Information on EC 3.1.1.6 - acetylesterase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.1.6
-
RECOMMENDED NAME
GeneOntology No.
acetylesterase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an acetic ester + H2O = an alcohol + acetate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
hydrolysis of carboxylic ester
transacetylation
transesterification
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sophorosyloxydocosanoate deacetylation
-
-
SYSTEMATIC NAME
IUBMB Comments
acetic-ester acetylhydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9000-82-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Candida bororiensis
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Manually annotated by BRENDA team
cv. Nausica and Arancha
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
palmarosa, 5 isozymes Est-A, Est-B, Est-C, Est-D, Est-E
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-
Manually annotated by BRENDA team
finger millet, also known as ragi, indigenous minor millet in india
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
CBS 1553
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Manually annotated by BRENDA team
two isoenzymes
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
parsley
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Manually annotated by BRENDA team
black cottonwood
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Kyokai 701
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Manually annotated by BRENDA team
Salmonella enterica serovar Typhi Vi phage I
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Manually annotated by BRENDA team
Salmonella enterica serovar Typhi Vi phage III
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Manually annotated by BRENDA team
Salmonella enterica serovar Typhi Vi phage IV
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Manually annotated by BRENDA team
Salmonella enterica serovar Typhi Vi phage V
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Manually annotated by BRENDA team
Salmonella enterica serovar Typhi Vi phage VI
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Manually annotated by BRENDA team
Salmonella enterica serovar Typhi Vi phage VII
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
PC22
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
formerly termed Chrysosporium lucknowense C1
UniProt
Manually annotated by BRENDA team
formerly termed Chrysosporium lucknowense C1
UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
cultivars Italia, Rubi, Benitaka, and Brasil
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Manually annotated by BRENDA team
wild-type strain NBRC and EAL-6, a low-respiratory, petite mutant of strain NBRC
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4R)-hydroxy-3-methyl-2-(2-propynyl)-cyclopent-2-enone acetate + H2O
?
show the reaction diagram
(acetyloxy)(phenyl)acetic acid + H2O
(S)-mandelic acid + (2R)-(acetyloxy)(phenyl)ethanoic acid
show the reaction diagram
(R)-1,2-O-isopropylidene glycol acetate + H2O
(R)-1,2-O-isopropylidene glycol + acetate
show the reaction diagram
-
-
-
-
?
(R,S)-1,2-O-isopropylidene glycol butyrate + H2O
(R)-1,2-O-isopropylidene glycol + butyrate
show the reaction diagram
-
fresh bacterial cells or purified EST1 (0.01 micromol p-nitrophenol/min), 28C, 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
show the reaction diagram
-
fresh bacterial cells or purified EST1 (0.01 micromol p-nitrophenol/min), 28C, 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-naphthol acetate + H2O
1-naphthol + acetate
show the reaction diagram
1-naphthyl acetate + H2O
1-naphthol + acetate
show the reaction diagram
1-phenyl-1-(trifluoromethyl)prop-2-yn-1-yl acetate + H2O
1-phenyl-1-(trifluoromethyl)prop-2-yn-1-ol + acetate
show the reaction diagram
-
determination of enantiopreference, wild-type R enantioselectivity is 42
spectrophotometric assay coupling released acetate to NADH generation
-
?
2-benzylcyclohex-1-en-1-yl acetate + H2O
2-benzylcyclohexanone + acetate
show the reaction diagram
2-ethylcyclohex-1-en-1-yl acetate + H2O
2-ethylcyclohexanone + acetate
show the reaction diagram
-
isoenzyme Est I, 99% conversion of substrate with 99% S-configuration of product
-
-
?
2-isopropylcyclohex-1-en-1-yl acetate + H2O
2-isopropylcyclohexanone + acetate
show the reaction diagram
-
isoenzyme Est I, 10% conversion of substrate with R-configuration of product
-
-
?
2-methylcyclohex-1-en-1-yl acetate + H2O
(S)-2-methylcyclohexanone + acetate
show the reaction diagram
-
isoenzyme Est I, 99% conversion of substrate with 99% S-configuration of product
-
-
?
2-n-pentylcyclohex-1-en-1-yl acetate + H2O
2-n-pentylcyclohexanone + acetate
show the reaction diagram
2-n-propylcyclohex-1-en-1-yl acetate + H2O
2-n-propylcyclohexanone + acetate
show the reaction diagram
-
isoenzyme Est I, 99% conversion of substrate with 99% R-configuration of product
-
-
?
2-naphthol acetate + H2O
2-naphthol + acetate
show the reaction diagram
2-naphthyl acetate + H2O
2-naphthol + acetate
show the reaction diagram
2-O-acetyl 4-nitrophenyl beta-D-xylopyranoside + H2O
?
show the reaction diagram
2-O-acetyl-4-nitrophenyl beta-D-xylopyranoside + H2O
?
show the reaction diagram
-
-
-
-
?
2-t-butylcyclohex-1-en-1-yl acetate + H2O
2-t-butylcyclohexanone + acetate
show the reaction diagram
3,6-diacetylmorphine + H2O
morphine + acetate
show the reaction diagram
3-O-acetyl 4-nitrophenyl beta-D-xylopyranoside + H2O
?
show the reaction diagram
3-O-acetyl-4-nitrophenyl beta-D-xylopyranoside + H2O
?
show the reaction diagram
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-
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?
3-O-methyl-D-glucopyranoside + vinyl acetate
6-O-acetyl-3-O-methyl-D-glucopyranoside + vinyl alcohol
show the reaction diagram
4-methylumbelliferone + H2O
?
show the reaction diagram
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-
-
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?
4-methylumbelliferyl acetate + H2O
?
show the reaction diagram
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
4-nitrophenyl beta-D-glucopyranoside + vinyl acetate
4-nitrophenyl 3-O-acetyl-beta-D-glucopyranoside + vinyl alcohol
show the reaction diagram
-
yield is 70.2%
-
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?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenyl D-xylopyranose
show the reaction diagram
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 + butyrate
show the reaction diagram
4-nitrophenyl formate + H2O
4-nitrophenol + formate
show the reaction diagram
5 min, 30C, pH 5.8
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?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
show the reaction diagram
-
-
-
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?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
show the reaction diagram
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?
4-nitrophenyl-2-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl-alpha-L-arabinofuranoside + acetate
show the reaction diagram
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-
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?
4-nitrophenyl-2-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
show the reaction diagram
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preferred substrate
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?
4-nitrophenyl-3-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-4-O-acetyl-beta-D-xylopyranoside + H2O
4-nitrophenyl-beta-D-xylopyranoside + acetate
show the reaction diagram
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?
4-nitrophenyl-5-O-acetyl-alpha-L-arabinofuranoside + H2O
4-nitrophenyl-alpha-L-arabinofuranoside + acetate
show the reaction diagram
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-
-
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?
4-nitrophenyl-butanoate + H2O
4-nitrophenol + butanoate
show the reaction diagram
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-
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?
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside + H2O
?
show the reaction diagram
4-O-acetyl-4-nitrophenyl beta-D-xylopyranoside + H2O
?
show the reaction diagram
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-
-
-
?
6,6-diacetyl 13-sophorosyloxysocosanoic acid + H2O
?
show the reaction diagram
Candida bororiensis
-
-
-
-
?
6-acetylmorphine + H2O
morphine + acetate
show the reaction diagram
6-O-acetyl-D-mannopyranose + H2O
?
show the reaction diagram
-
-
-
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?
6-O-acetyl-D-mannopyranoside + H2O
?
show the reaction diagram
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-
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?
7-aminocephalosporanic acid + H2O
?
show the reaction diagram
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-
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?
7-aminocephalosporanic acid + H2O
deacetylated 7-aminocephalosporanic acid + acetate
show the reaction diagram
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-
-
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?
9-O-acetyl sialic acid + H2O
sialic acid + acetate
show the reaction diagram
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-
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?
acetyl xylan + H2O
xylan + acetate
show the reaction diagram
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from beech wood or oat spelt
-
?
acetylated hemicellulose + H2O
? + acetate
show the reaction diagram
-
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
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-
?
acetylhemicellulose + H2O
hemicellulose + acetate
show the reaction diagram
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-
-
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?
acetylxylan + H2O
?
show the reaction diagram
acetylxylan + H2O
xylan + acetate
show the reaction diagram
-
60C, pH 6, acetyl xylan esterase (acetate-releasing) activity on birchwood xylan
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-
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alpha,alpha-trehalose + vinyl acetate
? + vinyl alcohol
show the reaction diagram
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-
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
show the reaction diagram
apigenin 7-O-(6-O-malonylglucoside) + H2O
?
show the reaction diagram
-
-
-
-
?
arabinogalactan + H2O
?
show the reaction diagram
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-
-
-
?
astragaloside I + H2O
astragaloside IV + ?
show the reaction diagram
astragaloside II + H2O
astragaloside IV + ?
show the reaction diagram
beta-naphthyl acetate + H2O
beta-naphthol + acetate
show the reaction diagram
birchwood xylan + H2O
?
show the reaction diagram
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-
-
-
?
bovine submaxillary mucin + H2O
deacetylated bovine submaxillary mucin + acetate
show the reaction diagram
-
-
-
?
cellobiose + vinyl acetate
? + vinyl alcohol
show the reaction diagram
cellobiose octaacetate + H2O
?
show the reaction diagram
-
low activity
-
?
cellulose acetate + H2O
cellulose + acetate
show the reaction diagram
-
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
-
?
cephalosporin C + H2O
deacetylated cephalosporin C + acetate
show the reaction diagram
-
-
-
-
?
cephalosporin C + H2O
deacetylcephalosporin C + acetate
show the reaction diagram
-
-
-
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?
chlorogenic acid + H2O
?
show the reaction diagram
-
-
-
-
?
D-galactose + vinyl acetate
? + vinyl alcohol
show the reaction diagram
D-glucopyranosyl beta-(1,3)-xylopyranoside + vinyl acetate
? + vinyl alcohol
show the reaction diagram
D-glucopyranosyl beta-(1,4)-xylopyranoside + vinyl acetate
? + vinyl alcohol
show the reaction diagram
D-glucose + vinyl acetate
6-O-acetyl-D-glucopyranose + vinyl alcohol
show the reaction diagram
D-mannose + vinyl acetate
6-O-acetyl-D-mannopyranose + vinyl alcohol
show the reaction diagram
D-xylopyranosyl beta-(1,4)-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
show the reaction diagram
diacetin + H2O
?
show the reaction diagram
-
-
-
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?
ethyl acetate + H2O
ethanol + acetate
show the reaction diagram
geraniol acetate + H2O
geraniol + acetate
show the reaction diagram
-
enzyme plays a role in geraniol production and improving palmarosa oil quality during florescence development
-
?
geranyl acetate + H2O
geraniol + acetate
show the reaction diagram
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-
-
?
glucose penta-acetate + H2O
?
show the reaction diagram
-
high activity
-
-
?
glucose pentaacetate + H2O
?
show the reaction diagram
glycerol triacetate + H2O
?
show the reaction diagram
isoamyl acetate + H2O
isoamyl alcohol + acetate
show the reaction diagram
-
25C, 1 h, pH 7, 7 mM MgCl2, cell extracts
-
-
?
isoastragaloside I + H2O
astragaloside IV + ?
show the reaction diagram
isoastragaloside II + H2O
astragaloside IV + ?
show the reaction diagram
kojic acid + vinyl acetate
7-O-acetyl-kojic acid + vinyl alcohol
show the reaction diagram
-
yield is 30.9%
-
-
?
malonylated isorhamnetin 3-O-glucoside + H2O
?
show the reaction diagram
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-
-
-
?
methyl 2,3-O-diacetyl-beta-D-xylopyranoside + H2O
?
show the reaction diagram
methyl 2,4-O-diacetyl-beta-D-xylopyranoside + H2O
?
show the reaction diagram
methyl 2-O-methyl-beta-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
show the reaction diagram
methyl 3,4-O-diacetyl-beta-D-xylopyranoside + H2O
?
show the reaction diagram
methyl 4-O-methyl-alpha-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
show the reaction diagram
methyl 6-O-acetyl-beta-D-glucopyranoside + H2O
?
show the reaction diagram
methyl acetate + H2O
methanol + acetate
show the reaction diagram
methyl alpha-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
show the reaction diagram
methyl beta-D-glucopyranoside + vinyl acetate
? + vinyl alcohol
show the reaction diagram
methyl beta-D-glucopyranoside + vinyl acetate
methyl 3-O-acetyl-beta-D-glucopyranoside + vinyl alcohol
show the reaction diagram
-
yield is 56.4%
-
-
?
methyl-beta-D-xylopyranoside + vinylacetate
methyl-beta-D-xylopyranoside monoacetate + vinyl alcohol
show the reaction diagram
transacetylation of methylxyloside in aqueous solution (40C, pH 6, 25 mM methyl-beta-D-xylopyranoside)
analysis by thin-layer chromatography
-
?
monoacetin + H2O
glycerol + acetate
show the reaction diagram
-
-
-
-
?
naphthyl acetate + H2O
naphthol + acetate
show the reaction diagram
-
-
-
-
?
naphthyl butyrate + H2O
naphthol + butyrate
show the reaction diagram
-
-
-
-
?
naphthyl propionate + H2O
naphthol + propionate
show the reaction diagram
-
-
-
-
?
O-acetyl-1,4-beta-xylooligosaccharide + H2O
1,4-beta-xylooligosaccharide + acetic acid
show the reaction diagram
O-acetyl-4-O-methyl-D-glucurono-D-xylan + H2O
4-O-methyl-D-glucurono-D-xylan + acetic acid
show the reaction diagram
O-acetyl-galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl decanoate + H2O
p-nitrophenol + decanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoate
show the reaction diagram
p-nitrophenyl laurate + H2O
p-nitrophenol + laurate
show the reaction diagram
p-nitrophenyl propionate + H2O
p-nitrophenol + propionate
show the reaction diagram
penta-O-acetyl-alpha-D-glucose + H2O
?
show the reaction diagram
-
complete and regioselective removal of primary acetyl-group in 6-position
-
-
?
phenyl acetate + H2O
phenol + acetate
show the reaction diagram
polygalacturonan + H2O
?
show the reaction diagram
-
-
-
-
?
potato pectin + H2O
? + acetate
show the reaction diagram
-
-
-
-
?
sugar beet pectin + H2O
? + acetate
show the reaction diagram
-
highest activity
-
-
?
tobacco hemicellulose + H2O
?
show the reaction diagram
-
lowest activity
-
-
?
triacetin + H2O
?
show the reaction diagram
-
EST1, pH 8, 20C, 0.5% (w/v) Triton X-100, 0.125% (w/v) Arabic gum
titration assay
-
?
triacetine + H2O
?
show the reaction diagram
-
-
-
-
?
tributyrin + H2O
?
show the reaction diagram
tripropionin + H2O
?
show the reaction diagram
-
-
-
-
?
xanthan + H2O
?
show the reaction diagram
xylobiose + vinyl acetate
? + vinyl alcohol
show the reaction diagram
xylose tetraacetate + H2O
?
show the reaction diagram
[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl acetate + H2O
[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl]methanol + acetate
show the reaction diagram
-
fresh bacterial cells or purified enzyme (EST1 or EST2, 0.01 micromol p-nitrophenol/min), 20C, 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
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
geraniol acetate + H2O
geraniol + acetate
show the reaction diagram
-
enzyme plays a role in geraniol production and improving palmarosa oil quality during florescence development
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag+
-
stimulation
Ba2+
-
stimulation
Co2+
-
stimulation
Cu+
-
activates
Cu2+
-
activates
Fe2+
121.2% activity at 2 mM
Hg2+
-
activates
Li+
112.8% activity at 2 mM
Mg2+
-
stimulation
Pb2+
-
stimulation
Zn2+
137.1% activity at 2 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-butanol
-
-
D-xylose
at low concentrations of 1-5 mM, altered activity with 4-nitrophenyl acetate as substrate
diisopropyl fluorophosphate
Candida bororiensis
-
-
dimethylarsinic acid
-
binding mechanism
eserine
-
competitive, complete inhibition at 25 mM
ethyl acetate
85.29% residual activity at 0.5 mM
K+
-
10 mM, 70% residual activity, EST1, p-nitrophenyl acetate as substrate
N-ethylmaleimide
Candida bororiensis
-
-
O-Ethyl-S-phenyl phosphoramidothiolate
-
-
p-hydroxymercuribenzoate
Candida bororiensis
-
-
Paraoxon
-
competitive irreversible inhibitor
Pb(NO3)2
-
-
PCMB
-
complete inhibition at 25 mM
phenyl methylsulfonyl fluoride
-
10 mM, 50% decreased acetyl esterase activity
phenylmethylsulfonyl fluoride
-
competitive irreversible inhibitor
Primary alcohols
-
-
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
Sodium acetate
at concentrations higher than 100 mM
Trifluorotetradecanone
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzethonium chloride
-
i.e. (diisobutyl phenoxyethoxyethyl) dimethyl benzylammonium chloride, up to 2.5fold enhancement of activity
bis(2-ethylhexyl) sodium sulfosuccinate
-
138% of initial activity
bis(octadecyl) ammonium chloride
-
246% of initial activity
cellobiose
enhanced activity with 4-nitrophenyl acetate as substrate
cetyltrimethyl ammonium bromide
-
184% of initial activity
Citric acid
-
-
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
Mandelic acid
110% activity at 0.5 mM
xylooligosaccharide
50 mM, enhanced activity with 4-nitrophenyl acetate as substrate
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
(R)-1,2-O-isopropylidene glycol acetate
-
EST1, after preparative electrophoresis
2.63
1-acetoxynaphthalene
-
pH 7.8, 45C
1.54
1-naphthol acetate
-
-
0.06 - 0.97
2-benzylcyclohex-1-en-1-yl acetate
0.11
2-ethylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35C
1.87
2-isopropylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35C
0.09
2-methylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35C
0.3 - 0.72
2-n-pentylcyclohex-1-en-1-yl acetate
0.54
2-n-propylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35C
4.42
2-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40C
3.6
2-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70C
2.01 - 2.54
2-t-butylcyclohex-1-en-1-yl acetate
1.55
3-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40C
4.2
3-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70C
0.185 - 3.76
4-nitrophenyl acetate
0.057 - 0.26
4-nitrophenyl butyrate
0.245 - 0.355
4-nitrophenyl hexanoate
0.137
4-nitrophenyl propionate
-
in 50 mM citrate-phosphate (pH 6) at 70C
44.6
4-nitrophenyl-2-O-acetyl-alpha-L-arabinofuranoside
-
pH 5.5, 45C
3.28
4-nitrophenyl-2-O-acetyl-beta-D-xylopyranoside
-
pH 5.5, 45C
9.44
4-nitrophenyl-3-O-acetyl-beta-D-xylopyranoside
-
pH 5.5, 45C
6.78
4-nitrophenyl-4-O-acetyl-beta-D-xylopyranoside
-
pH 5.5, 45C
16.4
4-nitrophenyl-5-O-acetyl-alpha-L-arabinofuranoside
-
pH 5.5, 45C
0.75 - 2
4-nitrophenyl-butanoate
1.24 - 4.31
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
4
4-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70C
0.5
6-acetylmorphine
-
recombinant enzyme, pH 8.0
0.056
acetylxylan
-
-
2.7 - 7.8
Alpha-naphthyl acetate
9.1
Cellulose acetate
-
pH 5.0, 45C
-
0.36
ethyl acetate
-
-
90
glyceryl triacetate
-
-
0.15
methylumbelliferone acetate
-
-
0.0067 - 385
p-nitrophenyl acetate
0.07
phenyl acetate
-
recombinant enzyme, pH 6.4
14
Triacetin
-
-
0.015 - 0.073
tributyrin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20 - 33
2-benzylcyclohex-1-en-1-yl acetate
63
2-ethylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35C
14
2-isopropylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35C
77
2-methylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35C
26 - 42
2-n-pentylcyclohex-1-en-1-yl acetate
79
2-n-propylcyclohex-1-en-1-yl acetate
-
isoenzyme Est I, pH 7.0, 35C
41.6
2-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40C
76.1
2-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70C
7 - 17
2-t-butylcyclohex-1-en-1-yl acetate
2101
3-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40C
70.1
3-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70C
57.5
4-nitrophenyl acetate
-
in 50 mM citrate-phosphate (pH 6) at 70C
29 - 340
4-nitrophenyl butyrate
34.5 - 48.8
4-nitrophenyl hexanoate
41.3
4-nitrophenyl propionate
-
in 50 mM citrate-phosphate (pH 6) at 70C
0.15
4-nitrophenyl-2-O-acetyl-alpha-L-arabinofuranoside
-
pH 5.5, 45C
3.23
4-nitrophenyl-2-O-acetyl-beta-D-xylopyranoside
-
pH 5.5, 45C
1.9
4-nitrophenyl-3-O-acetyl-beta-D-xylopyranoside
-
pH 5.5, 45C
0.91
4-nitrophenyl-4-O-acetyl-beta-D-xylopyranoside
-
pH 5.5, 45C
1.77
4-nitrophenyl-5-O-acetyl-alpha-L-arabinofuranoside
-
pH 5.5, 45C
21 - 155
4-nitrophenyl-butanoate
241.6 - 3210
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
78.6
4-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70C
12.6
6-acetylmorphine
-
recombinant enzyme, pH 8.0
3
phenyl acetate
-
recombinant enzyme, pH 6.4
6.2 - 17.5
tributyrin
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
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 40C
21.1
2-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70C
1356
3-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
-
isozyme CE2B, in 0.1 M sodium phosphate buffer, pH 6.0, at 40C
16.7
3-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70C
310.8
4-nitrophenyl acetate
-
in 50 mM citrate-phosphate (pH 6) at 70C
0.057 - 0.26
4-nitrophenyl butyrate
301.5
4-nitrophenyl propionate
-
in 50 mM citrate-phosphate (pH 6) at 70C
56.08 - 2599
4-O-acetyl 4-nitrophenyl beta-D-xylopyranoside
19.7
4-O-acetyl-4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM citrate-phosphate (pH 6) at 70C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12
dimethylarsinic acid
-
recombinant enzyme, pH 6.4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000109
4-nitrophenyl butyrate, purified recombinant enzyme
0.000213
4-nitrophenyl formate, purified recombinant enzyme
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
0.021
Candida bororiensis
-
-
0.027
-
purified native enzyme, substrate ragi
0.061
-
purified native enzyme, substrate larch wood xylan
0.082
-
substrate p-nitrophenyl laurate, pH 7.0, 25C
0.21
4-nitrophenyl acetate, over-expression culture supernatant; recombinant enzyme, culture supernatant
0.251
-
substrate p-nitrophenyl acetate, pH 7.0, 25C
0.282
-
purified native enzyme, substrate gum karaya
0.297
-
substrate p-nitrophenyl decanoate, pH 7.0, 25C
0.352
-
substrate p-nitrophenyl hexanoate, pH 7.0, 25C
0.369
-
substrate p-nitrophenyl propionate, pH 7.0, 25C
0.474
-
substrate p-nitrophenyl butyrate, pH 7.0, 25C
0.52
-
crude enzyme, at pH 8.0 and 35C
0.85
recombinant enzyme, after CM Sepharose FF column
1.12
recombinant enzyme, after DEAE FF column, 4-nitrophenyl acetate
1.21
4-nitrophenyl acetate, purified recombinant enzyme
3
-
isozyme CE2C, using 6-O-acetyl-D-mannopyranose as substrate, pH 6.0, 40C; isozyme CE2C, using methyl 3,4-O-diacetyl-beta-D-xylopyranoside as substrate, pH 6.0, 40C
3.38
-
purified native enzyme, substrate alpha-naphthyl acetate
4
-
isozyme CE2B, using methyl 3,4-O-diacetyl-beta-D-xylopyranoside as substrate, pH 6.0, 40C
4.44
-
purified native enzyme, substrate wheat
5.39
-
purified native enzyme, substrate 4-nitrophenyl acetate
8
-
isozyme CE2, using methyl 3,4-O-diacetyl-beta-D-xylopyranoside as substrate, pH 6.0, 40C
9.63
-
p-nitrophenyl acetate, after hydroxyapatite chromatography, pH 6.5
20.5
4-nitrophenyl acetate, maximum velocity, purified recombinant enzyme, 30C, pH 5.8
35
-
isozyme CE2, using 6-O-acetyl-D-mannopyranose as substrate, pH 6.0, 40C
46.5
-
mutant E188W/M193C, using 4-nitrophenyl acetate as substrate
60
-
isozyme CE2C, using methyl 6-O-acetyl-beta-D-glucopyranoside as substrate, pH 6.0, 40C
71
-
p-nitrophenyl acetate, pH 6.5
71.4
-
purified enzyme
221.9
-
after 423.39fold purification, at pH 8.0 and 35C
250
-
pH 7.1, 65C, purified recombinant wild-type enzyme
270
-
pH 7.1, 65C, purified recombinant mutant T74A
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, 40C
333
-
wild-type, using 4-nitrophenyl acetate as substrate
376
-
-
395
-
isozyme CE2B, using 6-O-acetyl-D-mannopyranose as substrate, pH 6.0, 40C
1027
-
alpha-naphthyl acetate, pH 6.5
1104
-
-
16050
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6
-
-
6.2
-
assay at
7.5 - 9
-
-
8.5
-
assay at, substrate geranyl acetate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
no activity below
5
-
inactive below, EST1 sample after anion-exchange chromatography, p-nitrophenyl acetate as substrate, 20C, 4 h
6
-
85% residual activity, alpha-naphthyl acetate as substrate, more active in acetate buffer than phosphate buffer
6.5 - 7
-
optimum activity, alpha-naphthyl acetate as substrate
7 - 10
-
100% activity, EST1 sample after anion-exchange chromatography, p-nitrophenyl acetate as substrate, 20C, 4 h
7 - 8.5
-
the enzyme retains about 90% and 88% of its maximal activity at pH 7.0 and 8.5, respectively
7
-
no activity above
8
-
65% residual activity, alpha-naphthyl acetate as substrate
11
-
16% activity, EST1 sample after anion-exchange chromatography, p-nitrophenyl acetate as substrate, 20C, 4 h
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
37
-
respiratory virus enzyme
39
-
enteropathogenic virus enzyme
53
optimal performance towards xanthan at 53C
80
-
100% relative activity, at 60-70C 90% relative activity, EST1 sample after anion-exchange chromatography, p-nitrophenyl acetate as substrate, pH 7, 3 min
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
no activity below
15 - 75
-
-
30 - 45
-
within the temperature range of 30-45C, the enzyme exhibits more than 95% of optimum activity, whereas at temperatures higher than 45C, the activity sharply declines
40 - 65
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
below, isoelectric focusing
3.6
-
isoelectric focusing
5.9
theoretical
6
purified recombinant enzyme
6.6
-
calculated from amino acid sequence
7.6
-
isoelectric focusing
additional information
-
all isoforms isolated have pI-values between 4.1 and 5.2
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
ubiquitous transcript of ca. 2.4 kb, highest gene expression level in liver, placenta and heart, Northern blot
Manually annotated by BRENDA team
-
kidney, cytochemistry and confocal microscopy
Manually annotated by BRENDA team
-
ubiquitous transcript of ca. 2.4 kb, highest gene expression level in liver and kidney, Northern blot
Manually annotated by BRENDA team
-
kidney, cytochemistry and confocal microscopy
Manually annotated by BRENDA team
-
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)
Manually annotated by BRENDA team
-
strong expression, lower expression level than in liver as revealed by Northern blot and quantitative RT-PCR, cell fractionation, FACS analysis
Manually annotated by BRENDA team
-
spikelets, maximal in immature florescences, isozyme Est-B is increased during development, activity of isozymes at different developmental stages, overview
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
young
Manually annotated by BRENDA team
-
no expression in granulocytes and lymphocytes according to cell surface domain-specific FACS analyses
Manually annotated by BRENDA team
-
highest expression level as revealed by Northern blot and quantitative RT-PCR, Western blot, cytochemistry and confocal microscopy
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
-
highest expression within pancreatic tissue at the islets of Langerhans, revealed by cytochemistry and confocal microscopy
Manually annotated by BRENDA team
-
high expression on monocytes according to cell-surface domain-specific FACS analyses
Manually annotated by BRENDA team
-
high expression level, Northern blot, quantitative RT-PCR
Manually annotated by BRENDA team
-
quantitative RT-PCR, Western blot
Manually annotated by BRENDA team
-
ELISA using cell surface domain-specific antibody
Manually annotated by BRENDA team
-
kidney, cytochemistry and confocal microscopy
Manually annotated by BRENDA team
additional information
-
acetic acid esterase from 72 h ragi malt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
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)
-
Manually annotated by BRENDA team
-
32 kDa low molecular weight variant, sucrose density gradient cell fractionation on RINm5F cells
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19700
-
4 * 19700, SDS-PAGE
20000
-
x * 20000, SDS-PAGE
22500
-
2 * 27000, isoenzyme EstI, 2 * 22500, isoenzyme Est II, SDS-PAGE
23000
-
? * 23000, SDS-PAGE, AXE II
27000
-
2 * 27000, isoenzyme EstI, 2 * 22500, isoenzyme Est II, SDS-PAGE
29000
-
preparative electrophoresis-purified EST1, SDS-PAGE
30480
-
? * 30480, SDS-PAGE
34000
-
? * 34000, SDS-PAGE
37090
theoretical, polypeptide of 348 amino acids
38000
-
SDS-PAGE
39500
-
2 * 39500, SDS-PAGE
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
42800
-
x * 42800, calculated from amino acid sequence
48000
-
? * 48000, SDS-PAGE, AXE I
51000
-
gel filtration
52000
-
high molecular variant in Hep-G2 and SH-SY5Y cells, Western blot
54000
-
gel filtration, isoenzyme Est I
55000
-
? * 55000, SDS-PAGE
67000 - 68000
67000
-
1 * 67000, SDS-PAGE
70000
-
1 * 70000, SDS-PAGE
78500
-
gel filtration
79400
-
gel filtration
84000
-
sucrose density gradient centrifugation
85000 - 95000
-
gel filtration
155000
-
native, gel-filtration on Sephacryl S-200 HR column
160000
190000
-
gel filtration
additional information
-
esterase isozyme analysis by native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
multimer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
side-chain modification
-
glycoprotein, 3.34% carbohydrate
additional information
-
residues C140, C149 and C409 with putative intra- and intermolecular disulfide bonds, in silico analysis
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 20C (native enzyme)
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
-
-
23596
5 - 9
-
stable for 30 min
701417
6 - 9
-
stable
680319
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
11
-
unstable above
35230
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
-
stable
37
-
40 min, the transiently expressed respiratory viruses show significantly reduced activity, while the transiently expressed enteropathogenic viruses are stable
40
-
pH 5-6, 24 h 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 20-45C, 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
55
-
the wild type enzyme shows a half-life of 40 min at 55C
61
-
denaturation of Aes mutant V20D, thermal stability analysis at 20-90C, differential scanning calorimetry and circular dichroism measurements, the irreversible inactivation process is more complex than a two-state transition
68
-
denaturation of Aes, thermal stability analysis at 20-90C, 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 100C, resulting in a half-life of less than 5 min
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
dimethyl sulfoxide
dimethylformamide
Ethanol
Methanol
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilization by reducing agents
-
35224
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, several months
-
stored at -20C in 20% glycerol
-
unstable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
8.6fold, to homogeneity
-
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 4C, liquid column chromatography
at 4C, 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 -20C 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
-
from the crude commercial enzyme preparation, 27fold
-
His-tagged protein
-
immobilized metal affinity chromatography
isoenzymes Est I and Est II
-
native enzyme from 72 h ragi malt 34fold by ammonium sulfate precipitation, anion exchange chromatography, gel filtration, and hydrophobic interaction chromatography, to homogeneity
-
native enzyme to homogeneity by SDS-PAGE and isoelectric focusing
-
nickel-chelating resin column chromatography and Superdex 200 gel filtration
-
partial, separation of isoenzymes
-
purification of virus tissue material, nasal swab and from COS-7 cells
-
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
-
single-step purification
-
Strep-tactin Superflow Plus column chromatography
two enzymes: AXE I and AXE II
-
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
expressed in Escherichia coli JM109 cells
-
expressed in Escherichia coli Rosetta 2(DE3) cells
expressed in Escherichia coli strain DL41
-
expressed in Nicotiana tabacum
-
expression in Escherichia coli
-
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)
-
gene ybaC, overexpression of wild-type and mutant enzymes
-
overexpression in Streptomyces lividans IAF10-164
-
overexpression of wild-type and mutant enzymes in strain BL21(DE3)
-
respiratory and enteropathogenic coronaviruses, DNA and amino acid sequence determination and analysis, transient and functional expression in COS-7 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the addition of ZnSO4 enhances enzyme production by 37%
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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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
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very low specific activity similar to mutant E188W, R enantioselectivity of 16
L209F
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the mutant shows 3.8fold increased activity compared to the wild type enzyme
L97F
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the mutant shows 5.4fold increased activity compared to the wild type enzyme
L97F/L209F
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the mutant shows 28.8fold increased activity compared to the wild type enzyme
R179A
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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
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random mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
V20D
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site-directed mutagenesis, the mutant shows slightly reduced thermal stability compared to the wild-type enzyme, kinetic analysis, overview
additional information
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 hide
LITERATURE
analysis
industry
molecular biology
paper production
synthesis
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enzyme is useful for the commercial geraniol production from palmarosa oil