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Information on EC 2.3.1.268 - ethanol O-acetyltransferase and Organism(s) Wickerhamomyces anomalus and UniProt Accession A0A1E3P8S6

for references in articles please use BRENDA:EC2.3.1.268
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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.
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Wickerhamomyces anomalus
UNIPROT: A0A1E3P8S6
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The taxonomic range for the selected organisms is: Wickerhamomyces anomalus
The enzyme appears in selected viruses and cellular organisms
Synonyms
ethanol acetyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ethanol acetyltransferase
ethanol acetyltransferase 1
-
-
Wanomala_5543
-
-
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + ethanol
CoA + ethyl acetate
show the reaction diagram
-
-
-
r
ethanol + acetyl-CoA
ethyl acetate + CoA
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ethanol + acetyl-CoA
ethyl acetate + CoA
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethynol
inhibitory above 80 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.12
acetyl-CoA
pH 7.5, 30°C
2.43
acetyl-CoA
at pH 7.5 and 30°C
3.12
ethanol
at pH 7.5 and 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
expression in Saccharomyces cerevisiae and Escherichia coli results in high ethyl acetate production
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and HiTrap SP column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae INVSc1 and Escherichia coli BL21 (DE3) cells
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 ATCC 58044 (A0A1E3P8S6), Wickerhamomyces anomalus DSM 6766
Manually annotated by BRENDA team