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Enzyme Nomenclature
Information on EC 3.1.1.6 - acetylesterase
for references in articles please use BRENDA:EC3.1.1.6
Word Map on EC 3.1.1.6
- 3.1.1.6
-
esterases
- xylans
-
deacetylation
-
receptor-destroying
- acetylxylan
- hemagglutinin-esterase
-
glucuronoyl
- isavs
- coronaviruses
-
carbohydrate-active
-
beta-naphthyl
-
cazymes
-
alpha-naphthyl
-
9-o-acetylated
-
saccharification
-
hemicellulolytic
- orthomyxoviridae
-
lignin-carbohydrate
-
n-acetyl-9-o-acetylneuraminic
-
reassortment
- xylooligosaccharides
- glucuronoxylans
-
xylopyranosyl
- industry
-
4-o-methyl-d-glucuronic
- analysis
- synthesis
- molecular biology
- paper production
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.1.1.6
-
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RECOMMENDED NAME
GeneOntology No.
acetylesterase
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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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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
-
-
wild-type strain NBRC and EAL-6, a low-respiratory, petite mutant of strain NBRC
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anamorph Trichoderma reesei, strain Rut-C30 (hypercellulolytic mutant of Trichoderma reesei QM 6a); Trichoderma reesei strain ATCC 56765
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
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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-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-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 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
-
-
?
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
-
-
-
?
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
-
?
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 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
-
-
?
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
-
-
-
?
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-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 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
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-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
-
?
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-O-methyl-beta-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
methyl 2-O-methyl-beta-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
-
-
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
no activity on p-nitrophenyl-beta-D-xylopyranoside and p-nitrophenyl-alpha-L-arabinofuranoside and no xylanolytic activity
-
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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+
Fe3+
Mn2+
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.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-xylose
at low concentrations of 1-5 mM, altered activity with 4-nitrophenyl acetate as substrate
K+
-
10 mM, 70% residual activity, EST1, p-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
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
8
-
isozyme CE2, using methyl 3,4-O-diacetyl-beta-D-xylopyranoside as substrate, pH 6.0, 40°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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
9
-
EST1 sample after anion-exchange chromatography, p-nitrophenyl acetate as substrate, 20°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 - 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
40
45
50
60
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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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
-
ubiquitous transcript of ca. 2.4 kb, highest gene expression level in liver and kidney, Northern blot
-
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)
-
strong expression, lower expression level than in liver as revealed by Northern blot and quantitative RT-PCR, cell fractionation, FACS analysis
-
spikelets, maximal in immature florescences, isozyme Est-B is increased during development, activity of isozymes at different developmental stages, overview
-
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
-
no expression in granulocytes and lymphocytes according to cell surface domain-specific FACS analyses
-
highest expression level as revealed by Northern blot and quantitative RT-PCR, Western blot, cytochemistry and confocal microscopy
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
-
highest expression within pancreatic tissue at the islets of Langerhans, revealed by cytochemistry and confocal microscopy
-
high expression on monocytes according to cell-surface domain-specific FACS analyses
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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)
-
-
32 kDa low molecular weight variant, sucrose density gradient cell fractionation on RINm5F cells
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
-
; 19 N-terminal residues serve as signal peptide for secretion
-
additional information
-
viruses are located in the cytoplasm and at perinuclear sites in the transfected COS-7 cells
-
additional information
-
not detectable by ELISA using cell surface domain-specific antibody
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus pumilus;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22500
-
2 * 27000, isoenzyme EstI, 2 * 22500, isoenzyme Est II, SDS-PAGE
27000
-
2 * 27000, isoenzyme EstI, 2 * 22500, isoenzyme Est II, SDS-PAGE
30000
32000
35000
36000
40000
42000
over-expression in Hypocrea jecorina Rut-C30, SDS-PAGE, molecular weight shift of purified recombinant enzyme (below theoretical weight) upon treatment with endoglycosidase H
45000
50000
65000
67000 - 68000
160000
30000
-
degradation product, Western blot, not detectable by cytosolic domain-specific antibody
32000
-
low molecular variant, membrane associated (Hep-G2 cell) or cytosolic (RINm5F cell), Western blot
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
multimer
tetramer
additional information
dimer
-
2 * 27000, isoenzyme EstI, 2 * 22500, isoenzyme Est II, SDS-PAGE
additional information
-
? * 23000, SDS-PAGE, AXE II; ? * 48000, SDS-PAGE, AXE I
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
additional information
-
residues C140, C149 and C409 with putative intra- and intermolecular disulfide bonds, in silico analysis
glycoprotein
N-glycosylation, sensitive to endoglycosidase H but not to O-glycosidase treatment, putative acceptor sites: N45, N146, N198, N204, N278
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
molecular dynamic simulations and automated docking with R and S enantiomers of substrate 1,1,1-trifluoro-2-phenyl-but-3-yn-1-yl acetate using structure of wild-type and structural model of double mutant E188W/M193C, S enantiomer fits better in active site of mutant E188W/M193C because subtrates phenyl group points out of it, docking of the preferred R enantiomer by the wild-type with lower free energy than docking of the S enantiomer
-
His-tagged protein, both in the native form and with selenomethionine substitution
-
structural superimposition of homology-generated model with Alicyclobacillus acidocaldarius EST2 and Escherichia coli beta-cystathionase MalY revealed nine amino acid consensus sequence putatively involved in protein-protein interactions, amino acids 178-184 are putative core of interaction with MalY and MalT
-
structural modelling using Cn3D 4.1 software and plant strictosidine synthase as model structure, six-bladed beta-propeller structure
-
purified selenomethionine enzyme, 6-7 mg/ml, pure or complexed with the inhibitor dimethylarsinic acid, crystal growth in 1.8 M ammonium sulfate, 0.1 M NaCl, 0.1 M cacodylate, pH 6.5, for crystallization of native methionine enzyme 1.7 M ammonium sulfate, 0.1 M NaCl, 0.1 M BES, pH 6.4, is used, X-ray structure determination and analysis at 1.3 A and 1.45 A resolution
-
hanging drop vapor diffusion method, using 20% (w/v) PEG-3000, 0.1 M HEPES pH 7.5, 0.2 M NaCl (selenomethionine-substituted enzyme) or nanodrop vapor diffusion method, using 0.2 M calcium acetate hydrate, 20% (w/v) PEG 3350, pH 7.3 at 20°C (native enzyme)
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.5
-
the enzyme is quite pH-stable over a broad range of pH 7.0-9.5, exhibiting a sharp decrease in activity below pH 4.5
730850
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
40 min, the transiently expressed respiratory viruses show significantly reduced activity, while the transiently expressed enteropathogenic viruses are stable
40 - 60
-
decreasing stability, EST1 sample after anion-exchange chromatography, p-nitrophenyl acetate as substrate, pH 7, 1 h
45
-
the deacetylation activity is quite thermostable in the range of 20-45°C, suffering a sharp decrease above 50?C
50
-
75% activity, EST1 sample after anion-exchange chromatography, p-nitrophenyl acetate as substrate, pH 7, 1 h
60
61
-
denaturation of Aes mutant V20D, thermal stability analysis at 20-90°C, differential scanning calorimetry and circular dichroism measurements, the irreversible inactivation process is more complex than a two-state transition
65
68
-
denaturation of Aes, thermal stability analysis at 20-90°C, differential scanning calorimetry and circular dichroism measurements, the irreversible inactivation process is more complex than a two-state transition
100
-
the enzyme is not stable at 100°C, resulting in a half-life of less than 5 min
65
-
t1/2 inactivation is 5 min for the wild-type enzyme, and 30 min for mutant T74A, thermal inactivation first-order kinetics, overview
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
dimethyl sulfoxide
dimethylformamide
Ethanol
Methanol
Acetone
-
15% (v/v), 48% residual activity, EST1, p-nitrophenyl acetate as substrate
Acetone
-
15% (v/v), 48% residual activity, EST1, p-nitrophenyl acetate as substrate
-
dimethyl sulfoxide
-
15% (v/v), 39% residual activity, EST1, p-nitrophenyl acetate as substrate
dimethyl sulfoxide
-
15% (v/v), 39% residual activity, EST1, p-nitrophenyl acetate as substrate
-
dimethylformamide
-
15% (v/v), 34% residual activity, EST1, p-nitrophenyl acetate as substrate
dimethylformamide
-
15% (v/v), 34% residual activity, EST1, p-nitrophenyl acetate as substrate
-
Ethanol
-
15% (v/v), 76% residual activity, EST1, p-nitrophenyl acetate as substrate
Ethanol
-
15% (v/v), 76% residual activity, EST1, p-nitrophenyl acetate as substrate
-
Methanol
-
15% (v/v), 82% residual activity, EST1, p-nitrophenyl acetate as substrate
Methanol
-
15% (v/v), 82% residual activity, EST1, p-nitrophenyl acetate as substrate
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
85% (NH4)2SO4-saturated bacterial protein extract to anion-exchange chromatography on DEAE-650 (S) column (gradient elution with 0-0.15 M NaCl), EST1 elution at 70 mM NaCl, EST2 elution at 90 mM NaCl, addition of (NH4)2SO4 (25% saturation) to EST1 fraction followed by hydrophobic interaction chromatography on phenyl Sepharose column, purification of main esterase activity (EST1) by elution with 10% (NH4)2SO4-saturated buffer, preparative electrophoresis (native)
-
after over-expression (up to 20fold activity) by liquid column chromatography, monitored by activity measurements, 300 mg recombinant enzyme from 1 litre culture; centrifugation at 4°C, liquid column chromatography
at 4°C, precipitation from culture filtrate by 40-80% (NH4)2SO4 saturation followed by anion-exchange (DEAE column, elution with 0-1 M NaCl gradient), t-butyl hydrophobic (elution with 1.7-0 M (NH4)2SO4 gradient) and hydroxyapatite chromatography (elution with 0.02-0.5 M sodium phosphate buffer, pH 6.8), stored at -20°C after addition of 20% glycerol
-
from bacterial extracts by binding to CNBr-activated Sepharose CL6B, 1.5 mg bound protein per ml resin, pH 8.3, 0.1 M sodium hydrogen carbonate, 0.5 M sodium chloride
-
from bacterial lysate or inclusion bodies by Superose 6 column chromatography in presence of 6-8 M urea for antibody generation, from insect cells by FPLC-based metal affinity chromatography (250 mM imidazole) and anion-exchange chromatography on Q-sepharose column for activity measurements
-
immobilized metal affinity chromatography
native enzyme from 72 h ragi malt 34fold by ammonium sulfate precipitation, anion exchange chromatography, gel filtration, and hydrophobic interaction chromatography, to homogeneity
-
nickel-chelating resin column chromatography and Superdex 200 gel filtration
-
Q-Sepharose column chromatography, phenyl Sepharose column chromatography, ceramic hydroxy-apatite column chromatography, and Resource Q column chromatography
-
recombinant from Escherichia coli as N-terminally His-tagged selenomethionine or methionine enzyme, removal of the His-tag
-
recombinant wild-type and mutant enzymes from strain BL21(DE3) by anion exchange and hydrophobic interaction chromatography, and gel filtration
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA of 1248 bp in pGEM-T-easy for sequencing (polymorphic residues at position 65, 282, 374, in middle European population homozygosity for R282 and R347) and subcloning, cDNA coding for residues 45-416 in pDEST15 or residues 58-416 in pGEX-1gammaT (yielding glutathione transferase-tag) for expression in Escherichia coli BL21, cDNA coding for residues 16-416 in pDEST10 for baculovirus-mediated expression in insect cell lines Sf9 and HighFive with N-terminal hexa-His-tag
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli DH5 alpha; from genomic DNA in pT3C to generate expression plasmid pTSP-TAE and transformation of Hypocrea jecorina Rut-C30
expression of the N-terminally His-tagged enzyme in Escherichia coli BL21(DE3)
-
respiratory and enteropathogenic coronaviruses, DNA and amino acid sequence determination and analysis, transient and functional expression in COS-7 cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the addition of ZnSO4 enhances enzyme production by 37%
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E188D
-
very low specific activity, R enantioselectivity of above 100, S enantioselectivity of 26, mutant generated using a focused directed-evolution approach based on saturation mutagenesis according to CASTing method
E188W
-
very low specific activity similar to mutant M193C, S enantioselectivity of 26
E188W/M193C
-
14% of wild-type specific activity, wider substrate range than wild-type with respect to tertiary alcohol acetates, inversed enantioselectivity, S enantioselectivity of 64, binding of S enantiomer of substrate 1,1,1-trifluoro-2-phenyl-but-3-yn-1-yl acetate with lower free energy than wild-type, M193C mutation seems to stabilize S orientation, mutant generated using a focused directed-evolution approach based on saturation mutagenesis according to CASTing method
M193C
-
very low specific activity similar to mutant E188W, R enantioselectivity of 16
L209F
-
the mutant shows 3.8fold increased activity compared to the wild type enzyme
L97F
-
the mutant shows 5.4fold increased activity compared to the wild type enzyme
L97F/L209F
-
the mutant shows 28.8fold increased activity compared to the wild type enzyme
R179A
-
mutation in interaction consensus sequence, wild-type activity, loss of interaction with Aes interactors such as MalY
R48A
the enzymatic activity of the mutant is enhanced by improvement of catalytic efficiency (3.7fold with 4-nitrophenyl butyrate and 8fold with tributyrin as substrate)
R48E
the enzymatic activity of the mutant is enhanced by improvement of catalytic efficiency (3.4fold with 4-nitrophenyl butyrate and 1.3fold with tributyrin as substrate)
R48K
the catalytic efficiency of the mutant is similar to the wild type enzyme
R48S
the enzymatic activity of the mutant is enhanced by improvement of catalytic efficiency (2.6fold with 4-nitrophenyl butyrate and 9.7fold with tributyrin as substrate)
T74A
-
random mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
V20D
-
site-directed mutagenesis, the mutant shows slightly reduced thermal stability compared to the wild-type enzyme, kinetic analysis, overview
additional information
additional information
-
random mutagenesis and screening for thermostable mutants at 85°C
additional information
-
construction of selenomethionine enzyme by growth of the recombinant methionine auxotroph Escherichia coli strain B834-(DE3) expressing the enzyme in minimal medium containing selenomethionine
additional information
-
construction of selenomethionine enzyme by growth of the recombinant methionine auxotroph Escherichia coli strain B834-(DE3) expressing the enzyme in minimal medium containing selenomethionine
-
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reversible unfolding of enzyme with both urea and guanidinium-HCl. Unfolding data suggest the presence of two domains which unfold more or less independently
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
industry
molecular biology
paper production
synthesis
-
enzyme is useful for the commercial geraniol production from palmarosa oil
industry
-
enhancement of sensory quality in alcoholic beverage through higher activity of Saccharomyces cerevisiae EAHase in mixed culture with Pichia anomala mutant with respiration deficiency
industry
-
enhancement of sensory quality in alcoholic beverage through higher activity of Saccharomyces cerevisiae EAHase in mixed culture with Pichia anomala low respirating mutant
industry
-
use of the very active biocatalyst EST1 for chiral resolution of 1,2-O-isopropylidene glycol esters
industry
-
cooperative action on birchwood xylan degradation in combination with Streptomyces sp. xylanase and beta xylosidase, production of biofuels utilizing hemicelluloses containing acetyl xylan, 1.16fold to 1.39fold increased sugar release
industry
-
use of the very active biocatalyst EST1 for chiral resolution of 1,2-O-isopropylidene glycol esters
-
molecular biology
-
postulated PON (paraoxonase) family membership due to similarity to primary structure of PON2, plant strictosidine synthase and di-isopropyl fluorophosphatase, its N-terminal single transmembrane domain, a nine-exon gene structure, a six-bladed beta-propeller tertiary structure, and similar metabolic regulation of gene expression
molecular biology
-
protein-protein interaction consensus sequence, involved in regulation of both sugar and lipid metabolism, according to interaction partners
paper production
-
the enzyme can be a potential source for pretreatment of pulps and biobleaching in paper manufacture due to its activity with acetylated xylan leading to complete hydrolysis
paper production
-
the enzyme can be a potential source for pretreatment of pulps and biobleaching in paper manufacture due to its activity with acetylated xylan leading to complete hydrolysis
-
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