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Information on EC 3.1.1.1 - carboxylesterase and Organism(s) Bacillus subtilis and UniProt Accession P37967

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.1 carboxylesterase
IUBMB Comments
Wide specificity. The enzymes from microsomes also catalyse the reactions of EC 3.1.1.2 (arylesterase), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.6 (acetylesterase), EC 3.1.1.23 (acylglycerol lipase), EC 3.1.1.28 (acylcarnitine hydrolase), EC 3.1.2.2 (palmitoyl-CoA hydrolase), EC 3.5.1.4 (amidase) and EC 3.5.1.13 (aryl-acylamidase). Also hydrolyses vitamin A esters.
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Bacillus subtilis
UNIPROT: P37967
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
esterase, carboxylesterase, butyrate esterase, carboxyl esterase, carboxylesterase 1, egasyn, serine protease-like, hce-2, acyl coenzyme a:cholesterol acyltransferase, esterase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-nitrophenyl esterase
-
-
ACAT
-
-
-
-
Acyl coenzyme A:cholesterol acyltransferase
-
-
-
-
ali-esterase
-
-
-
-
aliesterase
-
-
-
-
alpha-carboxylesterase
-
-
-
-
B-esterase
-
-
-
-
Brain carboxylesterase hBr1
-
-
-
-
butyrate esterase
-
-
-
-
butyryl esterase
-
-
-
-
CaE
-
-
-
-
carboxyesterase
-
-
-
-
Carboxyesterase ES-10
-
-
-
-
carboxyl ester hydrolase
-
-
-
-
carboxylate esterase
-
-
-
-
Carboxylesterase-5C
-
-
-
-
carboxylic acid esterase
-
-
-
-
carboxylic ester hydrolase
-
-
-
-
carboxylic esterase
-
-
-
-
Carboxylic-ester hydrolase
-
-
-
-
CES
-
-
-
-
cocaine esterase
-
-
-
-
Egasyn
-
-
-
-
Es-22
-
-
-
-
ES-HTEL
-
-
-
-
ES-HVEL
-
-
-
-
ES-Male
-
-
-
-
ES-THET
-
-
-
-
EST-5A
-
-
-
-
EST-5B
-
-
-
-
EST-5C
-
-
-
-
esterase A
-
-
-
-
esterase B
-
-
-
-
esterase D
-
-
-
-
esterase, carboxyl
-
-
-
-
Esterase-22
-
-
-
-
Esterase-31
-
-
-
-
HMSE
-
-
-
-
Kidney microsomal carboxylesterase
-
-
-
-
Liver microsomal carboxylesterase
-
-
-
-
methylbutyrase
-
-
-
-
methylbutyrate esterase
-
-
-
-
Microsomal palmitoyl-CoA hydrolase
-
-
-
-
monobutyrase
-
-
-
-
Monocyte/macrophage serine esterase
-
-
-
-
Non-specific carboxylesterase
-
-
-
-
nonspecific carboxylesterase
-
-
-
-
PI 5.5 esterase
-
-
-
-
PI 6.1 esterase
-
-
-
-
procaine esterase
-
-
-
-
Proline-beta-naphthylamidase
-
-
-
-
propionyl esterase
-
-
-
-
triacetin esterase
-
-
-
-
vitamin A esterase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a carboxylic ester + H2O = an alcohol + a carboxylate
show the reaction diagram
reaction and substrate binding mechanism, structure distinct binding pockets of the wild-type and mutant enzymes, Gly105 plays an important role
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
carboxylic-ester hydrolase
Wide specificity. The enzymes from microsomes also catalyse the reactions of EC 3.1.1.2 (arylesterase), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.6 (acetylesterase), EC 3.1.1.23 (acylglycerol lipase), EC 3.1.1.28 (acylcarnitine hydrolase), EC 3.1.2.2 (palmitoyl-CoA hydrolase), EC 3.5.1.4 (amidase) and EC 3.5.1.13 (aryl-acylamidase). Also hydrolyses vitamin A esters.
CAS REGISTRY NUMBER
COMMENTARY hide
9016-18-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-phenyl-3-butyn-2-yl acetate
2-phenyl-3-butyn-2-ol + acetate
show the reaction diagram
-
-
-
?
3-methyl-1-pentyn-3-yl acetate + H2O
3-methyl-1-pentyn-3-ol + acetate
show the reaction diagram
-
-
-
?
linalyl acetate + H2O
linalool + acetate
show the reaction diagram
-
-
-
?
p-nitrophenol butanoate + H2O
p-nitrophenol + butanoate
show the reaction diagram
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
-
-
?
t-butyl acetate + H2O
t-butanol + acetate
show the reaction diagram
-
-
-
?
t-butyl-gamma-(t-butoxycarbonylamino)-butyrate + H2O
?
show the reaction diagram
-
effective removal of t-butyl protecting group in organic synthesis
-
?
(+)-1,2-O-isopropylidenglycerol caprylate + H2O
(+)-1,2-O-isopropylidenglycerol + caprylate
show the reaction diagram
-
-
-
-
?
(+/-)-1,2-O-isopropylidenglycerol butanoate + H2O
(+/-)-1,2-O-isopropylidenglycerol + butanoate
show the reaction diagram
(-)-1,2-O-isopropylidenglycerol caprylate + H2O
(-)-1,2-O-isopropylidenglycerol + caprylate
show the reaction diagram
(R)-naproxen methyl ester + H2O
(R)-naproxen + methanol
show the reaction diagram
-
-
-
-
?
(S)-naproxen methyl ester + H2O
(S)-naproxen + methanol
show the reaction diagram
2-naphthyl acetate + H2O
2-naphthol + acetate
show the reaction diagram
-
-
-
-
?
2-phenyl-3-butyn-2-yl acetate + H2O
2-phenyl-3-butyn-2-ol + acetate
show the reaction diagram
-
model substrate for study of enantioselectivity in the enzyme reaction, overview
-
?
3-methyl-1-pentyn-3-yl acetate + H2O
3-methyl-1-pentyn-3-ol + acetate
show the reaction diagram
-
model substrate for study of enantioselectivity in the enzyme reaction, no enantioselectivity by the wild-type enzyme, overview
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
show the reaction diagram
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
highest activity (100%)
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
show the reaction diagram
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
show the reaction diagram
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
show the reaction diagram
about 30% activity compared to 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
show the reaction diagram
about 20% activity compared to 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
show the reaction diagram
-
30-35% of the activity with 4-nitrophenyl butanoate
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
show the reaction diagram
about 45% activity compared to 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
show the reaction diagram
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
show the reaction diagram
-
-
-
-
?
ethyl 2-hydroxy-4-phenylbutanoate + H2O
2-hydroxy-4-phenylbutanoate + ethanol
show the reaction diagram
-
enantiopreference for (S)-isomer with enantiomeric excess of 80%
-
?
ethyl acetate + H2O
ethanol + acetate
show the reaction diagram
-
-
-
-
?
ethyl propionate + H2O
ethanol + propionate
show the reaction diagram
-
-
-
-
?
indoxyl acetate + H2O
indol-3-ol + acetate
show the reaction diagram
-
-
-
-
?
isopropyl acetate + H2O
isopropanol + acetate
show the reaction diagram
-
-
-
-
?
linalyl acetate + H2O
linalool + acetate
show the reaction diagram
-
model substrate for study of enantioselectivity in the enzyme reaction, overview
-
?
n-butyl acetate + H2O
n-butanol + acetate
show the reaction diagram
-
-
-
-
?
n-heptyl acetate + H2O
n-heptanol + acetate
show the reaction diagram
-
-
-
-
?
n-hexyl acetate + H2O
n-hexanol + acetate
show the reaction diagram
-
-
-
-
?
n-octyl acetate + H2O
n-octanol + acetate
show the reaction diagram
-
-
-
-
?
n-pentyl acetate + H2O
n-pentanol + acetate
show the reaction diagram
-
-
-
-
?
N-propyl acetate + H2O
n-propanol + acetate
show the reaction diagram
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
show the reaction diagram
-
-
-
-
?
Rac-ibuprofen methyl ester + H2O
Rac-ibuprofen + methanol
show the reaction diagram
-
-
-
-
?
trans-permethrin + H2O
(1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylic acid + (3-phenoxyphenyl)methanol
show the reaction diagram
-
-
-
-
?
triacetin + H2O
?
show the reaction diagram
-
-
-
-
?
triacetin + H2O
acetic acid + glycerol
show the reaction diagram
about 65% of the activity with tributyrin
-
-
?
tributyrin + H2O
?
show the reaction diagram
-
-
-
-
?
tributyrin + H2O
butanoate + glycerol
show the reaction diagram
-
-
-
?
tricaproin + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
tricaprylin + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
about 20% stimulation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-naproxen
nearly 80% of the initial activity is lost when 2.5 mM of (S)-naproxen is added to the reaction system
ascorbic acid
1 mM, 40% residual activity
Cu2+
1 mM, more than 70% loss of activity
Fe2+
1 mM, more than 70% loss of activity
methyl paraoxon
-
-
Mn2+
-
partial
paraoxon
-
-
phenylmethylsulfonyl fluoride
-
1 mM, complete inhibition
sodium dodecylsulfate
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
119
p-nitrophenyl acetate
pH 7.4
0.05
4-nitrophenyl acetate
-
37°C
0.004 - 0.045
4-nitrophenyl butanoate
0.008 - 0.077
4-nitrophenyl caproate
0.017
4-nitrophenyl caprylate
-
37°C
0.1 - 0.36
4-nitrophenyl valerate
0.23 - 0.57
4-yethylumbelliferyl acetate
0.01 - 0.014
trans-permethrin
0.196
Triacetin
pH 7.5, 22°C
2.22
tributyrin
pH 7.5, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
69 - 580
4-nitrophenyl valerate
57 - 150
4-yethylumbelliferyl acetate
0.5 - 2.9
trans-permethrin
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000018 - 0.00027
methyl paraoxon
0.0000008 - 0.0000031
paraoxon
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
-
isoform CesB, substrate beta-naphthylacetate, pH 7.5, 32°C
0.03
-
isoform Cesb, substrate (R)-naproxen methyl ester, pH 7.5, 32°C
0.08
-
isoform CesA, substrate beta-naphthylacetate, pH 7.5, 32°C
0.1
-
substrate beta-naphthylacetate, pH 7.5, 32°C
0.17
-
isoform CesB, substrate (S)-naproxen methyl ester, pH 7.5, 32°C
0.55
-
isoform CesB, substrate Rac-ibuprofen methyl ester, pH 7.5, 32°C
1735
pH 7.5, 22°C
20.9
-
substrate Rac-ibuprofen methyl ester, pH 7.5, 32°C
25.4
-
isoform CesA, substrate Rac-ibuprofen methyl ester, pH 7.5, 32°C
4.23
-
isoform CesA, substrate (S)-naproxen methyl ester, pH 7.5, 32°C
4.6
-
substrate (S)-naproxen methyl ester, pH 7.5, 32°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
completely inactive above
6
-
inactive below
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
active up to
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform BS2, enzyme additionally shows amidase activity
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
52000
60000
-
PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 60000, SDS-PAGE and MALDI-TOF
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
alignment studies show that enzyme has an alpha/beta hydrolase fold with catalytic triad formed by S190, E305, and H394
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G105A
6fold increase in enantioselectivity against substrate (RS)-2-phenyl-3-butyn-2-yl acetate
A400I
-
activity with 4-nitrophenol is similar to the wild-type enzyme, similar enantioselectivity in the conversion of the model substrates compared to the wild-type
A400I/G105A
-
inactive mutant
G105A
-
90% reduced activity with 4-nitrophenol compared to the wild-type enzyme, 6fold increased enantioselectivity in the conversion of the model substrate 2-phenyl-3-butyn-2-yl acetate compared to the wild-type, inversion of enantiopreference towards linalyl acetate, slight enantioselectivity towarsd 3-methyl-1-pentyn-3-yl-acetate
L362A
-
more sensitive to inhibition by organophosphates than wild-type
L362D
-
more sensitive to inhibition by organophosphates than wild-type
L362E
-
similar to mutant L362D, some decrease in kcat and Km value compared to wild-type
L362R
-
22fold decrease in ratio kcat/Km value, mutant is less sensitive to organophosphates
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
-
670779
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 40
stable for at least 16 h
45
sharp decrease in stability above
55
-
1 h, 50% residual activity
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
20% v/v, 70-80% residual activity, 60% v/v, 45% residual activity
Ethanol
20% v/v, 70-80% residual activity, 60% v/v, almost complete inactivation
Methanol
20% v/v, 70-80% residual activity, 60% v/v, 45% residual activity
propanol
20% v/v, 70-80% residual activity, 60% v/v, almost complete inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least 2 weeks
-80°C, stable for at least 2 weeks
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
esterase A
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli BL21 cells
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
effective removal of t-butyl protecting group in organic synthesis
biotechnology
-
rational protein engineering for direct evolution of suitable enantioselective biocatalysts for synthesis of chiral substances
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Riefler III, J.F.; Higerd, T.B.
Characterization of intracellular esterase A from Bacillus subtilis
Biochim. Biophys. Acta
429
191-197
1976
Bacillus subtilis, Bacillus subtilis SR22
Manually annotated by BRENDA team
Henke, E.; Bornscheuer, U.T.; Schmid, R.D.; Pleiss, J.
A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases
ChemBioChem
4
485-493
2003
Bacillus subtilis, Sus scrofa
Manually annotated by BRENDA team
Droege, M.J.; Bos, R.; Boersma, Y.L.; Quax, W.J.
Comparison and functional characterization of three homologous intracellular carboxylesterases of Bacillus subtilis
J. Mol. Catal. B
32
261-270
2005
Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis Thai I-8
-
Manually annotated by BRENDA team
Kaiser, P.; Raina, C.; Parshad, R.; Johri, S.; Verma, V.; Andrabi, K.I.; Qazi, G.N.
A novel esterase from Bacillus subtilis (RRL 1789): purification and characterization of the enzyme
Protein Expr. Purif.
45
262-268
2006
Bacillus subtilis
Manually annotated by BRENDA team
Streit, T.M.; Borazjani, A.; Lentz, S.E.; Wierdl, M.; Potter, P.M.; Gwaltney, S.R.; Ross, M.K.
Evaluation of the side door in carboxylesterase-mediated catalysis and inhibition
Biol. Chem.
389
149-162
2008
Bacillus subtilis
Manually annotated by BRENDA team
Schmidt, M.; Henke, E.; Heinze, B.; Kourist, R.; Hidalgo, A.; Bornscheuer, U.T.
A versatile esterase from Bacillus subtilis: cloning, expression, characterization, and its application in biocatalysis
Biotechnol. J.
2
249-253
2007
Bacillus subtilis (P37967), Bacillus subtilis
Manually annotated by BRENDA team
Maqbool, Q.U.; Johri, S.; Rasool, S.; Riyaz-ul-Hassan, S.; Verma, V.; Nargotra, A.; Koul, S.; Qazi, G.N.
Molecular cloning of carboxylesterase gene and biochemical characterization of encoded protein from Bacillus subtilis (RRL BB1)
J. Biotechnol.
125
1-10
2006
Bacillus subtilis (Q4PNS3), Bacillus subtilis
Manually annotated by BRENDA team
Liu, X.; Xu, J.H.; Pan, J.; Zhao, J.
Efficient production of (S)-naproxen with (R)-substrate recycling using an overexpressed carboxylesterase BsE-NP01
Appl. Biochem. Biotechnol.
162
1574-1584
2010
Bacillus subtilis (D0EPY0), Bacillus subtilis ECU0554 (D0EPY0), Bacillus subtilis ECU0554
Manually annotated by BRENDA team