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Information on EC 3.1.1.28 - acylcarnitine hydrolase
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EC Tree
3.1.1.28 acylcarnitine hydrolaseIUBMB Comments
Acts on higher fatty acid (C6 to C18) esters of L-carnitine; highest activity is with O-decanoyl-L-carnitine.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
carboxylesterase 2, mces2, acylcarnitine hydrolase, ach m1, pa5384, palmitoyl-l-carnitine hydrolase, long-chain acyl-l-carnitine hydrolase, palmitoyl carnitine hydrolase, carnitine ester hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACH M1
carnitine ester hydrolase
-
-
-
-
HACH, high activity acylcarnitine hydrolase
-
-
-
-
hydrolase, acylcarnitine
-
-
-
-
long-chain acyl-L-carnitine hydrolase
-
-
-
-
palmitoyl carnitine hydrolase
-
-
-
-
palmitoyl-L-carnitine hydrolase
-
-
-
-
palmitoylcarnitine hydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
O-fatty-acyl-L-carnitine + H2O = a fatty acid + L-carnitine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
O-acylcarnitine acylhydrolase
Acts on higher fatty acid (C6 to C18) esters of L-carnitine; highest activity is with O-decanoyl-L-carnitine.
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CAS REGISTRY NUMBER
COMMENTARY
37278-42-5
-
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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
1,3-diacylglycerides + H2O
?
-
faster than corresponding 1-monoglycerides
-
-
?
O-fatty-acyl-L-carnitine + H2O
fatty acid + L-carnitine
-
hydrolyzes preferably medium and long chain fatty acids, important role in fatty acid metabolism
-
-
?
2 palmitoyl-DL-carnitine + 2 H2O
2 palmitate + L-carnitine + D-carnitine
-
-
-
?
2 palmitoyl-DL-carnitine + 2 H2O
2 palmitate + L-carnitine + D-carnitine
-
-
-
?
lysophospholipids + H2O
?
-
prevention of accumulation of cytotoxic esters in liver cell
-
-
?
palmitoyl carnitine + H2O
?
-
prevention of accumulation of cytotoxic esters in liver cell
-
-
?
additional information
?
-
no activity with D-acetylcarnitine, acetylcholine, and octanoyl-L-carnitine
-
-
?
additional information
?
-
-
no activity with D-acetylcarnitine, acetylcholine, and octanoyl-L-carnitine
-
-
?
additional information
?
-
-
acts on higher fatty acid, C6-C18 esters of L-carnitine, highest activity with O-decanoyl-L-carnitine
-
-
?
additional information
?
-
-
not: p-nitrophenyl palmitate, glycerol tripalmitate, cholesterol palmitate
-
-
?
additional information
?
-
-
not: p-nitrophenyl palmitate, glycerol tripalmitate, cholesterol palmitate
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
lysophospholipids + H2O
?
-
prevention of accumulation of cytotoxic esters in liver cell
-
-
?
O-fatty-acyl-L-carnitine + H2O
fatty acid + L-carnitine
-
hydrolyzes preferably medium and long chain fatty acids, important role in fatty acid metabolism
-
-
?
palmitoyl carnitine + H2O
?
-
prevention of accumulation of cytotoxic esters in liver cell
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Carboxylesterase 2 as a Determinant of Response to Irinotecan and Neoadjuvant FOLFIRINOX Therapy in Pancreatic Ductal Adenocarcinoma.
Breast Neoplasms
Effect of interferon-?2b on the expression of various drug-metabolizing enzymes and transporters in co-cultures of freshly prepared human primary hepatocytes.
Carcinoma
Visualization of carboxylesterase 2 with a near-infrared two-photon fluorescent probe and potential evaluation of its anticancer drug effects in an orthotopic colon carcinoma mice model.
Chemical and Drug Induced Liver Injury
Endoplasmic Reticulum Targeting Ratiometric Fluorescent Probe for Carboxylesterase 2 Detection in Drug-Induced Acute Liver Injury.
Colonic Neoplasms
Carboxylesterase 2 production and characterization in human cells: new insights into enzyme oligomerization and activity.
Colorectal Neoplasms
A highly selective near infrared fluorescent probe for carboxylesterase 2 and its biological applications.
Colorectal Neoplasms
Carboxylesterase 2 is downregulated in colorectal cancer following progression of the disease.
Colorectal Neoplasms
Expression of Topoisomerase 1 and carboxylesterase 2 correlates with irinotecan treatment response in metastatic colorectal cancer.
Colorectal Neoplasms
High-throughput proteomics integrated with gene microarray for discovery of colorectal cancer potential biomarkers.
Colorectal Neoplasms
Pharmacogenetics of human carboxylesterase 2, an enzyme involved in the activation of irinotecan into SN-38.
Colorectal Neoplasms
The Relationship between TP53 Gene Status and Carboxylesterase 2 Expression in Human Colorectal Cancer.
Fatty Liver
Carboxylesterase 2 prevents liver steatosis by modulating lipolysis, ER stress and lipogenesis and is regulated by HNF4?.
Glioma
Carboxylesterase 2 production and characterization in human cells: new insights into enzyme oligomerization and activity.
Hypertension
Carboxylesterase 2 and Intestine Transporters Contribute to the Low Bioavailability of Allisartan, a Prodrug of Exp3174 for Hypertension Treatment in Humans.
Liver Diseases
Intestine-Specific Overexpression of Carboxylesterase 2c Protects Mice From Diet-Induced Liver Steatosis and Obesity.
Metabolic Diseases
Carboxylesterase 2 proteins are efficient diglyceride and monoglyceride lipases possibly implicated in metabolic disease.
Neoplasms
Carboxylesterase 2 is downregulated in colorectal cancer following progression of the disease.
Neoplasms
Efficacy and Safety of CAP7.1 as Second-Line Treatment for Advanced Biliary Tract Cancers: Data from a Randomised Phase II Study.
Neoplasms
Efficacy of Low-Dose Oral Metronomic Dosing of the Prodrug of Gemcitabine, LY2334737, in Human Tumor Xenografts.
Neoplasms
Expression of Topoisomerase 1 and carboxylesterase 2 correlates with irinotecan treatment response in metastatic colorectal cancer.
Neoplasms
Tissue-infiltrating plasma cells are an important source of carboxylesterase 2 contributing to the therapeutic efficacy of prodrugs.
Non-alcoholic Fatty Liver Disease
Intestine-Specific Overexpression of Carboxylesterase 2c Protects Mice From Diet-Induced Liver Steatosis and Obesity.
Obesity
Human Carboxylesterase 2 Reverses Obesity-Induced Diacylglycerol Accumulation and Glucose Intolerance.
Pulmonary Disease, Chronic Obstructive
Muscarinic receptors, leukotriene B4 production and neutrophilic inflammation in COPD patients.
Thyroid Neoplasms
Preclinical Efficacy of a Carboxylesterase 2-Activated Prodrug of Doxazolidine.
Vaccinia
Characterization of Oncolytic Vaccinia Virus Harboring the Human IFNB1 and CES2 Transgenes.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is required for growth on acetylcarnitine and is important for osmoprotection and induction of the virulence factor PlcH
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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). EST2C_MOUSE
561
1
62470
Swiss-Prot
Secretory Pathway (Reliability: 1)
EST2C_RAT
561
1
62170
Swiss-Prot
Secretory Pathway (Reliability: 1)
Q9HTI0_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
331
0
34936
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
determination of acetylcarnitine for diagnosis of chronic fatigue syndrome
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mahadevan, S.; Sauer, F.
Carnitine ester hydrolase of rat liver
J. Biol. Chem.
244
4448-4453
1969
Rattus norvegicus
brenda
Berge, R.K.; Dossland, B.
Differences between microsomal and mitochondrial-matrix palmitoyl-coenzyme A hydrolase, and palmitoyl-L-carnitine hydrolase from rat liver
Biochem. J.
181
119-125
1979
Rattus norvegicus
brenda
Berge, R.K.; Slinde, E.; Farstad, M.
Intracellular localization of long-chain acyl-coenzyme A hydrolase and acyl-L-carnitine hydrolase in brown adipose tissue from guinea pigs
Biochem. J.
182
347-351
1979
Cavia porcellus
brenda
Mentlein, R.; Suttorp, M.; Heymann, E.
Specificity of purified monoacylglycerol lipase, palmitoyl-CoA hydrolase, palmitoyl-carnitine hydrolase, and nonspecific carboxylesterase from rat liver microsomes
Arch. Biochem. Biophys.
228
230-246
1984
Rattus norvegicus
brenda
Mentlein, R.; Reuter, G.; Heymann, E.
Specificity of two different purified acylcarnitine hydrolases from rat liver, their identity with other carboxylesterases, and their possible function
Arch. Biochem. Biophys.
240
801-810
1985
Rattus norvegicus
brenda
Mentlein, R.; Rix-Matzen, H.; Heymann, E.
Subcellular localization of non-specific carboxylesterases, acylcarnitine hydrolase, monoacylglycerol lipase and palmitoyl-CoA hydrolase in rat liver
Biochim. Biophys. Acta
964
319-328
1988
Rattus norvegicus
brenda
Mentlein, R.; Schumann, M.; Heymann, E.
Comparative chemical and immunological characterization of five lipolytic enzymes (carboxylesterases) from rat liver microsomes
Arch. Biochem. Biophys.
234
612-621
1984
Rattus norvegicus
brenda
Hagen, L.E.; Berge, R.K.; Farstad, M.
Different subcellular localization of palmitoyl-L-carnitine hydrolysis in human and rat liver
FEBS Lett.
104
297-299
1979
Homo sapiens
brenda
Mentlein, R.
The tumor promoter 12-O-tetradecanoyl phorbol 13-acetate and regulatory diacylglycerols are substrates for the same carboxylesterase
J. Biol. Chem.
261
7816-7818
1986
Rattus norvegicus
brenda
Berge, R.K.; Farstad, M.
Dual localization of long-chain acyl-CoA hydrolase in rat liver: one in the microsomes and one in the mitochondrial matrix
Eur. J. Biochem.
95
89-97
1979
Rattus norvegicus
brenda
Matsumoto, K.; Takahashi, M.; Takiyama, N.; Misaki, H.; Matsuo, N.; Murano, S.; Yuki, H.
Enzyme reactor for urinary acylcarnitines assay by reversed-phase high-performance liquid chromatography
Clin. Chim. Acta
216
135-143
1993
Alcaligenes sp.
brenda
Furihata, T.; Hosokawa, M.; Nakata, F.; Satoh, T.; Chiba, K.
Purification, molecular cloning, and functional expression of inducible liver acylcarnitine hydrolase in C57BL/6 mouse, belonging to the carboxylesterase multigene family
Arch. Biochem. Biophys.
416
101-109
2003
Mus musculus, Mus musculus C57BL/6
brenda
Tomita, K.; Sakurada, S.; Minami, S.
Enzymatic determination of acetylcarnitine for diagnostic applications
J. Pharm. Biomed. Anal.
24
1147-1150
2001
Alcaligenes sp.
brenda
Furihata, T.; Hosokawa, M.; Satoh, T.; Chiba, K.
Synergistic role of specificity proteins and upstream stimulatory factor 1 in transactivation of the mouse carboxylesterase 2/microsomal acylcarnitine hydrolase gene promoter
Biochem. J.
384
101-110
2004
Mus musculus
brenda
Meadows, J.A.; Wargo, M.J.
Characterization of Pseudomonas aeruginosa growth on O-acylcarnitines and identification of a short-chain acylcarnitine hydrolase
Appl. Environ. Microbiol.
79
3355-3363
2013
Pseudomonas aeruginosa (Q9HTI0), Pseudomonas aeruginosa
brenda
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