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Information on EC 3.1.1.1 - carboxylesterase and Organism(s) Aeropyrum pernix and UniProt Accession Q9YBQ2

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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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Aeropyrum pernix
UNIPROT: Q9YBQ2
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The taxonomic range for the selected organisms is: Aeropyrum pernix
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
ACAT
-
-
-
-
Acyl coenzyme A:cholesterol acyltransferase
-
-
-
-
ali-esterase
-
-
-
-
aliesterase
-
-
-
-
alpha-carboxylesterase
-
-
-
-
B-esterase
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-
-
-
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
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-
-
-
CES
-
-
-
-
cocaine esterase
-
-
-
-
Egasyn
-
-
-
-
Es-22
-
-
-
-
ES-HTEL
-
-
-
-
ES-HVEL
-
-
-
-
ES-Male
-
-
-
-
ES-THET
-
-
-
-
EST-5A
-
-
-
-
EST-5B
-
-
-
-
EST-5C
-
-
-
-
esterase A
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-
-
-
esterase B
-
-
-
-
esterase D
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-
-
-
esterase, carboxyl
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-
-
-
Esterase-22
-
-
-
-
Esterase-31
-
-
-
-
HMSE
-
-
-
-
Kidney microsomal carboxylesterase
-
-
-
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Liver microsomal carboxylesterase
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-
-
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methylbutyrase
-
-
-
-
methylbutyrate esterase
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-
-
-
Microsomal palmitoyl-CoA hydrolase
-
-
-
-
monobutyrase
-
-
-
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Monocyte/macrophage serine esterase
-
-
-
-
Non-specific carboxylesterase
-
-
-
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nonspecific carboxylesterase
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-
-
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PI 5.5 esterase
-
-
-
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PI 6.1 esterase
-
-
-
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procaine esterase
-
-
-
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Proline-beta-naphthylamidase
-
-
-
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propionyl esterase
-
-
-
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triacetin esterase
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-
-
-
vitamin A esterase
-
-
-
-
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-octanyl acetate + H2O
2-octanol + acetate
show the reaction diagram
the mutant enzyme R11G/L36P/V225A/I551L/A564T treated twice with acetone has a 9fold increase for enantioselectivity in resolution of 2-octanyl acetate relative to that purified by Ni-chelating column, but the wild-type enzyme is less sensitive to acetone in terms of enantioselectivity
-
-
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
show the reaction diagram
switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycerol
inhibition of mutant enzyme R11G/L36P/V225A/I551L/A564T no matter that it is or is not treated by acetone
Tween-80
inhibition of wild-type and mutant enzyme R11G/L36P/V225A/I551L/A564T no matter that they are or are not treated by acetone
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycerol
some increase for the activity of the wild-type enzyme treated with acetone
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00075 - 0.0118
4-nitrophenyl dodecanoate
0.0117 - 0.0266
4-nitrophenyl octanoate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.35 - 26.25
4-nitrophenyl dodecanoate
0.0313 - 8.67
4-nitrophenyl octanoate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
157.2 - 11220
4-nitrophenyl dodecanoate
1.18 - 374
4-nitrophenyl octanoate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
wild-type enzyme
8.3
mutant enzyme R11G/L36P/V225A/I551L/A564T purified by Ni-chelating column
additional information
acetone treatment shifts the optimum pH of wild-type and mutant enzymes
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 8.8
pH 5.8: about% of maximal activity, pH 8.8: about% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
the monomer subunit is composed of one hydrolase and one propeller domain. In the homodimeric structures only one subunit displayed the closed form of the enzyme. The other subunit exhibits an open gate to the catalytic site, thus revealing the structural basis that controls the oligopeptidase activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method, crystal structure determination of the native and two mutant structures (D524N and D524A)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D524A
the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
D524N
the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
F488G/R526V/T560W
1.55fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V/T560W
R11G/L36P/V225A/I551L/A564T
in the resolution of 2-octanol acetate, the acetone-treated mutant A has a 9fold enantioselective increase relative to that purified by Ni-chelating column
R526V
mutant enzyme with high esterase activity, extreme thermal stability, and high tolerance to organic solvents
R526V/T560W
1.5fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V
W474V/F488G/R526V/T560W
the mutant enzyme has 7fold higher catalytic efficiency (kcat/Km) for 4-nitrophenyl dodecanoate than the mutant enzyme R526V
W474V/R526V/T560W
3.11fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V/T560W
additional information
the esterase activity of the mutant R526V (this mutation transforms a promiscuous acylaminoacyl peptidase into a specific carboxylesterase) towards substrates with long acyl chains is enhanced by protein engineering and solvent optimization. The substrate preference of the enzyme can be further changed from 4-nitrophenyl octanoate to 4-nitrophenyl dodecanoate by protein and solvent engineering
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
acetone is utilized to purify wild-type and mutant enzymes to improve their activity and enantioselectivity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cong, F.; Xing, K.; Gao, R.; Cao, S.; Zhang, G.
Enhanced activity and enantioselectivity of a hyperthermophilic esterase from archaeon Aeropyrum pernix K1 by acetone treatment
Appl. Biochem. Biotechnol.
165
795-801
2011
Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix DSM 11879 (Q9YBQ2)
Manually annotated by BRENDA team
Harmat, V.; Domokos, K.; Menyhard, D.K.; Pallo, A.; Szeltner, Z.; Szamosi, I.; Beke-Somfai, T.; Naray-Szabo, G., Polgar, L.
Structure and catalysis of acylaminoacyl peptidase: closed and open subunits of a dimer oligopeptidase
J. Biol. Chem.
286
1987-1998
2011
Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix DSM 11879 (Q9YBQ2)
Manually annotated by BRENDA team
Liu, C.; Yang, G.; Wu, L.; Tian, G.; Zhang, Z.; Feng, Y.
Switch of substrate specificity of hyperthermophilic acylaminoacyl peptidase by combination of protein and solvent engineering
Protein Cell
2
497-506
2011
Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix DSM 11879 (Q9YBQ2)
Manually annotated by BRENDA team