additional alcoholysis activity of WsEAT1 is observed. EAT1 functions in relieving acetyl-CoA accumulation
physiological function
-
enzyme WsEHT1 catalyzes the production of ethyl decanoate via its AATase activity. Additional thioesterase activity of WsEHT1 is observed. EHT1 functions in medium-chain fatty acid (MCFA) detoxification
physiological function
-
expression in Saccharomyces cerevisiae and Escherichia coli results in high ethyl acetate production
-
physiological function
-
the alcohol acetyltransferase Eat1 is the critical enzyme for ethyl, isoamyl, and phenylethyl acetate production. Ethyl acetate is formed from the condensation of ethanol and acetyl-CoA. Mitochondrial localization of Eat1 is necessary for high ethyl acetate production
-
physiological function
-
the alcohol acetyltransferase Eat1 is the critical enzyme for ethyl, isoamyl, and phenylethyl acetate production. Ethyl acetate is formed from the condensation of ethanol and acetyl-CoA. Mitochondrial localization of Eat1 is necessary for high ethyl acetate production
-
physiological function
-
the alcohol acetyltransferase Eat1 is the critical enzyme for ethyl, isoamyl, and phenylethyl acetate production. Ethyl acetate is formed from the condensation of ethanol and acetyl-CoA. Mitochondrial localization of Eat1 is necessary for high ethyl acetate production
-
additional information
the enzyme contains a conserved Ser-Asp-His catalytic triad
additional information
-
the enzyme harbors a Ser-Asp-His catalytic triad, it is active with ethanol and fusel alcohols
additional information
-
the enzyme harbors a Ser-Asp-His catalytic triad
additional information
-
the enzyme contains a conserved Ser-Asp-His catalytic triad
-
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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). AT9_ACTER
432
0
47661
Swiss-Prot
Secretory Pathway (Reliability: 2)
AT9_ACTCC
432
0
47639
Swiss-Prot
-
EAT1_WICAA
Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8)
391
0
45069
Swiss-Prot
Secretory Pathway (Reliability: 3)
EAT1_CYBJN
Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 / NRRL Y-1542)
336
0
38427
Swiss-Prot
other Location (Reliability: 1)
EAT1_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
393
0
44775
Swiss-Prot
-
EAT1_ERECY
Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582)
358
0
40864
Swiss-Prot
-
AT9_ACTDE
432
0
47716
Swiss-Prot
other Location (Reliability: 2)
EAT1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
328
0
37937
Swiss-Prot
-
EAT1_KLULA
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
368
0
41851
Swiss-Prot
other Location (Reliability: 1)
EAT1_KLUMD
Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
363
0
41758
Swiss-Prot
-
ATF1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
525
0
61036
Swiss-Prot
-
ATF2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
535
0
61898
Swiss-Prot
Secretory Pathway (Reliability: 1)
W0T8X1_KLUMD
Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
515
0
59796
TrEMBL
other Location (Reliability: 3)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 37880, sequence calculation, x * 38000, recombinant His-tagged wild-type enzyme, SDS-PAGE
?
-
x * 37880, sequence calculation, x * 38000, recombinant His-tagged wild-type enzyme, SDS-PAGE
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N149S
site-directed mutagenesis, the mutant shows enhanced enzyme activity toward pNP-hexanoate by 5.0, 6.6, and 3.6fold compared to wild-type enzyme
Y204S
site-directed mutagenesis, the mutant shows enzyme activity for pNP-butyrate enhanced by 2.6 times compared to wild-type enzyme due to a wider substrate binding pocket and enhanced hydrophobicity
N149S
-
site-directed mutagenesis, the mutant shows enhanced enzyme activity toward pNP-hexanoate by 5.0, 6.6, and 3.6fold compared to wild-type enzyme
-
Y204S
-
site-directed mutagenesis, the mutant shows enzyme activity for pNP-butyrate enhanced by 2.6 times compared to wild-type enzyme due to a wider substrate binding pocket and enhanced hydrophobicity
-
D145A
mutation in Ser-Asp-His catalytic triad, loss of activity
H295A
mutation in Ser-Asp-His catalytic triad, loss of activity
S121A
mutation in Ser-Asp-His catalytic triad, loss of activity
D145A
-
mutation in Ser-Asp-His catalytic triad, loss of activity
-
H295A
-
mutation in Ser-Asp-His catalytic triad, loss of activity
-
S121A
-
mutation in Ser-Asp-His catalytic triad, loss of activity
-
additional information
additional information
catalytic mechanism of enzyme mutants, overview
additional information
construction of an Eat1 knockout mutant and of N-terminally truncated mutants. Modulation of expression of the TCA cycle and electron transport chain genes using a highly multiplexed CRISPRi approach, simultaneous knockdown of ACO2b, SDH2, RIP1, and MSS51 results in a 3.8fold increase in ethyl acetate productivity over the already high natural capacity. Mitochondrial localization is partially lost when the first 14 amino acids are removed with complete cytosolic expression resulting from truncation at the predicted cut site, i.e. mutants Eat1(DELTA1-14) and Eat1(DELTA1-19)
additional information
in order to expand the product profile of this bacterium, five alcohol acetyltransferases (AATs) from yeast are heterologously expressed in Clostridium ljungdahlii strain DSM 13528 to elevate ethyl acetate production. When growing on CO2 and H2, up to 7.38 mg/l of ethyl acetate are produced. Using fructose as the main carbon and energy source, up to 23.15 mg/l of ethyl acetate are produced. Ethanol and fumarate supplementation are able to boost ethyl acetate titers (up to 37.51 mg/l). Ethyl acetate production is enabled in Clostridium ljungdahlii at low titers, which could be explained by the high energetic cost of operation of AATs, and their shown promiscuity
additional information
in order to expand the product profile of this bacterium, five alcohol acetyltransferases (AATs) from yeast are heterologously expressed in Clostridium ljungdahlii strain DSM 13528 to elevate ethyl acetate production. When growing on CO2 and H2, up to 7.38 mg/l of ethyl acetate are produced. Using fructose as the main carbon and energy source, up to 23.15 mg/l of ethyl acetate are produced. Ethanol and fumarate supplementation are able to boost ethyl acetate titers (up to 37.51 mg/l). Ethyl acetate production is enabled in Clostridium ljungdahlii at low titers, which could be explained by the high energetic cost of operation of AATs, and their shown promiscuity
additional information
-
construction of an Eat1 knockout mutant and of N-terminally truncated mutants. Modulation of expression of the TCA cycle and electron transport chain genes using a highly multiplexed CRISPRi approach, simultaneous knockdown of ACO2b, SDH2, RIP1, and MSS51 results in a 3.8fold increase in ethyl acetate productivity over the already high natural capacity. Mitochondrial localization is partially lost when the first 14 amino acids are removed with complete cytosolic expression resulting from truncation at the predicted cut site, i.e. mutants Eat1(DELTA1-14) and Eat1(DELTA1-19)
-
additional information
-
in order to expand the product profile of this bacterium, five alcohol acetyltransferases (AATs) from yeast are heterologously expressed in Clostridium ljungdahlii strain DSM 13528 to elevate ethyl acetate production. When growing on CO2 and H2, up to 7.38 mg/l of ethyl acetate are produced. Using fructose as the main carbon and energy source, up to 23.15 mg/l of ethyl acetate are produced. Ethanol and fumarate supplementation are able to boost ethyl acetate titers (up to 37.51 mg/l). Ethyl acetate production is enabled in Clostridium ljungdahlii at low titers, which could be explained by the high energetic cost of operation of AATs, and their shown promiscuity
-
additional information
-
construction of an Eat1 knockout mutant and of N-terminally truncated mutants. Modulation of expression of the TCA cycle and electron transport chain genes using a highly multiplexed CRISPRi approach, simultaneous knockdown of ACO2b, SDH2, RIP1, and MSS51 results in a 3.8fold increase in ethyl acetate productivity over the already high natural capacity. Mitochondrial localization is partially lost when the first 14 amino acids are removed with complete cytosolic expression resulting from truncation at the predicted cut site, i.e. mutants Eat1(DELTA1-14) and Eat1(DELTA1-19)
-
additional information
-
in order to expand the product profile of this bacterium, five alcohol acetyltransferases (AATs) from yeast are heterologously expressed in Clostridium ljungdahlii strain DSM 13528 to elevate ethyl acetate production. When growing on CO2 and H2, up to 7.38 mg/l of ethyl acetate are produced. Using fructose as the main carbon and energy source, up to 23.15 mg/l of ethyl acetate are produced. Ethanol and fumarate supplementation are able to boost ethyl acetate titers (up to 37.51 mg/l). Ethyl acetate production is enabled in Clostridium ljungdahlii at low titers, which could be explained by the high energetic cost of operation of AATs, and their shown promiscuity
-
additional information
-
construction of an Eat1 knockout mutant and of N-terminally truncated mutants. Modulation of expression of the TCA cycle and electron transport chain genes using a highly multiplexed CRISPRi approach, simultaneous knockdown of ACO2b, SDH2, RIP1, and MSS51 results in a 3.8fold increase in ethyl acetate productivity over the already high natural capacity. Mitochondrial localization is partially lost when the first 14 amino acids are removed with complete cytosolic expression resulting from truncation at the predicted cut site, i.e. mutants Eat1(DELTA1-14) and Eat1(DELTA1-19)
-
additional information
-
in order to expand the product profile of this bacterium, five alcohol acetyltransferases (AATs) from yeast are heterologously expressed in Clostridium ljungdahlii strain DSM 13528 to elevate ethyl acetate production. When growing on CO2 and H2, up to 7.38 mg/l of ethyl acetate are produced. Using fructose as the main carbon and energy source, up to 23.15 mg/l of ethyl acetate are produced. Ethanol and fumarate supplementation are able to boost ethyl acetate titers (up to 37.51 mg/l). Ethyl acetate production is enabled in Clostridium ljungdahlii at low titers, which could be explained by the high energetic cost of operation of AATs, and their shown promiscuity
-
additional information
in Saccharomyces cerevisiae, the genes encoding phosphopantothenate-cysteine ligase, acetyl-CoA synthetase, and alcohol acetyltransferase are overexpressed by inserting the combined strong promoter PGK1p and the terminator PGK1t. The ethyl acetate levels of all engineered strains are enhanced. The final engineered strain CLy12a-ATF1-ACS2-CAB2 has an ethyl acetate yield of max. 610.26 mg/l, and the yield of higher alcohols is significantly decreased. The modification of ethyl acetate metabolic pathway is extremely important for the high level production of ethyl acetate in Saccharomyces cerevisiae
additional information
in order to expand the product profile of this bacterium, five alcohol acetyltransferases (AATs) from yeast are heterologously expressed in Clostridium ljungdahlii strain DSM 13528 to elevate ethyl acetate production. When growing on CO2 and H2, up to 7.38 mg/l of ethyl acetate are produced. Using fructose as the main carbon and energy source, up to 23.15 mg/l of ethyl acetate are produced. Ethanol and fumarate supplementation are able to boost ethyl acetate titers (up to 37.51 mg/l). Ethyl acetate production is enabled in Clostridium ljungdahlii at low titers, which could be explained by the high energetic cost of operation of AATs, and their shown promiscuity
additional information
in order to expand the product profile of this bacterium, five alcohol acetyltransferases (AATs) from yeast are heterologously expressed in Clostridium ljungdahlii strain DSM 13528 to elevate ethyl acetate production. When growing on CO2 and H2, up to 7.38 mg/l of ethyl acetate are produced. Using fructose as the main carbon and energy source, up to 23.15 mg/l of ethyl acetate are produced. Ethanol and fumarate supplementation are able to boost ethyl acetate titers (up to 37.51 mg/l). Ethyl acetate production is enabled in Clostridium ljungdahlii at low titers, which could be explained by the high energetic cost of operation of AATs, and their shown promiscuity
additional information
-
in Saccharomyces cerevisiae, the genes encoding phosphopantothenate-cysteine ligase, acetyl-CoA synthetase, and alcohol acetyltransferase are overexpressed by inserting the combined strong promoter PGK1p and the terminator PGK1t. The ethyl acetate levels of all engineered strains are enhanced. The final engineered strain CLy12a-ATF1-ACS2-CAB2 has an ethyl acetate yield of max. 610.26 mg/l, and the yield of higher alcohols is significantly decreased. The modification of ethyl acetate metabolic pathway is extremely important for the high level production of ethyl acetate in Saccharomyces cerevisiae
-
additional information
-
in order to expand the product profile of this bacterium, five alcohol acetyltransferases (AATs) from yeast are heterologously expressed in Clostridium ljungdahlii strain DSM 13528 to elevate ethyl acetate production. When growing on CO2 and H2, up to 7.38 mg/l of ethyl acetate are produced. Using fructose as the main carbon and energy source, up to 23.15 mg/l of ethyl acetate are produced. Ethanol and fumarate supplementation are able to boost ethyl acetate titers (up to 37.51 mg/l). Ethyl acetate production is enabled in Clostridium ljungdahlii at low titers, which could be explained by the high energetic cost of operation of AATs, and their shown promiscuity
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 10
purified recombinant His-tagged wild-type enzyme, 80% activity remaining within this range
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
purified recombinant His-tagged wild-type enzyme, loss of 30% activity after 3h, still 70% activity remaining after 24 h
30
purified recombinant His-tagged wild-type enzyme, loss of 30% activity after 6h, still 70% activity remaining after 24 h
40
purified recombinant His-tagged wild-type enzyme, loss of 80% activity after 9 h, inactivation after 24 h
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and HiTrap SP column chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae INVSc1 and Escherichia coli BL21 (DE3) cells
gene ATF1, cloning and recombinant expression of gene ATF1 from Kluyveromyces marxianus strain DSM 5418 in Clostridium ljungdahlii strain DSM 13528
gene ATF1, cloning and recombinant expression of gene ATF1 from Saccharomyces cerevisiae strain DSM 70449 in Clostridium ljungdahlii strain DSM 13528
gene EAT1, cloning and recombinant expression of gene ATF1 from Kluyveromyces marxianus strain DSM 5418 in Clostridium ljungdahlii strain DSM 13528
gene eat1, quantitative RT-PCR enzyme expression analysis in engineered strain CLy12a derivatives
gene EAT1, recombinant expression of N-terminally truncated mutants Eat1(DELTA1-14) and Eat1(DELTA1-19) in Saccharomyces cerevisiae and Kluyveromyces marxianus, recombinant expression of GFP-tagged wild-type enzyme in Kluyveromyces marxianus
gene eath, cloning and codon optimization, sequence comparisons and phylogenetic analysis and tree, recombinant expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
Eat1-catalyzed ethyl acetate production occurs in yeast mitochondria
synthesis
evaluation of yeast alcohol acetyltransferases for ethyl acetate production in Clostridium ljungdahlii strain DSM 13528, overview
synthesis
evaluation of yeast alcohol acetyltransferases for ethyl acetate production in Clostridium ljungdahlii strain DSM 13528, overview
synthesis
ethyl acetate, one of the most essential industrial compounds, has a broad range of applications, including flavors, fragrances, pharmaceuticals, cosmetics, and green solvents. Eat1 is accountable for bulk ethyl acetate production in yeasts
synthesis
-
evaluation of yeast alcohol acetyltransferases for ethyl acetate production in Clostridium ljungdahlii strain DSM 13528, overview
-
synthesis
-
Eat1-catalyzed ethyl acetate production occurs in yeast mitochondria
-
synthesis
-
evaluation of yeast alcohol acetyltransferases for ethyl acetate production in Clostridium ljungdahlii strain DSM 13528, overview
-
synthesis
-
evaluation of yeast alcohol acetyltransferases for ethyl acetate production in Clostridium ljungdahlii strain DSM 13528, overview
-
synthesis
-
evaluation of yeast alcohol acetyltransferases for ethyl acetate production in Clostridium ljungdahlii strain DSM 13528, overview
-
synthesis
-
ethyl acetate, one of the most essential industrial compounds, has a broad range of applications, including flavors, fragrances, pharmaceuticals, cosmetics, and green solvents. Eat1 is accountable for bulk ethyl acetate production in yeasts
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kruis, A.J.; Levisson, M.; Mars, A.E.; van der Ploeg, M.; Garces Daza, F.; Ellena, V.; Kengen, S.W.M.; van der Oost, J.; Weusthuis, R.A.
Ethyl acetate production by the elusive alcohol acetyltransferase from yeast
Metab. Eng.
41
92-101
2017
Wickerhamomyces anomalus, Wickerhamomyces anomalus (A0A1E3P8S6), Wickerhamomyces anomalus DSM 6766, Wickerhamomyces anomalus ATCC 58044 (A0A1E3P8S6)
brenda
Loebs, A.K.; Schwartz, C.; Thorwall, S.; Wheeldon, I.
Highly multiplexed CRISPRi repression of respiratory functions enhances mitochondrial localized ethyl acetate biosynthesis in Kluyveromyces marxianus
ACS Synth. Biol.
7
2647-2655
2018
Kluyveromyces marxianus (W0T4A7), Kluyveromyces marxianus DMKU3-1042 (W0T4A7), Kluyveromyces marxianus BCC 29191 (W0T4A7), Kluyveromyces marxianus NBRC 104275 (W0T4A7)
brenda
Kruis, A.; Mars, A.; Kengen, S.; Borst, J.; van derOost, J.; Weusthuis, R.
Alcohol acetyltransferase Eat1 is located in yeast mitochondria
Appl. Environ. Microbiol.
84
e01640
2018
Kluyveromyces lactis (Q6CLY8), Kluyveromyces lactis ATCC 8585 (Q6CLY8)
brenda
Dong, J.; Wang, P.; Fu, X.; Dong, S.; Li, X.; Xiao, D.
Increase ethyl acetate production in Saccharomyces cerevisiae by genetic engineering of ethyl acetate metabolic pathway
J. Ind. Microbiol. Biotechnol.
46
801-808
2019
Saccharomyces cerevisiae (P53208), Saccharomyces cerevisiae ATCC 204508 (P53208)
brenda
Boto, S.T.; Gerges, K.; Bardl, B.; Rosenbaum, M.A.
Evaluation of yeast alcohol acetyltransferases for ethyl acetate production in Clostridium ljungdahlii
Eng. Life Sci.
25
e202400076
2025
Saccharomyces cerevisiae (P40353), Saccharomyces cerevisiae (P53296), Kluyveromyces marxianus (W0T4A7), Kluyveromyces marxianus (W0T8X1), Saccharomyces cerevisiae ATCC 204508 (P40353), Saccharomyces cerevisiae ATCC 204508 (P53296), Kluyveromyces marxianus DMKU3-1042 (W0T4A7), Kluyveromyces marxianus DMKU3-1042 (W0T8X1), Kluyveromyces marxianus BCC 29191 (W0T4A7), Kluyveromyces marxianus BCC 29191 (W0T8X1), Kluyveromyces marxianus NBRC 104275 (W0T4A7), Kluyveromyces marxianus NBRC 104275 (W0T8X1)
brenda
Yoo, S.J.; Kim, H.J.; Moon, H.Y.; Jeon, M.S.; Cho, Y.U.; Jeon, C.O.; Eyun, S.I.; Kang, H.A.
Genome-wide identification and biochemical characterization of alcohol acyltransferases for aroma generation in Wickerhamomyces subpelliculosus isolates from fermented food
J. Agric. Food Chem.
72
28194-28208
2024
Wickerhamomyces subpelliculosus
brenda
Ni, B.; Fu, Z.; Zhao, J.; Yao, X.; Li, W.; Li, X.; Sun, B.
Characterization and mechanism study of a novel ethanol acetyltransferase from Hanseniaspora uvarum (EatH) with good thermostability, pH stability, and broad alcohol substrate specificity
J. Agric. Food Chem.
73
6828-6841
2025
Hanseniaspora uvarum (A0A1E5RUL9), Hanseniaspora uvarum DSM 2768 (A0A1E5RUL9)
brenda
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