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Information on EC 3.1.1.1 - carboxylesterase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97VW1
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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: Saccharolobus solfataricus
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
(R)-2-(3-benzoylphenyl)propanoic methyl ester + H2O
methanol + (R)-2-(3-benzoylphenyl)propanoate
when tested with the racemic substrate, the enzyme leads to the production of the R-configured acid with an enantiomeric excess of 80% at the conversion rate of 20% in 32 h
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
hydrolysis at about 90% compared to activity with 4-nitrophenyl pentanoate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
hydrolysis at about 50% compared to activity with 4-nitrophenyl pentanoate
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
hydrolysis at about 75% compared to activity with 4-nitrophenyl pentanoate
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
-
-
-
?
4-nitrophenyl propanoate + H2O
4-nitrophenol + propanoate
hydrolysis at about 85% compared to activity with 4-nitrophenyl pentanoate
-
-
?
4-nitrophenyl tetradecanoate + H2O
4-nitrophenol + tetradecanoate
hydrolysis at less tha 10% compared to activity with 4-nitrophenyl pentanoate
-
-
?
methyl (-)-2-(3-benzoylphenyl)propionate + H2O
(-)-2-(3-benzoylphenyl)propionate + methanol
-
-
-
?
(S)-ibuprofen methyl ester + H2O
(S)-ibuprofen + methanol
-
the enzyme has S-form specificity for ibuprofen
-
-
?
(S)-naproxen methyl ester + H2O
(S)-naproxen + methanol
-
the enzyme yields highly optically pure (S) naproxen
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
-
-
-
?
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferone + butyrate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
the enzyme shows the highest activity with p-nitrophenyl caproate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
the enzyme shows the highest specific activity with p-nitrophenyl caprylate
-
-
?
4-nitrophenyl hexadecanoate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
-
-
-
-
?
glyceryl tridecanoate + H2O
?
activity with mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
-
-
?
glyceryl trihexanoate + H2O
?
activity with mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
-
-
?
glyceryl trioctanoate + H2O
?
activity with mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
-
-
?
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoate
-
-
-
?
S-methyl thiobutanoate + H2O
methanol + thiobutanoate
activity with mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
hydrolysis at about 70% compared to activity with 4-nitrophenyl pentanoate
-
-
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
-
-
-
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
hydrolysis at about 30% compared to activity with 4-nitrophenyl pentanoate
-
-
?
4-nitrophenyl hexadecanoate + H2O
4-nitrophenol + hexadecanoate
-
-
-
?
4-nitrophenyl hexadecanoate + H2O
4-nitrophenol + hexadecanoate
hydrolysis at less than 10% compared to activity with 4-nitrophenyl pentanoate
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
hydrolysis at about 90% compared to activity with 4-nitrophenyl pentanoate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
at 37°C, 14% of the activity with pentanoyl-CoA
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
specific activity is less than 10% compared to the activity with caprylate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
at 37°C, 74% of the activity with pentanoyl-CoA
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
specific activity is about 80% compared to the activity with caprylate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
specific activity is about 50% compared to the activity with caprylate
-
-
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
-
-
-
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
activity with mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
at 37°C, 69% of the activity with pentanoyl-CoA
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
activity with mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
specific activity is about 10% compared to the activity with caprylate
-
-
?
glyceryl tributyrate + H2O
?
activity with mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
-
-
?
glyceryl trioleate + H2O
?
activity with mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
-
-
?
additional information
?
-
broad substrate specificities toward various p-nitrophenyl esters ranging from C2 to C16. The activity of the enzyme decreases slowly from 4-nitrophenyl hexanoate to 4-nitrophenyl dodecanoate and is very low for 4-nitrophenyl 4-nitrophenyl hexadecanoate
-
-
?
additional information
?
-
-
broad substrate specificities toward various p-nitrophenyl esters ranging from C2 to C16. The activity of the enzyme decreases slowly from 4-nitrophenyl hexanoate to 4-nitrophenyl dodecanoate and is very low for 4-nitrophenyl 4-nitrophenyl hexadecanoate
-
-
?
additional information
?
-
the activity of the enzyme is strongly influenced by the chain length of the acyl group. Activity increases up to C6 and then decreases
-
-
?
additional information
?
-
-
the activity of the enzyme is strongly influenced by the chain length of the acyl group. Activity increases up to C6 and then decreases
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
2 mM, enhances the enzyme activity to 134% compared to the activity of EDTA-treated enzyme
additional information
the enzyme does not require a divalent cation for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethylfluorophosphate
0.01 mM, 30°C, 30 min, 75% inhibition
diphenylamine-2-carboxylate
5 mM, 30°C, 30 min, 77% inhibition
2-propanol
5% (w/v), 58% inhibition. 10% (w/v), 94% inhibition
additional information
-
enzyme retains 97% of activity after 60 min in 1 M urea. Not inhibitory: 1% Tween 20, 1% Lubrol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DMSO
-
optimal activation at 3.5% v/v with an increase in kcat of 20-30%, no dramatic changes in conformation of the enzyme at 3.5% v/v DMSO and 50-80°C, but significant changes at small DMSO concentrations
additional information
-
microwave irradiation (300 W) significantly stimulates activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.8
4-nitrophenyl caproate
pH and temperature not specified in the publication
0.63
4-nitrophenyl butyrate
pH 7.4, 37°C, mutant enzyme R210A
0.028
4-nitrophenyl caprylate
pH 7.4, 37°C, wild-type enzyme
0.043
4-nitrophenyl caprylate
pH 7.4, 37°C, mutant enzyme R210A
0.05
4-nitrophenyl hexanoate
pH 7.1, 70°C, mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
4-nitrophenyl butyrate
pH 7.4, 37°C, mutant enzyme R210A
7.8
4-nitrophenyl caprylate
pH 7.4, 37°C, mutant enzyme R210A
2.47
4-nitrophenyl hexanoate
pH 7.1, 70°C, mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17
4-nitrophenyl butyrate
pH 7.4, 37°C, mutant enzyme R210A
192
4-nitrophenyl caprylate
pH 7.4, 37°C, mutant enzyme R210A
49.4
4-nitrophenyl hexanoate
pH 7.1, 70°C, mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.3
4.3
pH 7.1, 70°C, substrate: 4-nitrophenyl hexanoate, mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.1
7.1
substrate: 4-nitrophenyl hexanoate, mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10
pH 6.5: about 40% of maximal activity, pH 10.0: about 50% of maximal activity
4 - 10
pH 4.0: about 40% of maximal activity, pH 10.0: aboutv 40% of maximal activity, mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
4.8 - 9.2
-
pH 4.8: about 40% of maximal activity, pH 9.2: about 40% of maximal activity
5 - 8.5
-
pH 5.0: about 50% of maximal activity, pH 8.5: about 60% of maximal activity, substrate: 4-methylumbelliferyl butyrate
5 - 9
pH 5.0: about 40% of maximal activity, pH 9.0: about 50% of maximal activity
6.5 - 8
pH 6.5: about 50% of maximal activity, pH 8.0: about 90% of maximal activity, less than 10% of maximal activity at pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
70
80
70
substrate: 4-nitrophenyl hexanoate, mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 90
40°C: about 50% of maximal activity, 90°C: about 70% of maximal activity
60 - 90
60°C: about 60% of maximal activity, 90°C: about 70% of maximal activity
40 - 80
40°C: about 70% of maximal activity, 80°C: about 60% of maximal activity
60 - 75
60°C: 55% of maximal activity, 75°C: about 35% of maximal activity, substrate: 4-nitrophenyl hexanoate, mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
70 - 90
70°C: about 55% of maximal activity, 90°C: about 80% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
homotrimer
monomer
tetramer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D266N
specific activity of the mutant enzyme is 2% of the wild-type activity
F188A
activity with 4-nitrophenyl butyrate as substrate is unchanged as compared to the wild-type value
H295N
specific activity of the mutant enzyme is 2% of the wild-type activity
K187A
partial loss of activity with 4-nitrophenyl butyrate as substrate
R210A
catalytic efficiency (kcat/Km) of the mutant enzyme triples over that of wild-type enzyme
S144A
specific activity of the mutant enzyme is 1% of the wild-type activity
S144C
specific activity of the mutant enzyme is 5% of the wild-type activity
T58A
partial loss of activity with 4-nitrophenyl butyrate as substrate
W59A
activity with 4-nitrophenyl butyrate as substrate is unchanged as compared to the wild-type value
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
80
90
70
stable for more than 10 h, mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-propanol
Ethanol
Methanol
Ethanol
-
stable at high concentrations of polar organic solvents, such as ethanol and methanol as compared to other mesophilic counterparts
Methanol
-
stable at high concentrations of polar organic solvents, such as ethanol and methanol as compared to other mesophilic counterparts
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme expressed from the gene that has a deletion of about 60 residues at the N terminus(SSODELTAN)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a 6His-tagged fusion protein
expression in Escherichia coli
overexpression in Escherichia coli with fusion His-tags at the C-terminus
the gene that has a deletion of about 60 residues at the N terminus(SSODELTAN) is expressed in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
biotechnology
-
the enzyme can be used as a biocatalyst at suboptimal temperatures through addition of DMSO as an activator
synthesis
-
the enzyme shows chiral resolution activity for (S)-ibuprofen, indicating that the enzyme can be used for the production of commercially important chiral drugs
synthesis
the enzyme can be used for application in the synthesis of chiral compounds
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sehgal, A.C.; Tompson, R.; Cavanagh, J.; Kelly, R.M.
Structural and catalytic response to temperature and cosolvents of carboxylesterase EST1 from the extremely thermoacidophilic archaeon Sulfolobus solfataricus P1
Biotechnol. Bioeng.
80
784-793
2002
Saccharolobus solfataricus, Saccharolobus solfataricus P1
Mandrich, L.; Merone, L.; Pezzullo, M.; Cipolla, L.; Nicotra, F.; Rossi, M.; Manco, G.
Role of the N terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family
J. Mol. Biol.
345
501-512
2004
Alicyclobacillus acidocaldarius, Saccharolobus solfataricus, Saccharolobus solfataricus (Q97VU2), Saccharolobus solfataricus P2 (Q97VU2), Saccharolobus solfataricus P2
Park, Y.; Choi, S.Y.; Lee, H.
A carboxylesterase from the thermoacidophilic archaeon Sulfolobus solfataricus P1; purification, characterization, and expression
Biochim. Biophys. Acta
1760
820-828
2006
Saccharolobus solfataricus, Saccharolobus solfataricus P1
Morana, A.; Di Prizito, N.; Aurilia, V.; Rossi, M.; Cannio, R.
A carboxylesterase from the hyperthermophilic archaeon Sulfolobus solfataricus: cloning of the gene, characterization of the protein.
Gene
283
107-115
2002
Saccharolobus solfataricus, Saccharolobus solfataricus MT4
Sehgal, A.C.; Callen, W.; Mathur, E.J.; Short, J.M.; Kelly, R.M.
Carboxylesterase from Sulfolobus solfataricus P1.
Methods Enzymol.
330
461-471
2001
Saccharolobus solfataricus, Saccharolobus solfataricus P1
Wang, J.; Wang, J.; Gong, X.; Zheng, G.
A novel esterase Sso2518 from Sulfolobus solfataricus with a much lower temperature optimum than the growth temperature
Biotechnol. Lett.
32
1103-1108
2010
Saccharolobus solfataricus (Q97VU1), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97VU1), Saccharolobus solfataricus P2
Shang, Y.S.; Zhang, X.E.; Wang, X.D.; Guo, Y.C.; Zhang, Z.P.; Zhou, Y.F.
Biochemical characterization and mutational improvement of a thermophilic esterase from Sulfolobus solfataricus P2
Biotechnol. Lett.
32
1151-1157
2010
Saccharolobus solfataricus (Q97VU1), Saccharolobus solfataricus P2 (Q97VU1), Saccharolobus solfataricus P2
Chung, Y.; Park, C.; Lee, S.
Partial purification and characterization of thermostable esterase from the hyperthermophilic archaeon Sulfolobus solfataricus
Biotechnol. Bioprocess Eng.
5
53-56
2000
Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617
-
Kim, S.; Lee, S.B.
Thermostable esterase from a thermoacidophilic archaeon: purification and characterization for enzymatic resolution of a chiral compound
Biosci. Biotechnol. Biochem.
68
2289-2298
2004
Saccharolobus solfataricus (Q97VW1), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97VW1), Saccharolobus solfataricus P2
Sehgal, A.C.; Kelly, R.M.
Strategic selection of hyperthermophilic esterases for resolution of 2-arylpropionic esters
Biotechnol. Prog.
19
1410-1416
2003
Saccharolobus solfataricus, Saccharolobus solfataricus P1
Young, D.D.; Nichols. J.; Kelly, R.M.; Deiters, A.
Microwave activation of enzymatic catalysis
J. Am. Chem. Soc.
130
10048-10049
2008
Saccharolobus solfataricus, Saccharolobus solfataricus P1
Nam, J.-K.; Park, Y.-J.; Lee, H.-B.
Cloning, expression, purification, and characterization of a thermostable esterase from the archaeon Sulfolobus solfataricus P1
J. Mol. Catal. B
94
95-103
2013
Saccharolobus solfataricus (M5DDN2), Saccharolobus solfataricus P1 (M5DDN2)
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EXTERNAL LINKS (specific for EC-Number 3.1.1.1)
Transporter Classification Database (TCDB): 1.B.12.5.9
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