Liver carboxylesterase 1

Details

Name
Liver carboxylesterase 1
Kind
protein
Synonyms
  • ACAT
  • Acyl-coenzyme A:cholesterol acyltransferase
  • Brain carboxylesterase hBr1
  • Carboxylesterase 1
  • CE-1
  • CEH
  • CES2
  • Cholesteryl ester hydrolase
  • Cocaine carboxylesterase
  • Egasyn
  • hCE-1
  • HMSE
  • Methylumbelliferyl-acetate deacetylase 1
  • Monocyte/macrophage serine esterase
  • REH
  • Retinyl ester hydrolase
  • Serine esterase 1
  • SES1
  • TGH
  • Triacylglycerol hydrolase
Gene Name
CES1
UniProtKB Entry
P23141Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0005305|Liver carboxylesterase 1
MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPL
GPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLN
IYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST
GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLF
HRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLK
MKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIP
MQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDL
IADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPF
LKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLK
DKEVAFWTNLFAKKAVEKPPQTEHIEL
Number of residues
567
Molecular Weight
62520.62
Theoretical pI
6.58
GO Classification
Functions
carboxylesterase activity
Processes
cellular response to cholesterol / cellular response to low-density lipoprotein particle stimulus / cholesterol biosynthetic process / cholesterol ester hydrolysis involved in cholesterol transport / cholesterol homeostasis / cholesterol metabolic process / medium-chain fatty acid metabolic process / negative regulation of cholesterol storage / positive regulation of cholesterol efflux / positive regulation of cholesterol metabolic process / regulation of bile acid biosynthetic process / regulation of bile acid secretion / reverse cholesterol transport
Components
cytoplasm / cytosol / endoplasmic reticulum / lipid droplet
General Function
Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs (PubMed:18762277, PubMed:7980644, PubMed:9169443, PubMed:9490062). Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester (PubMed:18762277, PubMed:7980644, PubMed:9169443, PubMed:9490062). Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine (PubMed:7980644). Catalyzes the transesterification of cocaine to form cocaethylene (PubMed:7980644). Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate (PubMed:7980644). Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins (PubMed:21049984). Hydrolyzes cellular cholesteryl esters to free cholesterols and promotes reverse cholesterol transport (RCT) by facilitating both the initial and final steps in the process (PubMed:11015575, PubMed:16024911, PubMed:16971496, PubMed:18762277). First of all, allows free cholesterol efflux from macrophages to extracellular cholesterol acceptors and secondly, releases free cholesterol from lipoprotein-delivered cholesteryl esters in the liver for bile acid synthesis or direct secretion into the bile (PubMed:16971496, PubMed:18599737, PubMed:18762277)
Specific Function
carboxylesterase activity
Pfam Domain Function
Signal Regions
1-17
Transmembrane Regions
Not Available
Cellular Location
Endoplasmic reticulum lumen
Gene sequence
>lcl|BSEQ0021334|Liver carboxylesterase 1 (CES1)
ATGTGGCTCCGTGCCTTTATCCTGGCCACTCTCTCTGCTTCCGCGGCTTGGGGGCATCCG
TCCTCGCCACCTGTGGTGGACACCGTGCATGGCAAAGTGCTGGGGAAGTTCGTCAGCTTA
GAAGGATTTGCACAGCCTGTGGCCATTTTCCTGGGAATCCCTTTTGCCAAGCCGCCTCTT
GGACCCCTGAGGTTTACTCCACCGCAGCCTGCAGAACCATGGAGCTTTGTGAAGAATGCC
ACCTCGTACCCTCCTATGTGCACCCAAGATCCCAAGGCGGGGCAGTTACTCTCAGAGCTA
TTTACAAACCGAAAGGAGAACATTCCTCTCAAGCTTTCTGAAGACTGTCTTTACCTCAAT
ATTTACACTCCTGCTGACTTGACCAAGAAAAACAGGCTGCCGGTGATGGTGTGGATCCAC
GGAGGGGGGCTGATGGTGGGTGCGGCATCAACCTATGATGGGCTGGCCCTTGCTGCCCAT
GAAAACGTGGTGGTGGTGACCATTCAATATCGCCTGGGCATCTGGGGATTCTTCAGCACA
GGGGATGAACACAGCCGGGGGAACTGGGGTCACCTGGACCAGGTGGCTGCCCTGCGCTGG
GTCCAGGACAACATTGCCAGCTTTGGAGGGAACCCAGGCTCTGTGACCATCTTTGGAGAG
TCAGCGGGAGGAGAAAGTGTCTCTGTTCTTGTTTTGTCTCCATTGGCCAAGAACCTCTTC
CACCGGGCCATTTCTGAGAGTGGCGTGGCCCTCACTTCTGTTCTGGTGAAGAAAGGTGAT
GTCAAGCCCTTGGCTGAGCAAATTGCTATCACTGCTGGGTGCAAAACCACCACCTCTGCT
GTCATGGTTCACTGCCTGCGACAGAAGACGGAAGAGGAGCTCTTGGAGACGACATTGAAA
ATGAAATTCTTATCTCTGGACTTACAGGGAGACCCCAGAGAGAGTCAACCCCTTCTGGGC
ACTGTGATTGATGGGATGCTGCTGCTGAAAACACCTGAAGAGCTTCAAGCTGAAAGGAAT
TTCCACACTGTCCCCTACATGGTCGGAATTAACAAGCAGGAGTTTGGCTGGTTGATTCCA
ATGCAGTTGATGAGCTATCCACTCTCCGAAGGGCAACTGGACCAGAAGACAGCCATGTCA
CTCCTGTGGAAGTCCTATCCCCTTGTTTGCATTGCTAAGGAACTGATTCCAGAAGCCACT
GAGAAATACTTAGGAGGAACAGACGACACTGTCAAAAAGAAAGACCTGTTCCTGGACTTG
ATAGCAGATGTGATGTTTGGTGTCCCATCTGTGATTGTGGCCCGGAACCACAGAGATGCT
GGAGCACCCACCTACATGTATGAGTTTCAGTACCGTCCAAGCTTCTCATCAGACATGAAA
CCCAAGACGGTGATAGGAGACCACGGGGATGAGCTCTTCTCCGTCTTTGGGGCCCCATTT
TTAAAAGAGGGTGCCTCAGAAGAGGAGATCAGACTTAGCAAGATGGTGATGAAATTCTGG
GCCAACTTTGCTCGCAATGGAAACCCCAATGGGGAAGGGCTGCCCCACTGGCCAGAGTAC
AACCAGAAGGAAGGGTATCTGCAGATTGGTGCCAACACCCAGGCGGCCCAGAAGCTGAAG
GACAAAGAAGTAGCTTTCTGGACCAACCTCTTTGCCAAGAAGGCAGTGGAGAAGCCACCC
CAGACAGAACACATAGAGCTGTGA
Chromosome Location
16
Locus
16q12.2
External Identifiers
ResourceLink
UniProtKB IDP23141
UniProtKB Entry NameEST1_HUMAN
GenBank Gene IDM73499
GeneCard IDCES1
GenAtlas IDCES1
HGNC IDHGNC:1863
PDB ID(s)1MX1, 1MX5, 1MX9, 1YA4, 1YA8, 1YAH, 1YAJ, 2DQY, 2DQZ, 2DR0, 2H7C, 2HRQ, 2HRR, 3K9B, 4AB1, 5A7F, 5A7G, 5A7H, 8EOR
KEGG IDhsa:1066
IUPHAR/Guide To Pharmacology ID2592
NCBI Gene ID1066
General References
  1. Munger JS, Shi GP, Mark EA, Chin DT, Gerard C, Chapman HA: A serine esterase released by human alveolar macrophages is closely related to liver microsomal carboxylesterases. J Biol Chem. 1991 Oct 5;266(28):18832-8. [Article]
  2. Kroetz DL, McBride OW, Gonzalez FJ: Glycosylation-dependent activity of baculovirus-expressed human liver carboxylesterases: cDNA cloning and characterization of two highly similar enzyme forms. Biochemistry. 1993 Nov 2;32(43):11606-17. [Article]
  3. Shibata F, Takagi Y, Kitajima M, Kuroda T, Omura T: Molecular cloning and characterization of a human carboxylesterase gene. Genomics. 1993 Jul;17(1):76-82. [Article]
  4. Becker A, Bottcher A, Lackner KJ, Fehringer P, Notka F, Aslanidis C, Schmitz G: Purification, cloning, and expression of a human enzyme with acyl coenzyme A: cholesterol acyltransferase activity, which is identical to liver carboxylesterase. Arterioscler Thromb. 1994 Aug;14(8):1346-55. [Article]
  5. Islam MR, Waheed A, Shah GN, Tomatsu S, Sly WS: Human egasyn binds beta-glucuronidase but neither the esterase active site of egasyn nor the C terminus of beta-glucuronidase is involved in their interaction. Arch Biochem Biophys. 1999 Dec 1;372(1):53-61. [Article]
  6. Ghosh S: Cholesteryl ester hydrolase in human monocyte/macrophage: cloning, sequencing, and expression of full-length cDNA. Physiol Genomics. 2000 Jan 24;2(1):1-8. [Article]
  7. Alam M, Ho S, Vance DE, Lehner R: Heterologous expression, purification, and characterization of human triacylglycerol hydrolase. Protein Expr Purif. 2002 Feb;24(1):33-42. [Article]
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  10. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  11. Mori M, Hosokawa M, Ogasawara Y, Tsukada E, Chiba K: cDNA cloning, characterization and stable expression of novel human brain carboxylesterase. FEBS Lett. 1999 Sep 10;458(1):17-22. [Article]
  12. Brzezinski MR, Abraham TL, Stone CL, Dean RA, Bosron WF: Purification and characterization of a human liver cocaine carboxylesterase that catalyzes the production of benzoylecgonine and the formation of cocaethylene from alcohol and cocaine. Biochem Pharmacol. 1994 Nov 1;48(9):1747-55. [Article]
  13. Schindler R, Mentlein R, Feldheim W: Purification and characterization of retinyl ester hydrolase as a member of the non-specific carboxylesterase supergene family. Eur J Biochem. 1998 Feb 1;251(3):863-73. [Article]
  14. Satoh T, Hosokawa M: Molecular aspects of carboxylesterase isoforms in comparison with other esterases. Toxicol Lett. 1995 Dec;82-83:439-45. [Article]
  15. Alam M, Vance DE, Lehner R: Structure-function analysis of human triacylglycerol hydrolase by site-directed mutagenesis: identification of the catalytic triad and a glycosylation site. Biochemistry. 2002 May 28;41(21):6679-87. [Article]
  16. Long RM, Calabrese MR, Martin BM, Pohl LR: Cloning and sequencing of a human liver carboxylesterase isoenzyme. Life Sci. 1991;48(11):PL43-9. [Article]
  17. Zschunke F, Salmassi A, Kreipe H, Buck F, Parwaresch MR, Radzun HJ: cDNA cloning and characterization of human monocyte/macrophage serine esterase-1. Blood. 1991 Jul 15;78(2):506-12. [Article]
  18. Riddles PW, Richards LJ, Bowles MR, Pond SM: Cloning and analysis of a cDNA encoding a human liver carboxylesterase. Gene. 1991 Dec 15;108(2):289-92. [Article]
  19. Pindel EV, Kedishvili NY, Abraham TL, Brzezinski MR, Zhang J, Dean RA, Bosron WF: Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin. J Biol Chem. 1997 Jun 6;272(23):14769-75. [Article]
  20. Zhu HJ, Patrick KS, Yuan HJ, Wang JS, Donovan JL, DeVane CL, Malcolm R, Johnson JA, Youngblood GL, Sweet DH, Langaee TY, Markowitz JS: Two CES1 gene mutations lead to dysfunctional carboxylesterase 1 activity in man: clinical significance and molecular basis. Am J Hum Genet. 2008 Jun;82(6):1241-8. doi: 10.1016/j.ajhg.2008.04.015. Epub 2008 May 15. [Article]
  21. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
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  24. Bencharit S, Morton CL, Xue Y, Potter PM, Redinbo MR: Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme. Nat Struct Biol. 2003 May;10(5):349-56. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
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AvasimibeinvestigationalyestargetinhibitorDetails
Capecitabineapproved, investigationalnoenzymesubstrateDetails
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Indomethacinapproved, investigationalunknownenzymesubstrateDetails
MevastatinexperimentalunknownenzymeinhibitorDetails
4-Piperidino-PiperidineexperimentalyestargetinhibitorDetails
Cholic AcidapprovedyestargetinhibitorDetails
(1R)-1,2,2-trimethylpropyl (R)-methylphosphinateexperimentalunknowntargetDetails
(1S,7S,8S,8AR)-1,2,3,7,8,8A-HEXAHYDRO-7-METHYL-8-[2-[(2R,4R)-TETRAHYDRO-4-HY DROXY-6-OXO-2H-PYRAN-2-YL]ETHYL]-1-NAPHTHALENOLexperimentalunknowntargetDetails
Ciclesonideapproved, investigationalunknownenzymesubstrateDetails
Levocarnitineapproved, investigationalunknowntargetDetails
CyclandelateapprovedunknowntargetDetails
Probucolapproved, investigationalunknowntargetDetails
Benzocaineapproved, investigationalunknownenzymeinhibitorDetails
TrandolaprilapprovedunknownenzymesubstrateDetails
RufinamideapprovedunknownenzymesubstrateDetails
Dabigatran etexilateapprovedunknownenzymesubstrateDetails
ClopidogrelapprovednoenzymesubstrateDetails
Mycophenolate mofetilapproved, investigationalunknownenzymesubstrateDetails
SelexipagapprovednoenzymesubstrateDetails
Phenylacetic acidapprovedunknownenzymesubstrateDetails
MeperidineapprovedunknowntargetDetails
Dextropropoxypheneapproved, illicit, investigational, withdrawnunknowntargetDetails
Naloxoneapproved, vet_approvedunknowntargetbinderDetails
Tacrineapproved, investigational, withdrawnunknowntargetDetails
Cocaineapproved, illicitunknowntargetbinderDetails
Diamorphineapproved, illicit, investigationalunknowntargetDetails
PropoxycaineapprovedunknownenzymesubstrateDetails
HomatropineapprovedunknownenzymesubstrateDetails
Tenofovir alafenamideapprovednoenzymesubstrateDetails
OseltamivirapprovedyesenzymesubstrateDetails
Quinaprilapproved, investigationalunknownenzymesubstrateDetails
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Remimazolamapproved, investigationalunknownenzymesubstrateDetails
Filgotinibapproved, investigationalunknownenzymemetabolizerDetails
Remdesivirapproved, investigationalyesenzymesubstrateDetails
Flupentixolapproved, investigational, withdrawnnoenzymeinhibitorDetails
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Cannabidiolapproved, investigationalnoenzymeinhibitorDetails
Dronabinolapproved, illicitnoenzymeinhibitorDetails
Cannabinolexperimental, investigationalunknownenzymeinhibitorDetails
Medical Cannabisexperimental, investigationalunknownenzymeinhibitorDetails
SimvastatinapprovedunknownenzymeinhibitorDetails
Telotristat ethylapproved, investigationalnoenzymesubstrateDetails
N-MethylnaloxoniumexperimentalyestargetinhibitorDetails
Benzoinapproved, experimentalyestargetinhibitorDetails
1,1,1-TRIFLUORO-3-(OCTYLTHIO)ACETONEexperimentalyestargetinhibitorDetails
PactimibeinvestigationalyestargetinhibitorDetails