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Information on EC 3.1.1.6 - acetylesterase
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3.1.1.6 acetylesteraseSpecify your search results
Word Map
- 3.1.1.6
- esterases
- xylans
-
deacetylation
- coronavirus
- acetylxylan
-
receptor-destroying
- hemagglutinin-esterase
-
saccharification
- isavs
-
carbohydrate-active
-
glucuronoyl
- glucuronoxylans
-
alpha-naphthyl
-
hemicellulolytic
- xylooligosaccharides
- arylesterase
- orthomyxoviridae
-
cazymes
-
methylesterase
-
lignin-carbohydrate
- industry
-
beta-naphthyl
-
reassortment
- paper production
- molecular biology
- synthesis
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
6-O-deacetylase, ACE, AcE1, acetate ester-hydrolysing esterase, acetic acid esterase, Acetic ester hydrolase, Acetyl esterase, acetyl xylan esterase, acetyl-esterase, acetylesterase CE16, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-O-deacetylase
ACE
acetate ester-hydrolysing esterase
Acetic ester hydrolase
-
-
-
-
Acetyl esterase
acetyl xylan esterase
acetylesterase CE16
AE
Aes1
Axe3
C-esterase
-
-
-
-
carbohydrate acetylesterase
carbohydrate esterase
CE16 acetyl esterase
CE16A
Chloroesterase
-
-
-
-
Citrus acetylesterase
-
-
-
-
Est1
EST2
HerE
p-nitrophenyl acetate esterase
-
-
-
-
PAE1
pectin acetylesterase
ybaC
additional information
-
the enzyme belongs to the carbohydrate esterase family 1
acetate ester-hydrolysing esterase
-
ethyl acetate- and isoamyl acetate-hydrolysing esterase activities
carbohydrate esterase
new family, less than 30% identity to carbohydrate esterases of known families
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an acetic ester + H2O = an alcohol + acetate
-
-
-
-
an acetic ester + H2O = an alcohol + acetate
active site serine, active site structure, reaction and ligand binding mechanism
-
an acetic ester + H2O = an alcohol + acetate
active site serine, active site structure, reaction and ligand binding mechanism
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylation
hydrolysis of carboxylic ester
transacetylation
hydrolysis of carboxylic ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
acetic-ester acetylhydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9000-82-2
-
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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
(acetyloxy)(phenyl)acetic acid + H2O
(S)-mandelic acid + (2R)-(acetyloxy)(phenyl)ethanoic acid
(R)-1,2-O-isopropylidene glycol acetate + H2O
(R)-1,2-O-isopropylidene glycol + acetate
-
-
-
-
?
(R,S)-1,2-O-isopropylidene glycol butyrate + H2O
(R)-1,2-O-isopropylidene glycol + butyrate
-
fresh bacterial cells or purified EST1 (0.01 micromol p-nitrophenol/min), 28°C, pH 8, 5% (v/v) glycerol, 1 mM EDTA, 1 mM dithiothreitol
low enantioselectivity (enantiomeric ratio E: 2.5 for EST1, E: 2.5 for whole cells)
-
?
(R,S)-1,2-O-isopropylidene glycol caproate + H2O
(R)-1,2-O-isopropylidene glycol + caproate
-
fresh bacterial cells or purified EST1 (0.01 micromol p-nitrophenol/min), 28°C, pH 8, 5% (v/v) glycerol, 1 mM EDTA, 1 mM dithiothreitol
no enantioselectivity by EST1 (enantiomeric ratio E: 1) compared to E: 2.8 for whole cells
-
?
1-naphthyl butyrate + H2O
1-naphthol + butyrate
36% activity compared to 1-naphthyl acetate
-
-
?
1-phenyl-1-(trifluoromethyl)prop-2-yn-1-yl acetate + H2O
1-phenyl-1-(trifluoromethyl)prop-2-yn-1-ol + acetate
-
determination of enantiopreference, wild-type R enantioselectivity is 42
spectrophotometric assay coupling released acetate to NADH generation
-
?
2-ethylcyclohex-1-en-1-yl acetate + H2O
2-ethylcyclohexanone + acetate
-
isoenzyme Est I, 99% conversion of substrate with 99% S-configuration of product
-
-
?
2-isopropylcyclohex-1-en-1-yl acetate + H2O
2-isopropylcyclohexanone + acetate
-
isoenzyme Est I, 10% conversion of substrate with R-configuration of product
-
-
?
2-methylcyclohex-1-en-1-yl acetate + H2O
(S)-2-methylcyclohexanone + acetate
-
isoenzyme Est I, 99% conversion of substrate with 99% S-configuration of product
-
-
?
2-n-propylcyclohex-1-en-1-yl acetate + H2O
2-n-propylcyclohexanone + acetate
-
isoenzyme Est I, 99% conversion of substrate with 99% R-configuration of product
-
-
?
3-O-methyl-D-glucopyranoside + vinyl acetate
6-O-acetyl-3-O-methyl-D-glucopyranoside + vinyl alcohol
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
?
4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + vinyl acetate
4-nitrophenyl 3-O-acetyl-beta-D-glucopyranoside + vinyl alcohol
-
yield is 70.2%
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenyl D-xylopyranose
4 mM substrate, position-specificity, hydrolysis activity is specific for 3-, and 4-O-acetyl 4-nitrophenyl-beta-D-xylopyranoside, 2-O-acetyl 4-nitrophenyl-beta-D-xylopyranoside is a bad substrate
beta-xylosidase-coupled assay
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + buytrate
-
lowest activity
-
-
?
4-nitrophenyl formate + H2O
4-nitrophenol + formate
5 min, 30°C, pH 5.8
-
-
?
4-nitrophenyl-2-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl-alpha-L-arabinofuranoside + acetate
-
-
-
-
?
4-nitrophenyl-2-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
-
preferred substrate
-
-
?
4-nitrophenyl-3-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
-
-
-
-
?
4-nitrophenyl-4-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
-
-
-
-
?
4-nitrophenyl-5-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl-alpha-L-arabinofuranoside + acetate
-
-
-
-
?
7-aminocephalosporanic acid + H2O
deacetylated 7-aminocephalosporanic acid + acetate
-
-
-
-
?
acetyl xylan + H2O
xylan + acetate
-
from beech wood or oat spelt
-
?
acetylated hemicellulose + H2O
? + acetate
-
the best substrate of the enzyme is 3-O-acetylated Xylp residue followed by 4-O-acetylated Xylp residue with a free vicinal hydroxyl group
-
-
?
acetylglucuronoxylan + H2O
glucuronoxylan + acetate
-
the enzyme deacetylates singly and doubly acetylated xylopyranosyl residues in the polymer to such an extent that it results in the polymer precipitation
-
-
?
acetylxylan + H2O
xylan + acetate
-
60°C, pH 6, acetyl xylan esterase (acetate-releasing) activity on birchwood xylan
-
-
-
bovine submaxillary mucin + H2O
deacetylated bovine submaxillary mucin + acetate
-
-
-
?
geraniol acetate + H2O
geraniol + acetate
-
enzyme plays a role in geraniol production and improving palmarosa oil quality during florescence development
-
?
isoamyl acetate + H2O
isoamyl alcohol + acetate
-
25°C, 1 h, pH 7, 7 mM MgCl2, cell extracts
-
-
?
kojic acid + vinyl acetate
7-O-acetyl-kojic acid + vinyl alcohol
-
yield is 30.9%
-
-
?
methyl 2,3,4-O-triacetyl-beta-D-xylopyranoside + H2O
methyl 3,4-O-diacetyl-beta-D-xylopyranoside + acetate
-
-
-
-
?
methyl 2,3,4-O-triacetyl-beta-D-xylopyranoside + H2O
methyl beta-D-xylopyranoside + acetate
-
all four acetylated derivatives of methyl beta-xylopyranoside are completely deacetylated after 24 h
-
-
?
methyl 2,3-O-diacetyl-beta-D-xylopyranoside + H2O
methyl 2-O-acetyl-beta-D-xylopyranoside + acetate
-
-
-
-
?
methyl 2,3-O-diacetyl-beta-D-xylopyranoside + H2O
methyl beta-D-xylopyranoside + acetate
-
all four acetylated derivatives of methyl beta-xylopyranoside are completely deacetylated after 24 h
-
-
?
methyl 2,4-O-diacetyl-beta-D-xylopyranoside + H2O
methyl beta-D-xylopyranoside + acetate
-
all four acetylated derivatives of methyl beta-xylopyranoside are completely deacetylated after 24 h
-
-
?
methyl 3,4-O-diacetyl-beta-D-xylopyranoside + H2O
methyl beta-D-xylopyranoside + acetate
-
all four acetylated derivatives of methyl beta-xylopyranoside are completely deacetylated after 24 h
-
-
?
methyl beta-D-glucopyranoside + vinyl acetate
methyl 3-O-acetyl-beta-D-glucopyranoside + vinyl alcohol
-
yield is 56.4%
-
-
?
methyl-beta-D-xylopyranoside + vinylacetate
methyl-beta-D-xylopyranoside monoacetate + vinyl alcohol
transacetylation of methylxyloside in aqueous solution (40°C, pH 6, 25 mM methyl-beta-D-xylopyranoside)
analysis by thin-layer chromatography
-
?
O-acetyl-4-O-methyl-D-glucurono-D-xylan + H2O
4-O-methyl-D-glucurono-D-xylan + acetic acid
penta-O-acetyl-alpha-D-glucose + H2O
?
-
complete and regioselective removal of primary acetyl-group in 6-position
-
-
?
racemic 1-phenylethyl acetate + H2O
(1R)-phenylethanol + (1S)-phenylethanol + acetate
-
-
-
-
?
triacetin + H2O
?
-
EST1, pH 8, 20°C, 0.5% (w/v) Triton X-100, 0.125% (w/v) Arabic gum
titration assay
-
?
[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl acetate + H2O
[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl]methanol + acetate
-
fresh bacterial cells or purified enzyme (EST1 or EST2, 0.01 micromol p-nitrophenol/min), 20°C, pH 8, 5% (v/v) glycerol, 1 mM EDTA, 1 mM dithiothreitol
high enantioselectivity (enantiomeric ratio E: 20 for EST1, E: 15 for whole cells), thin-layer chromatography, enantiomeric composition of reactants controlled by gas chromatography, acetate detection spectrophotometrically through NADH absorbance at 340 nm
-
?
(4R)-hydroxy-3-methyl-2-(2-propynyl)-cyclopent-2-enone acetate + H2O
?
-
highly enantioselective enzyme, enantioselectivity raises by 1.2fold from 16 to 20 when reaction temperature is raised from 30°C to 60°C. Both enantioselectivity and activity are raised by addition of the cationic detergent benzethonium chloride
-
-
?
(4R)-hydroxy-3-methyl-2-(2-propynyl)-cyclopent-2-enone acetate + H2O
?
-
highly enantioselective enzyme, enantioselectivity raises by 1.2fold from 16 to 20 when reaction temperature is raised from 30°C to 60°C. Both enantioselectivity and activity are raised by addition of the cationic detergent benzethonium chloride
-
-
?
(acetyloxy)(phenyl)acetic acid + H2O
(S)-mandelic acid + (2R)-(acetyloxy)(phenyl)ethanoic acid
-
-
-
?
(acetyloxy)(phenyl)acetic acid + H2O
(S)-mandelic acid + (2R)-(acetyloxy)(phenyl)ethanoic acid
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
product determination by NMR and mass spectroscopy
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
highest activity (100%)
-
-
?
2-benzylcyclohex-1-en-1-yl acetate + H2O
2-benzylcyclohexanone + acetate
-
isoenzyme Est I, 99% conversion of substrate with 99% S-configuration of product
-
-
?
2-benzylcyclohex-1-en-1-yl acetate + H2O
2-benzylcyclohexanone + acetate
-
isoenzyme Est II, 11% conversion of substrate with R-configuration of product
-
-
?
2-n-pentylcyclohex-1-en-1-yl acetate + H2O
2-n-pentylcyclohexanone + acetate
-
isoenzyme Est I, 20% conversion of substrate with R-configuration of product
-
-
?
2-n-pentylcyclohex-1-en-1-yl acetate + H2O
2-n-pentylcyclohexanone + acetate
-
isoenzyme Est II, 16% conversion of substrate with S-configuration of product
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
about 40% activity compared to 1-naphthyl acetate
-
-
?
2-O-acetyl 4-nitrophenyl beta-D-xylopyranoside + H2O
?
-
-
-
-
?
2-t-butylcyclohex-1-en-1-yl acetate + H2O
2-t-butylcyclohexanone + acetate
-
isoenzyme Est I, 21% conversion of substrate with S-configuration of product
-
-
?
2-t-butylcyclohex-1-en-1-yl acetate + H2O
2-t-butylcyclohexanone + acetate
-
isoenzyme Est II, 20% conversion of substrate with R-configuration of product
-
-
?
3,6-diacetylmorphine + H2O
morphine + acetate
-
i.e. heroin, rapid spontaneous hydrolysis of the instable 3-acetyl group
-
?
3,6-diacetylmorphine + H2O
morphine + acetate
-
i.e. heroin, rapid spontaneous hydrolysis of the instable 3-acetyl group
-
?
3-O-acetyl 4-nitrophenyl beta-D-xylopyranoside + H2O
?
-
-
-
-
?
3-O-methyl-D-glucopyranoside + vinyl acetate
6-O-acetyl-3-O-methyl-D-glucopyranoside + vinyl alcohol
-
-
-
-
?
3-O-methyl-D-glucopyranoside + vinyl acetate
6-O-acetyl-3-O-methyl-D-glucopyranoside + vinyl alcohol
-
-
-
-
?
4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
-
-
-
-
?
4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
-
-
-
-
?
4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
-
-
-
-
?
4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
serine esterase activity
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
determination of specific activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
product determination by NMR and mass spectroscopy
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
highest activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
highest activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
highest activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
5 min, 30°C, pH 5.8, for kinetic analyses: 0.05-5 mM substrate in 100 mM sodium phosphate buffer
analysis by spectrophotometry at 410 nm
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
5 min, 30°C, pH 5.8
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
-
-
?
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside + H2O
?
-
-
-
-
?
6-acetylmorphine + H2O
morphine + acetate
-
substrate specificity
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
EST1, non-denaturating PAGE, pH7.4
zymogram analyses using Fast Blue PR salt
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
EST1, non-denaturating PAGE, pH7.4
zymogram analyses using Fast Blue PR salt
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
15 min, 50°C, pH 6.5
-
-
?
astragaloside I + H2O
astragaloside IV + ?
-
-
i.e. 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol
-
?
astragaloside I + H2O
astragaloside IV + ?
-
-
i.e. 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol
-
?
astragaloside II + H2O
astragaloside IV + ?
-
-
i.e. 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol
-
?
astragaloside II + H2O
astragaloside IV + ?
-
-
i.e. 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol
-
?
beta-naphthyl acetate + H2O
beta-naphthol + acetate
-
sucrose density gradient cell fractions from Hep-G2 and RINm5F cells, pH 8
SDS-PAGE and in gel-zymography
-
?
cellulose acetate + H2O
cellulose + acetate
-
also in form of acetylated starch, water-soluble and water-insoluble substrate, specific for acetyl substituents at the C2- and C3-positions, C6-acetyl is not hydrolyzed
-
?
D-galactose + vinyl acetate
? + vinyl alcohol
-
isozyme CE2B shows 22% transacetylation conversion, isozyme CE2A shows 48% transacetylation conversion
-
-
?
D-galactose + vinyl acetate
? + vinyl alcohol
-
isozyme CE2B shows 89% transacetylation conversion
-
-
?
D-glucopyranosyl beta-(1,3)-xylopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
D-glucopyranosyl beta-(1,3)-xylopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
D-glucopyranosyl beta-(1,4)-xylopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
D-glucopyranosyl beta-(1,4)-xylopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
D-glucose + vinyl acetate
6-O-acetyl-D-glucopyranose + vinyl alcohol
-
isozyme CE2B shows 31% transacetylation conversion, isozyme CE2A shows 25% transacetylation conversion
-
-
?
D-glucose + vinyl acetate
6-O-acetyl-D-glucopyranose + vinyl alcohol
-
isozyme CE2B shows 86% transacetylation conversion
-
-
?
D-mannose + vinyl acetate
6-O-acetyl-D-mannopyranose + vinyl alcohol
-
isozyme CE2B shows 46% transacetylation conversion, isozyme CE2A shows 26% transacetylation conversion
-
-
?
D-mannose + vinyl acetate
6-O-acetyl-D-mannopyranose + vinyl alcohol
-
isozyme CE2B shows 71% transacetylation conversion
-
-
?
D-xylopyranosyl beta-(1,4)-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
D-xylopyranosyl beta-(1,4)-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
ethyl acetate + H2O
ethanol + acetate
-
25°C, 1 h, pH 7, 7 mM MgCl2, cell extracts
-
-
?
isoastragaloside I + H2O
astragaloside IV + ?
-
-
i.e. 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol
-
?
isoastragaloside I + H2O
astragaloside IV + ?
-
-
i.e. 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol
-
?
isoastragaloside II + H2O
astragaloside IV + ?
-
-
i.e. 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol
-
?
isoastragaloside II + H2O
astragaloside IV + ?
-
-
i.e. 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol
-
?
methyl 2,3-O-diacetyl-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl 2,4-O-diacetyl-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl 2-O-methyl-beta-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
methyl 2-O-methyl-beta-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
methyl 3,4-O-diacetyl-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl 4-O-methyl-alpha-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
methyl 4-O-methyl-alpha-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
methyl alpha-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
methyl alpha-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
methyl beta-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
methyl beta-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
O-acetyl-1,4-beta-xylooligosaccharide + H2O
1,4-beta-xylooligosaccharide + acetic acid
-
-
-
ir
O-acetyl-1,4-beta-xylooligosaccharide + H2O
1,4-beta-xylooligosaccharide + acetic acid
-
-
-
-
ir
O-acetyl-4-O-methyl-D-glucurono-D-xylan + H2O
4-O-methyl-D-glucurono-D-xylan + acetic acid
-
-
-
-
?
O-acetyl-4-O-methyl-D-glucurono-D-xylan + H2O
4-O-methyl-D-glucurono-D-xylan + acetic acid
-
-
-
ir
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
EST1, pH 7.4, 20°C, 0.5% (w/v) Triton X-100, 0.125% (w/v) Arabic gum
spectrophotometry, 400 nm
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
10 min, 50°C, pH 6.5
-
-
?
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoate
-
-
-
-
?
p-nitrophenyl propionate + H2O
p-nitrophenol + propionate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
sucrose density gradient cell fractions from Hep-G2 and RINm5F cells, pH 8, 3 min, 1 mM CaCl2 or 5 mM EDTA
spectrophotometry, absorbance at 270 nm
-
?
tributyrin + H2O
?
-
EST1, pH 8, 20°C, 0.5% (w/v) Triton X-100, 0.125% (w/v) Arabic gum
titration assay
-
?
xanthan + H2O
?
the enzyme removes 57% of all acetyl groups present in xanthan after a 72 h incubation which corresponds to the removal of about 70% of all acetyl groups positioned on the inner mannose unit
-
-
?
xanthan + H2O
?
the enzyme removes 57% of all acetyl groups present in xanthan after a 72 h incubation which corresponds to the removal of about 70% of all acetyl groups positioned on the inner mannose unit
-
-
?
additional information
?
-
-
enzyme has receptor-destroying enzyme function
-
?
additional information
?
-
-
substrate specificity and regioselectivity, deacetylation activity of the enzyme is not restricted to polymers with beta-1,4 glycosidic bonds, no activity with cellulose sulfate, the enzyme enhances endoglucanase, but is itself not influenced by endoglucanase
-
?
additional information
?
-
-
the enzyme, feruloyl esterase AoFae, behaves as a non-specific acetyl esterase rather than a feruloyl esterase, with a preference for 2-O-acetyl-beta-D-xylopyranoside, AoFae shows only a very weak activity on feruloyl esters
-
-
-
additional information
?
-
-
1-(4-fluorophenyl)-1-(trifluoromethyl)prop-2-yn-1-yl acetate, 1-(4-chlorophenyl)-1-(trifluoromethyl)prop-2-yn-1-yl acetate, 1-(4-methylphenyl)-1-(trifluoromethyl)prop-2-yn-1-yl acetate, 1-(3-fluorophenyl)-1-(trifluoromethyl)prop-2-yn-1-yl acetate, 1-(3,4-difluorophenyl)-1-(trifluoromethyl)prop-2-yn-1-yl acetate are substrates of double mutant E188W/M193C, conversion with inversed enantioselectivity
-
-
-
additional information
?
-
-
1-phenyl-1-(trifluoromethyl)but-2-yn-1-yl acetate and 1-phenyl-1-(trifluoromethyl)prop-2-en-1-yl acetate are no substrates of neither wild-type nor any mutant
-
-
-
additional information
?
-
-
size of residue at position 188 (from Asp to Trp) determines enantioselectivity and -preference
-
-
-
additional information
?
-
-
no transacetylation occurs with vinyl acetate and D-xylose, xylobiose, methyl 6-O-methyl-alpha-D-glucopyranoside, 6-O-methyl D-glucopyranose, and methyl beta-D-xylopyranoside
-
-
-
additional information
?
-
-
the enzyme shows a strong preference for deacetylation of the 6-position in aldohexoses. Xylose and xylooligosaccharides do not serve as acetyl group acceptors
-
-
-
additional information
?
-
-
removal of acetyl group in 3-position of beta-lactams with 98% conversion and 91-93% product yield
-
-
-
additional information
?
-
-
the enzyme deacetylates cereal products like water soluble polysaccharides such as ragi, wheat, larch wood xylan, and gum karaya, the enzyme cleaves the acetyl groups substituted at O-2/O-3 of the xylan backbone of arabinoxylans and is known to modulate their functional properties
-
-
-
additional information
?
-
-
activated Sepharose CL6B-bound activity, pH 8
-
-
-
additional information
?
-
-
no transacetylation occurs with vinyl acetate and D-xylose, xylobiose, methyl 6-O-methyl-alpha-D-glucopyranoside, 6-O-methyl D-glucopyranose, and methyl beta-D-xylopyranoside
-
-
-
additional information
?
-
-
the enzyme shows a strong preference for deacetylation of the 6-position in aldohexoses. Xylose and xylooligosaccharides do not serve as acetyl group acceptors
-
-
-
additional information
?
-
-
activity of EST1 only on short chain triglyceride substrates
-
-
-
additional information
?
-
-
EST2 shows lower activity and enantioselectivity towards (R,S)-1,2-O-isopropylidene glycol acetate as substrate than EST1
-
-
-
additional information
?
-
-
no activity of EST1 on p-nitrophenyl butyrate, p-nitrophenyl caproate, p-nitrophenyl caprylate, p-nitrophenyl laurate and p-nitrophenyl palmitate
-
-
-
additional information
?
-
-
no activity of EST1 on triacylglyceride esters tricaprylin and triolein
-
-
-
additional information
?
-
-
activity of EST1 only on short chain triglyceride substrates
-
-
-
additional information
?
-
-
EST2 shows lower activity and enantioselectivity towards (R,S)-1,2-O-isopropylidene glycol acetate as substrate than EST1
-
-
-
additional information
?
-
-
no activity of EST1 on p-nitrophenyl butyrate, p-nitrophenyl caproate, p-nitrophenyl caprylate, p-nitrophenyl laurate and p-nitrophenyl palmitate
-
-
-
additional information
?
-
-
no activity of EST1 on triacylglyceride esters tricaprylin and triolein
-
-
-
additional information
?
-
-
the enzyme does not attack the 3-O-acetyl group of xylopyranosyl residues carrying 4-O-methyl-D-glucuronic acid at position 2
-
-
-
additional information
?
-
-
the enzyme does not attack the 3-O-acetyl group of xylopyranosyl residues carrying 4-O-methyl-D-glucuronic acid at position 2
-
-
-
additional information
?
-
-
the enzyme has no activity toward 4-nitrophenyl valerate, 4-nitrophenyl caproate, 4-nitrophenyl palmitate, 4-nitrophenyl benzoate, 4-nitrophenyl phosphate, methyl benzoate, methyl 4-hydroxybenzoate, or methyl cyclohexane-1-carboxylate
-
-
-
additional information
?
-
no activity with 1-naphthyl phosphate, 4-methylumbelliferyl phosphate, linalyl acetate, alpha-terpinyl acetate, glyceryl trioleate, fish oil, or olive oil
-
-
-
additional information
?
-
-
no activity with 1-naphthyl phosphate, 4-methylumbelliferyl phosphate, linalyl acetate, alpha-terpinyl acetate, glyceryl trioleate, fish oil, or olive oil
-
-
-
additional information
?
-
-
no activity on p-nitrophenyl-beta-D-xylopyranoside and p-nitrophenyl-alpha-L-arabinofuranoside and no xylanolytic activity
-
-
-
additional information
?
-
-
no activity with 4-nitrophenyl octanoate. The enzyme does not exhibit de-esterification activity toward an acetylated xylooligosaccharide extracted from hot-water treated eucalyptus
-
-
-
additional information
?
-
-
the enzyme has no activity with acetylated xylans
-
-
-
additional information
?
-
-
no activity is detected on xylan or acetylated xylan or N-acetyl-D-glucosamine
-
-
-
additional information
?
-
new family of microbial esterases with hemicellulase activity for biodegradation of lignocellulose, complementary activity to acetylxylan esterase Axe1
-
-
-
additional information
?
-
-
acetylesterases generally prefer aliphatic substrates involving acetic acid
-
-
-
additional information
?
-
-
isoamyl acetate and ethyl acetate-synthesizing esterase activities in mutant strain 100fold less than respective acetate ester-hydrolysing esterase activities
-
-
-
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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
geraniol acetate + H2O
geraniol + acetate
-
enzyme plays a role in geraniol production and improving palmarosa oil quality during florescence development
-
?
additional information
?
-
-
enzyme has receptor-destroying enzyme function
-
?
additional information
?
-
A7J2C6
new family of microbial esterases with hemicellulase activity for biodegradation of lignocellulose, complementary activity to acetylxylan esterase Axe1
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe3+
Mn2+
Zn2+
additional information
additional information
-
10 mM Ca2+, Co2+, Mg2+ or Mn2+ without any affect on acetyl esterase activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-xylose
at low concentrations of 1-5 mM, altered activity with 4-nitrophenyl acetate as substrate
phenyl methylsulfonyl fluoride
-
10 mM, 50% decreased acetyl esterase activity
SDS
-
complete inhibition, 1% (w/v), short-term incubation, EST1, p-nitrophenyl acetate as substrate
Sn2+
-
0.1 mM, 93% residual activity, EST1, p-nitrophenyl acetate as substrate
Ca2+
-
10 mM, 92% residual activity, EST1, p-nitrophenyl acetate as substrate
Co2+
-
10 mM, 56% residual activity, EST1, p-nitrophenyl acetate as substrate
Cu2+
-
complete inhibition, 10 mM, EST1, p-nitrophenyl acetate as substrate
EDTA
-
strong inhibitor, 10 mM, 18% residual activity, EST1, p-nitrophenyl acetate as substrate
Fe2+
-
0.1 mM, 70% residual activity, EST1, p-nitrophenyl acetate as substrate
Fe3+
-
0.1 mM, 93% residual activity, EST1, p-nitrophenyl acetate as substrate
Hg2+
-
strong inhibitor, 10 mM, 9% residual activity, EST1, p-nitrophenyl acetate as substrate
K+
-
10 mM, 70% residual activity, EST1, p-nitrophenyl acetate as substrate
Mg2+
-
10 mM, 80% residual activity, EST1, p-nitrophenyl acetate as substrate
Mn2+
-
10 mM, 60% residual activity, EST1, p-nitrophenyl acetate as substrate
Zn2+
-
complete inhibition, 10 mM, EST1, p-nitrophenyl acetate as substrate
additional information
-
10 mM ethylmethylaminopropyl carbodiimide or iodacetamide without effect on acetyl esterase activity
-
additional information
rates of hydrolysis of 4-nitrophenyl acetate by the purified Aes1 are inhibited by low concentrations (1.0 to 5.0 mM) but significantly enhanced by high concentrations (10.0 to 500 mM) of D-xylose
-
additional information
-
no inhibition by 4-chloromercuribenzoate, thiamethoxam, malathion and methyl-parathion
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
benzethonium chloride
-
i.e. (diisobutyl phenoxyethoxyethyl) dimethyl benzylammonium chloride, up to 2.5fold enhancement of activity
cellobiose
enhanced activity with 4-nitrophenyl acetate as substrate
D-galactose
enhanced activity with 4-nitrophenyl acetate as substrate
D-glucose
1% (w/v), enhanced activity with 4-nitrophenyl acetate as substrate
D-xylose
at high concentrations of 10-500 mM, enhanced activity with 4-nitrophenyl acetate as substrate
xylooligosaccharide
50 mM, enhanced activity with 4-nitrophenyl acetate as substrate
additional information
not influenced by olive oil, methyl acetate and Tween-80
-
additional information
no influence on activity on 4-nitrophenyl acetate as substrate by L-arabinose, mannose, lactose; rates of hydrolysis of 4-nitrophenyl acetate by the purified Aes1 are inhibited by low concentrations (1.0 to 5.0 mM) but significantly enhanced by high concentrations (10.0 to 500 mM) of D-xylose; sodium acetate at concentrations below 100 mM does not inhibit the hydrolysis, higher concentrations inhibit the reactions; using 4-nitrophenyl acetate as substrate the activity of the recombinant enzyme is enhanced by D-xylose, D-glucose, cellobiose, D-galactose, and xylooligosaccharides but not by arabinose, mannose, or lactose
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anemia
Deletions in the Highly Polymorphic Region (HPR) of Infectious Salmon Anaemia Virus HPR0 haemagglutinin-esterase enhance viral fusion and influence the interaction with the fusion protein.
Anemia
Dual Mutation Events in the Haemagglutinin-Esterase and Fusion Protein from an Infectious Salmon Anaemia Virus HPR0 Genotype Promote Viral Fusion and Activation by an Ubiquitous Host Protease.
Anemia
Sequence analysis of the fusion protein gene from infectious salmon anemia virus isolates: evidence of recombination and reassortment.
Cysts
An Arabidopsis thaliana pectin acetylesterase gene is upregulated in nematode feeding sites induced by root-knot and cyst nematodes.
Encephalomyelitis
Isolation and characterization of the acetylesterase of hemagglutinating encephalomyelitis virus (HEV).
Hepatitis
Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein.
Infections
Bovine coronavirus uses N-acetyl-9-O-acetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells.
Influenza, Human
Antigenic and genetic analyses of eight influenza C strains isolated in various areas of Japan during 1985-9.
Influenza, Human
Characterization of antigenically unique influenza C virus strains isolated in Yamagata and Sendai cities, Japan, during 1992-1993.
Influenza, Human
Construction of an antigenic map of the haemagglutinin-esterase protein of influenza C virus.
Influenza, Human
Effect of anti-haemagglutinin-esterase glycoprotein monoclonal antibodies on the receptor-destroying activity of influenza C virus.
Influenza, Human
Frequent occurrence of genetic reassortment between influenza C virus strains in nature.
Influenza, Human
Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses.
Influenza, Human
Influenza C virus esterase: analysis of catalytic site, inhibition, and possible function.
Influenza, Human
Phylogenetic analysis of influenza C virus nonstructural (NS) protein genes and identification of the NS2 protein.
Influenza, Human
Role of individual oligosaccharide chains in antigenic properties, intracellular transport, and biological activities of influenza C virus hemagglutinin-esterase protein.
Influenza, Human
Serine 71 of the glycoprotein HEF is located at the active site of the acetylesterase of influenza C virus.
Influenza, Human
Surface glycoprotein of influenza C virus: inactivation and restoration of the acetylesterase activity on nitrocellulose.
Influenza, Human
The glycoprotein of influenza C virus is the haemagglutinin, esterase and fusion factor.
Influenza, Human
The receptor-destroying enzyme of influenza C virus is required for entry into target cells.
Influenza, Human
Transfer of an esterase-resistant receptor analog to the surface of influenza C virions results in reduced infectivity due to aggregate formation.
Nematode Infections
An Arabidopsis thaliana pectin acetylesterase gene is upregulated in nematode feeding sites induced by root-knot and cyst nematodes.
Vaccinia
Substitution of 4-(2-hydroxyethyl)-1-piperazineethane sulfonic acid (HEPES) for bicarbonate in protein-free animal cell culture medium: application to vaccinia virus quantitation and fluorogenic acetylesterase assay in living LM cells.
Vaccinia
The JHM strain of mouse hepatitis virus induces a spike protein-specific Db-restricted cytotoxic T cell response.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
(R)-1,2-O-isopropylidene glycol acetate
-
EST1, after preparative electrophoresis
1.87
2-isopropylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35°C
0.09
2-methylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35°C
0.54
2-n-propylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35°C
4.42
2-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
3.6
2-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70°C
1.55
3-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
4.2
3-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70°C
0.137
4-nitrophenyl propionate
-
in 50 mM citrate-phosphate (pH 6) at 70°C
4
4-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70°C
0.06
2-benzylcyclohex-1-en-1-yl acetate
-
isoenzyme Est II, pH 7.0, 35°C
0.97
2-benzylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35°C
0.3
2-n-pentylcyclohex-1-en-1-yl acetate
-
isoenzyme Est II, pH 7.0, 35°C
0.72
2-n-pentylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35°C
2.01
2-t-butylcyclohex-1-en-1-yl acetate
-
isoenzyme Est II, pH 7.0, 35°C
2.54
2-t-butylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35°C
0.23
4-nitrophenyl acetate
30°C, pH 5.8; purified recombinant enzyme, 30°C, pH 5.8
1.4
4-nitrophenyl acetate
-
mutant enzyme D179A, at pH 5.5 and 50°C
1.8
4-nitrophenyl acetate
-
mutant enzyme H182A, at pH 5.5 and 50°C
4.7
4-nitrophenyl acetate
-
mutant enzyme C16A, at pH 5.5 and 50°C
5.1
4-nitrophenyl acetate
-
mutant enzyme S10A, at pH 5.5 and 50°C
0.057
4-nitrophenyl butyrate
-
mutant enzyme L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.069
4-nitrophenyl butyrate
-
mutant enzyme L97F/L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.13
4-nitrophenyl butyrate
mutant enzyme R48E, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.14
4-nitrophenyl butyrate
mutant enzyme R48K, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.16
4-nitrophenyl butyrate
wild type enzyme, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.17
4-nitrophenyl butyrate
-
wild type enzyme, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.18
4-nitrophenyl butyrate
mutant enzyme R48A, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.19
4-nitrophenyl butyrate
mutant enzyme R48S, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.26
4-nitrophenyl butyrate
-
mutant enzyme L97F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
1.24
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
2.46
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
4.31
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2C, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
32.5
p-nitrophenyl acetate
-
pH 7.0, 25°C, presence of benzethonium chloride
0.015
tributyrin
mutant enzyme R48S, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.018
tributyrin
mutant enzyme R48A, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.047
tributyrin
mutant enzyme R48K, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.052
tributyrin
wild type enzyme, in 20 mM phosphate buffer (pH 7.1), at 30°C
0.073
tributyrin
mutant enzyme R48E, in 20 mM phosphate buffer (pH 7.1), at 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14
2-isopropylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35°C
79
2-n-propylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35°C
41.6
2-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
76.1
2-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70°C
2101
3-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
70.1
3-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70°C
41.3
4-nitrophenyl propionate
-
in 50 mM citrate-phosphate (pH 6) at 70°C
78.6
4-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70°C
additional information
4-nitrophenyl-beta-D-xylopyranoside monoacetate
initial rate ratio between 2-, 3-, and 4-O-acetyl 4-nitrophenyl-beta-D-xylopyranoside is 1:19:17.7
26
2-n-pentylcyclohex-1-en-1-yl acetate
-
isoenzyme Est II, pH 7.0, 35°C
42
2-n-pentylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35°C
17
2-t-butylcyclohex-1-en-1-yl acetate
-
isoenzyme Est II, pH 7.0, 35°C
21.8
4-nitrophenyl acetate
-
mutant enzyme S10A, at pH 5.5 and 50°C
26.2
4-nitrophenyl acetate
-
mutant enzyme C16A, at pH 5.5 and 50°C
36.3
4-nitrophenyl acetate
-
mutant enzyme D179A, at pH 5.5 and 50°C
38.8
4-nitrophenyl acetate
-
mutant enzyme H182A, at pH 5.5 and 50°C
29
4-nitrophenyl butyrate
mutant enzyme R48K, in 20 mM phosphate buffer (pH 7.1), at 30°C; wild type enzyme, in 20 mM phosphate buffer (pH 7.1), at 30°C
29
4-nitrophenyl butyrate
-
wild type enzyme, in 20 mM phosphate buffer, at pH 7.1 and 30°C
29.8
4-nitrophenyl butyrate
-
wild type enzyme, at pH 5.5 and 50°C
37
4-nitrophenyl butyrate
-
mutant enzyme L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
78
4-nitrophenyl butyrate
mutant enzyme R48E, in 20 mM phosphate buffer (pH 7.1), at 30°C
86
4-nitrophenyl butyrate
mutant enzyme R48S, in 20 mM phosphate buffer (pH 7.1), at 30°C
113
4-nitrophenyl butyrate
mutant enzyme R48A, in 20 mM phosphate buffer (pH 7.1), at 30°C
240
4-nitrophenyl butyrate
-
mutant enzyme L97F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
340
4-nitrophenyl butyrate
-
mutant enzyme L97F/L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
241.6
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2C, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
1331
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
3210
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
6.2
tributyrin
wild type enzyme, in 20 mM phosphate buffer (pH 7.1), at 30°C
6.9
tributyrin
mutant enzyme R48K, in 20 mM phosphate buffer (pH 7.1), at 30°C
9.3
tributyrin
mutant enzyme R48E, in 20 mM phosphate buffer (pH 7.1), at 30°C
17.4
tributyrin
mutant enzyme R48A, in 20 mM phosphate buffer (pH 7.1), at 30°C
17.5
tributyrin
mutant enzyme R48S, in 20 mM phosphate buffer (pH 7.1), at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.42
2-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
21.1
2-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70°C
1356
3-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
16.7
3-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70°C
301.5
4-nitrophenyl propionate
-
in 50 mM citrate-phosphate (pH 6) at 70°C
19.7
4-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70°C
4.2
4-nitrophenyl acetate
-
mutant enzyme S10A, at pH 5.5 and 50°C
5.4
4-nitrophenyl acetate
-
mutant enzyme C16A, at pH 5.5 and 50°C
20.7
4-nitrophenyl acetate
-
mutant enzyme H182A, at pH 5.5 and 50°C
24.8
4-nitrophenyl acetate
-
mutant enzyme D179A, at pH 5.5 and 50°C
0.057
4-nitrophenyl butyrate
-
mutant enzyme L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.069
4-nitrophenyl butyrate
-
mutant enzyme L97F/L209F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.17
4-nitrophenyl butyrate
-
wild type enzyme, in 20 mM phosphate buffer, at pH 7.1 and 30°C
0.26
4-nitrophenyl butyrate
-
mutant enzyme L97F, in 20 mM phosphate buffer, at pH 7.1 and 30°C
56.08
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2C, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
541.5
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
2599
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000225
-
mutant strain, ethyl acetate-hydrolysing esterase (EAHase) activity
0.000236
-
mutant strain, isoamyl acetate-hydrolysing esterase (IAHase) activity
0.000342
-
wild-type strain, ethyl acetate-hydrolysing esterase (EAHase) activity
0.000347
-
wild-type strain, isoamyl acetate-hydrolysing esterase (IAHase) activity
0.21
4-nitrophenyl acetate, over-expression culture supernatant; recombinant enzyme, culture supernatant
1.12
recombinant enzyme, after DEAE FF column, 4-nitrophenyl acetate
3
-
isozyme CE2C, using 6-O-acetyl-D-mannopyranose as substrate, pH 6.0, 40°C; isozyme CE2C, using methyl 3,4-O-diacetyl-beta-D-xylopyranoside as substrate, pH 6.0, 40°C
4
-
isozyme CE2B, using methyl 3,4-O-diacetyl-beta-D-xylopyranoside as substrate, pH 6.0, 40°C
5.64
-
with 4-nitrophenyl 4-O-acetyl-beta-D-xylopyranoside as substrate, at pH 6.0 and 35°C
8
-
isozyme CE2, using methyl 3,4-O-diacetyl-beta-D-xylopyranoside as substrate, pH 6.0, 40°C
10.3
-
with 4-nitrophenyl 2-O-acetyl-beta-D-xylopyranoside as substrate, at pH 6.0 and 35°C
13.3
-
with 4-nitrophenyl 3-O-acetyl-beta-D-xylopyranoside as substrate, at pH 6.0 and 35°C
20.5
4-nitrophenyl acetate, maximum velocity, purified recombinant enzyme, 30°C, pH 5.8
35
-
isozyme CE2, using 6-O-acetyl-D-mannopyranose as substrate, pH 6.0, 40°C
60
-
isozyme CE2C, using methyl 6-O-acetyl-beta-D-glucopyranoside as substrate, pH 6.0, 40°C
183
324
-
(R,S)-1,2-O-isopropylidene glycol acetate, EST1, after preparative electrophoresis
328
-
isozyme CE2B, using methyl 6-O-acetyl-beta-D-glucopyranoside as substrate, pH 6.0, 40°C
395
-
isozyme CE2B, using 6-O-acetyl-D-mannopyranose as substrate, pH 6.0, 40°C
additional information
2
-
isozyme CE2C, using methyl 2,4-O-diacetyl-beta-D-xylopyranoside as substrate, pH 6.0, 40°C
2
-
isozyme CE2, using methyl 2,4-O-diacetyl-beta-D-xylopyranoside as substrate, pH 6.0, 40°C
5
-
isozyme CE2B, using methyl 2,4-O-diacetyl-beta-D-xylopyranoside as substrate, pH 6.0, 40°C
183
-
isozyme CE2, using methyl 6-O-acetyl-beta-D-glucopyranoside as substrate, pH 6.0, 40°C
183
-
isozyme CE2, using methyl 6-O-acetyl-beta-D-glucopyranoside as substrate, pH 6.0, 40°C
additional information
-
isoforms with pI-values 4.2 and 5.0 are the most active ones in all samples
additional information
-
(R)-1,2-O-isopropylidene glycol acetate, EST1, 1.0 micromol/min by activity corresponding to synthesis of 0.01 micromol p-nitrophenol/min/mg EST1; (R,S)-1,2-O-isopropylidene glycol acetate as substrate for EST1, 20 micromol/min by activity corresponding to synthesis of 0.01 micromol p-nitrophenol/min/mg EST1; (R,S)-1,2-O-isopropylidene glycol butyrate as substrate for EST1, 4.6 micromol/min by activity corresponding to synthesis of 0.01 micromol p-nitrophenol/min/mg EST1; (R,S)-1,2-O-isopropylidene glycol caproate as substrate for EST1, 0.7 micromol/min by activity corresponding to synthesis of 0.01 micromol p-nitrophenol/min/mg EST1; (S)-1,2-O-isopropylidene glycol acetate, EST1, 1.2 micromol/min by activity corresponding to synthesis of 0.01 micromol p-nitrophenol/min/mg EST1; triacetin as substrate for EST1, 4.06 micromol/min by activity corresponding to synthesis of 0.01 micromol p-nitrophenol/min/mg EST1; tributyrin as substrate for EST1, 2.8 micromol/min by activity corresponding to synthesis of 0.01 micromol p-nitrophenol/min/mg EST1
additional information
extremly low activities against 4-nitrophenyl formate, butyrate, or canoate
additional information
-
mutant strain, 61% lower ethyl acetate-hydrolysing esterase (EAHase) activity than in wild-type strain; mutant strain, 68% lower isoamyl acetate-hydrolysing esterase (IAHase) activity than in wild-type strain
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
7.5
7.5
9
-
EST1 sample after anion-exchange chromatography, p-nitrophenyl acetate as substrate, 20°C
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
inactive below, EST1 sample after anion-exchange chromatography, p-nitrophenyl acetate as substrate, 20°C, 4 h
6
-
85% residual activity, alpha-naphthyl acetate as substrate, more active in acetate buffer than phosphate buffer
7 - 9
-
about 35% activity at pH 7.0, 100% activity at pH 8.0, about 60% activity at pH 9.0, almost no activity below pH 6.0 and above pH 10.0
7 - 10
-
100% activity, EST1 sample after anion-exchange chromatography, p-nitrophenyl acetate as substrate, 20°C, 4 h
7 - 8.5
-
the enzyme retains about 90% and 88% of its maximal activity at pH 7.0 and 8.5, respectively
11
-
16% activity, EST1 sample after anion-exchange chromatography, p-nitrophenyl acetate as substrate, 20°C, 4 h
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
40
45
50
60
65
80
-
100% relative activity, at 60-70°C 90% relative activity, EST1 sample after anion-exchange chromatography, p-nitrophenyl acetate as substrate, pH 7, 3 min
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 45
-
within the temperature range of 30-45°C, the enzyme exhibits more than 95% of optimum activity, whereas at temperatures higher than 45°C, the activity sharply declines
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
all isoforms isolated have pI-values between 4.1 and 5.2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
different strains of respiratory and enteropathogenic viruses, bovine, isolated from nasal swab samples and lung tissues of feedlot cattle with acute respiratory tract disease, the viruses exhibiting distinct phenotype features from enteropathogenic bovine coronaviruses
-
-
brenda
finger millet, also known as ragi, indigenous minor millet in india
-
-
brenda
formerly termed Chrysosporium lucknowense C1
UniProt
brenda
formerly termed Chrysosporium lucknowense C1
UniProt
brenda
wild-type strain NBRC and EAL-6, a low-respiratory, petite mutant of strain NBRC
-
-
brenda
anamorph Trichoderma reesei, strain Rut-C30 (hypercellulolytic mutant of Trichoderma reesei QM 6a); Trichoderma reesei strain ATCC 56765
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
ubiquitous transcript of ca. 2.4 kb, highest gene expression level in liver, placenta and heart, Northern blot
brenda
-
ubiquitous transcript of ca. 2.4 kb, highest gene expression level in liver and kidney, Northern blot
brenda
-
lower expression level than in Hep-G2 cells as revealed by Northern blot and quantitative RT-PCR, serum-induced inhibition of gene expression (quantitative RT-PCR, FACS, reporter gene assay)
brenda
-
strong expression, lower expression level than in liver as revealed by Northern blot and quantitative RT-PCR, cell fractionation, FACS analysis
brenda
-
spikelets, maximal in immature florescences, isozyme Est-B is increased during development, activity of isozymes at different developmental stages, overview
brenda
-
lower expression level than in liver as revealed by Northern blot and quantitative RT-PCR, Western blot, strong in glomeruli and tubular structures according to cytochemistry and confocal microscopy
brenda
-
no expression in granulocytes and lymphocytes according to cell surface domain-specific FACS analyses
brenda
-
highest expression level as revealed by Northern blot and quantitative RT-PCR, Western blot, cytochemistry and confocal microscopy
brenda
high transcript level induced by 4 mM sophorose, 1% (w/v) cellulose, 1% (w/v) oat spelt xylan, or 1% (w/v) lactose, significant transcript levels induced by 1% (w/v) L-arabinose, low transcript levels induced by acetic acid (4 mM sodium acetate, 1% (w/v) glycerol), revealed by Northern blot
brenda
-
highest expression within pancreatic tissue at the islets of Langerhans, revealed by cytochemistry and confocal microscopy
brenda
-
high expression on monocytes according to cell-surface domain-specific FACS analyses
brenda
-
kidney, cytochemistry and confocal microscopy
brenda
-
cells were grown with different carbohydrate sources: birch wood xylan, birch wood, beech wood xylan, beech wood, wheat arabinoxylan, wheat bran, wheat straw, rape straw, oat spelt, olive oil, and triacetin
brenda
-
cells were grown with different carbohydrate sources: birch wood xylan, birch wood, beech wood xylan, beech wood, wheat arabinoxylan, wheat bran, wheat straw, rape straw, oat spelt, olive oil, and triacetin
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
heavy membrane after sucrose density gradient cell fractionation on Hep-G2 (full-length protein and 32 kDa variant) and RINm5F cells (full-length protein)
-
brenda
-
32 kDa low molecular weight variant, sucrose density gradient cell fractionation on RINm5F cells
brenda
additional information
-
C-terminus of full-length protein (residues 62-416) as revealed by cell surface domain-specific FACS analyses on monocytes and Hep-G2 cells as well as cell surface domain-specific cytochemistry and confocal microscopy on liver, kidney, and pancreas, detection by ELISA in urine and supernatant of thrombin-treated Hep-G2 cells
-
brenda
; 19 N-terminal residues serve as signal peptide for secretion
-
brenda
additional information
-
viruses are located in the cytoplasm and at perinuclear sites in the transfected COS-7 cells
-
brenda
additional information
-
not detectable by ELISA using cell surface domain-specific antibody
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
the enzyme exhibits the capability to solubilize in vitro beech wood to release water-soluble lignin fragments with molecular masses of 1000-3000xa0Da
metabolism
-
the enzyme exhibits the capability to solubilize in vitro beech wood to release water-soluble lignin fragments with molecular masses of 1000-3000xa0Da
-
physiological function
Salmonella enterica serovar Typhi Vi phage I
-
a conserved acetyl esterase domain targets bacteriophages to the Vi capsular receptor of Salmonella enterica serovar Typhi
physiological function
Salmonella enterica serovar Typhi Vi phage III
-
a conserved acetyl esterase domain targets bacteriophages to the Vi capsular receptor of Salmonella enterica serovar Typhi
physiological function
Salmonella enterica serovar Typhi Vi phage IV
-
a conserved acetyl esterase domain targets bacteriophages to the Vi capsular receptor of Salmonella enterica serovar Typhi
physiological function
Salmonella enterica serovar Typhi Vi phage V
-
a conserved acetyl esterase domain targets bacteriophages to the Vi capsular receptor of Salmonella enterica serovar Typhi
physiological function
Salmonella enterica serovar Typhi Vi phage VI
-
a conserved acetyl esterase domain targets bacteriophages to the Vi capsular receptor of Salmonella enterica serovar Typhi
physiological function
Salmonella enterica serovar Typhi Vi phage VII
-
a conserved acetyl esterase domain targets bacteriophages to the Vi capsular receptor of Salmonella enterica serovar Typhi
physiological function
-
acetylesterase-mediated deacetylation of pectin impairs cell elongation, pollen germination, and plant reproduction. Plants overexpressing PAE1 exhibit severe male sterility, by affecting the development of pollen grains and the capsule, and reduces acetyl content in the pectin of transgenic plants
physiological function
-
the enzyme is involved in biotic and abiotic stress tolerance
physiological function
the enzyme deacetylates oligosaccharides in the plant cell wall
physiological function
Trichoderma reesei anamorph Trichoderma reesei
-
the enzyme deacetylates oligosaccharides in the plant cell wall
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence