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Information on EC 3.1.1.1 - carboxylesterase

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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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UNIPROT: O28511
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Word Map
The enzyme appears in 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
AF1763
ACAT
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-
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Acyl coenzyme A:cholesterol acyltransferase
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-
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ali-esterase
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aliesterase
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alpha-carboxylesterase
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-
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B-esterase
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Brain carboxylesterase hBr1
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-
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butyrate esterase
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-
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butyryl esterase
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-
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CaE
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-
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carboxyesterase
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-
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Carboxyesterase ES-10
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carboxyl ester hydrolase
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carboxylate esterase
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Carboxylesterase-5C
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carboxylic acid esterase
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carboxylic ester hydrolase
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carboxylic esterase
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Carboxylic-ester hydrolase
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CES
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cocaine esterase
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Egasyn
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Es-22
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ES-HTEL
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ES-HVEL
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ES-Male
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ES-THET
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EST-5A
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EST-5B
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EST-5C
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esterase A
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esterase B
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esterase D
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esterase, carboxyl
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Esterase-22
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Esterase-31
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HMSE
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Kidney microsomal carboxylesterase
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Liver microsomal carboxylesterase
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methylbutyrase
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methylbutyrate esterase
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Microsomal palmitoyl-CoA hydrolase
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monobutyrase
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Monocyte/macrophage serine esterase
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Non-specific carboxylesterase
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nonspecific carboxylesterase
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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -
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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
converted twice as fast as the corresponding palmitate
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?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
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-
?
butyl acetate + H2O
butanol + acetate
show the reaction diagram
ethyl acetate + H2O
ethanol + acetate
show the reaction diagram
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-
-
?
ethyl butyrate + H2O
ethanol + butanoate
show the reaction diagram
the enzyme preferentially hydrolyzes esters of short-chain fatty acids (C2–C4) and especially those of medium chain (C5–C6) fatty acids with short chain alcohols
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-
?
ethyl propionate + H2O
ethanol + propionate
show the reaction diagram
methyl acetate + H2O
methanol + acetate
show the reaction diagram
methyl butyrate + H2O
methanol + butanoate
show the reaction diagram
preferred substrate. The enzyme preferentially hydrolyzes esters of short-chain fatty acids (C2–C4) and especially those of medium chain (C5–C6) fatty acids with short chain alcohols
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?
methyl butyrate + H2O
methanol + butyrate
show the reaction diagram
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?
methyl hexanoate + H2O
methanol + hexanoate
show the reaction diagram
methyl propionate + H2O
methanol + propionate
show the reaction diagram
phenyl acetate + H2O
phenol + acetate
show the reaction diagram
tributyrin + H2O
?
show the reaction diagram
hydrolyzed at a lower rate than short and medium chain fatty acid esters
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?
additional information
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.876
4-nitrophenyl palmitate
pH 7, 50°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
47.5
4-nitrophenyl palmitate
pH 7, 50°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
54
4-nitrophenyl palmitate
pH 7, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 11
at room temperature
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 12
pH 7.0: about 40% of maximal activity, pH 12: about 30% of maximal activity, at room temperature
8 - 12
pH 8: about 60% of maximal activity, pH 12: about 30% of maximal activity, at room temperature
9 - 12
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 90
40°C: about 40% of maximal activity, 90°C: about 65% of maximal activity
40 - 95
40°C: about 40% of maximal activity, 95°C: about 40% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O28511_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
474
0
52828
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52800
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D163N
D169N
H210N
S136C
Y244stop
a truncated version of the enzyme covering the 244 N-terminal residues reveals measurable activity
Y255stop
88% loss of activity compared to wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rusnak, M.; Nieveler, J.M Schmid, R. D.; Petri, R.
The putative lipase, AF1763, from Archaeoglobus fulgidus is a carboxylesterase with a very high pH optimum
Biotechnol. Lett.
27
743-748
2005
Archaeoglobus fulgidus (O28511)
Manually annotated by BRENDA team