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Information on EC 3.1.1.1 - carboxylesterase and Organism(s) Geobacillus stearothermophilus and UniProt Accession Q06174
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EC Tree
3.1.1.1 carboxylesteraseIUBMB 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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Word Map
- 3.1.1.1
- lipase
-
insecticide
- leukocyte
- lymphocyte
-
alpha-naphthyl
- leukemia
-
cytochemical
- urine
- isozymes
- p-nitrophenyl
-
organophosphate
-
prodrugs
-
ache
- phagocytic
- marrow
- urinary
-
organophosphorus
- hydrolases
-
pesticide
- lysosomal
- fluoride
- myeloid
- granulocyte
-
lipolytic
-
pyrethroids
- nitrite
-
neurotoxic
- paraoxon
-
phagocytosis
- carbamate
- mosquito
- chlorpyrifos
- paraoxonase
- histiocytic
-
urinalysis
-
cytochemistry
- kallikreins
- culex
- irinotecan
- dfp
- fluorophosphate
- diptera
-
diisopropyl
-
myelomonocytic
- pmsf
- soman
- parathion
-
allozymes
- diisopropylfluorophosphate
- oseltamivir
- industry
- environmental protection
- agriculture
- analysis
- diagnostics
- synthesis
- degradation
- biotechnology
- medicine
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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 TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
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
9016-18-6
-
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
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
Est55, 97% of the activity with 4-nitrophenyl butanoate, activation energy 35.7 kJ/mol. Est30, activation energy 101.9 kJ/mol
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
Est55, 13% of the activity with 4-nitrophenyl butanoate, Est30, 50% of the activity with 4-nitrophenyl caproate
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
-
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
-
-
-
-
?
4-nitrophenyl propanoate + H2O
4-nitrophenol + propanoate
-
Est55, 50% of the activity with 4-nitrophenyl butanoate, Est30, 45% of the activity with 4-nitrophenyl caproate
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
-
-
?
7-ethyl-10-[4-(1-piperidino)-1-piperidino] carbonyloxycamptothecin + H2O
7-ethyl-10-hydroxycampothecin + ?
-
i.e. irinotecan, CPT-11, prodrug
i.e. SN-38, topoisomerase inhibitor used in cancer therapy
-
?
benzyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
benzyloxycarbonyl-Gly + 4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-L-Ala-p-nitrophenyl ester + H2O
benzyloxycarbonyl-L-Ala + 4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-L-Tyr-p-nitrophenyl ester + H2O
benzyloxycarbonyl-L-Tyr + 4-nitrophenol
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
Est55, 30% of the activity with 4-nitrophenyl butanoate, Est30, 20% of the activity with 4-nitrophenyl caproate
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
Est30, 65% of the activity with 4-nitrophenyl caproate
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + capric acid
-
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + capric acid
-
Est55, 1.6% of the activity with 4-nitrophenyl butanoate, Est30, 32% of the activity with 4-nitrophenyl caproate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + lauric acid
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + lauric acid
-
Est55, 0.6% of the activity with 4-nitrophenyl butanoate, Est30, 12% of the activity with 4-nitrophenyl caproate
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
1 mM, Est55, 33% stimulation, Est30, 7% stimulation
dithiothreitol
-
1 mM, Est55, 45% stimulation, Est30, 719% stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0186
7-ethyl-10-[4-(1-piperidino)-1-piperidino] carbonyloxycamptothecin
-
wild-type, pH 8.5
0.0206
7-ethyl-10-[4-(1-piperidino)-1-piperidino] carbonyloxycamptothecin
-
mutant C408P, pH 8.5
0.0223
7-ethyl-10-[4-(1-piperidino)-1-piperidino] carbonyloxycamptothecin
-
mutant C408V, pH 8.5
0.0224
7-ethyl-10-[4-(1-piperidino)-1-piperidino] carbonyloxycamptothecin
-
mutant C408G, pH 8.5
0.0453
7-ethyl-10-[4-(1-piperidino)-1-piperidino] carbonyloxycamptothecin
-
mutant C408A, pH 8.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
influence of bovine serum albumin on kinetic parameters
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 2.0 and 1.58 A resolution. Enzyme folds into a catalytic domain, an alpha/beta domain and a regulatory domain. Residue C408 adjacent to the active site is triply oxidized and may have a regulatory role
-
enzyme Est30, hanging drop vapour diffusion method, ammonium sulfate is used as a precipitant, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
D232-K211, E105-K82, E54-K134, E238-R12 and E147-K134 are critical ion-pairs of fundamental importance in maintaining the structural integrity of the protein structure. Among these five pairs, one ion-pair (D232-K211) is extremely stable throughout the simulation up to 70°C. D232-K211 ion-pair between alphaF and beta8 adds more stability towards thermostable beta-sheet core region
additional information
-
D232-K211, E105-K82, E54-K134, E238-R12 and E147-K134 are critical ion-pairs of fundamental importance in maintaining the structural integrity of the protein structure. Among these five pairs, one ion-pair (D232-K211) is extremely stable throughout the simulation up to 70°C. D232-K211 ion-pair between alphaF and beta8 adds more stability towards thermostable beta-sheet core region
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27 - 100
at 27°C, 70°C, and 100°C the enzyme is stable and maintains its global three-dimensional structure
60
70
additional information
-
bovine serum albumin enhances thermostability
70
-
the recombinant enzyme shows 76.7-67.6% activity after incubation at 70°C for 30 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris strain GS115 and Aspergillus niger strain M54
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
enzyme can activate prodrug 7-ethyl-10-[4-(1-piperidino)-1-piperidino] carbonyloxycamptothecin to give 7-ethyl-10-hydroxycampothecin, i.e. SN-38, a topoisomerase inhibitor used in cancer therapy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wood, A.N.P.; Fernandez-Lafuente, R.; Cowan, D.A.
Purification and partial characterization of a novel thermophilic carboxylesterase with high mesophilic specific activity
Enzyme Microb. Technol.
17
816-825
1995
Geobacillus stearothermophilus
Liu, P.; Wang, Y.F.; Ewis, H.E.; Abdelal, A.; Lu, C.D.; Weber, I.T.
Crystallization and preliminary X-ray diffraction data for the carboxylesterase Est30 from Bacillus stearothermophilus
Acta Crystallogr. Sect. D
59
1472-1473
2003
Geobacillus stearothermophilus
Ewis, H.E.; Abdelal, A.T.; Lu, C.D.
Molecular cloning and characterization of two thermostable carboxyl esterases from Geobacillus stearothermophilus
Gene
329
187-195
2004
Geobacillus stearothermophilus
Liu, P.; Ewis, H.E.; Tai, P.C.; Lu, C.D.; Weber, I.T.
Crystal structure of the Geobacillus stearothermophilus carboxylesterase Est55 and its activation of prodrug CPT-11
J. Mol. Biol.
367
212-223
2007
Geobacillus stearothermophilus
Kundu, S.; Roy, D.
Structural study of carboxylesterase from hyperthermophilic bacteria Geobacillus stearothermophilus by molecular dynamics simulation
J. Mol. Graph. Model.
28
820-827
2010
Geobacillus stearothermophilus (Q06174), Geobacillus stearothermophilus
Sun, J.; Liu, Z.
Heterologous expression and characterization of the carboxylesterase from Geobacillus stearothermophilus
Prog. Biochem. Biophys.
37
967-974
2010
Geobacillus stearothermophilus, Geobacillus stearothermophilus CICC 20156
-
EXTERNAL LINKS (specific for EC-Number 3.1.1.1)
Transporter Classification Database (TCDB): 1.B.12.5.9
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