CES1

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Carboxylesterase 1 (monocyte/macrophage serine esterase 1)
PDB rendering based on 1mx1.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols CES1 ; ACAT; CEH; CES2; HMSE; HMSE1; MGC117365; PCE-1; SES1; TGH
External IDs Template:OMIM5 Template:MGI HomoloGene35606
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Carboxylesterase 1 (monocyte/macrophage serine esterase 1), also known as CES1, is a human gene.[1]

Carboxylesterase 1 is a member of a large multigene family. The enzymes encoded by these genes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolize long-chain fatty acid esters and thioesters. This enzyme is known to hydrolyze aromatic and aliphatic esters and is necessary for cellular cholesterol esterification. It may also play a role in detoxification in the lung and/or protection of the central nervous system from ester or amide compounds. Carboxylesterase deficiency may be associated with non-Hodgkin lymphoma or B-cell lymphocytic leukemia. Three transcript variants encoding three different isoforms have been found for this gene.[1]

References

  1. 1.0 1.1 "Entrez Gene: CES1 carboxylesterase 1 (monocyte/macrophage serine esterase 1)".

Further reading

  • Riddles PW, Richards LJ, Bowles MR, Pond SM (1992). "Cloning and analysis of a cDNA encoding a human liver carboxylesterase". Gene. 108 (2): 289–92. PMID 1748313.
  • Munger JS, Shi GP, Mark EA; et al. (1991). "A serine esterase released by human alveolar macrophages is closely related to liver microsomal carboxylesterases". J. Biol. Chem. 266 (28): 18832–8. PMID 1918003.
  • Long RM, Calabrese MR, Martin BM, Pohl LR (1991). "Cloning and sequencing of a human liver carboxylesterase isoenzyme". Life Sci. 48 (11): PL43–9. PMID 1997784.
  • Zschunke F, Salmassi A, Kreipe H; et al. (1991). "cDNA cloning and characterization of human monocyte/macrophage serine esterase-1". Blood. 78 (2): 506–12. PMID 2070086.
  • Ketterman AJ, Bowles MR, Pond SM (1990). "Purification and characterization of two human liver carboxylesterases". Int. J. Biochem. 21 (12): 1303–12. PMID 2612723.
  • Becker A, Böttcher A, Lackner KJ; et al. (1994). "Purification, cloning, and expression of a human enzyme with acyl coenzyme A: cholesterol acyltransferase activity, which is identical to liver carboxylesterase". Arterioscler. Thromb. 14 (8): 1346–55. PMID 8049197.
  • Kroetz DL, McBride OW, Gonzalez FJ (1993). "Glycosylation-dependent activity of baculovirus-expressed human liver carboxylesterases: cDNA cloning and characterization of two highly similar enzyme forms". Biochemistry. 32 (43): 11606–17. PMID 8218228.
  • Shibata F, Takagi Y, Kitajima M; et al. (1993). "Molecular cloning and characterization of a human carboxylesterase gene". Genomics. 17 (1): 76–82. doi:10.1006/geno.1993.1285. PMID 8406473.
  • Langmann T, Becker A, Aslanidis C; et al. (1997). "Structural organization and characterization of the promoter region of a human carboxylesterase gene". Biochim. Biophys. Acta. 1350 (1): 65–74. PMID 9003459.
  • Brzezinski MR, Spink BJ, Dean RA; et al. (1997). "Human liver carboxylesterase hCE-1: binding specificity for cocaine, heroin, and their metabolites and analogs". Drug Metab. Dispos. 25 (9): 1089–96. PMID 9311626.
  • Yan B, Matoney L, Yang D (1999). "Human carboxylesterases in term placentae: enzymatic characterization, molecular cloning and evidence for the existence of multiple forms". Placenta. 20 (7): 599–607. doi:10.1053/plac.1999.0407. PMID 10452915.
  • Mori M, Hosokawa M, Ogasawara Y; et al. (1999). "cDNA cloning, characterization and stable expression of novel human brain carboxylesterase". FEBS Lett. 458 (1): 17–22. PMID 10518925.
  • Islam MR, Waheed A, Shah GN; et al. (1999). "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. 372 (1): 53–61. doi:10.1006/abbi.1999.1449. PMID 10562416.
  • Ghosh S (2001). "Cholesteryl ester hydrolase in human monocyte/macrophage: cloning, sequencing, and expression of full-length cDNA". Physiol. Genomics. 2 (1): 1–8. PMID 11015575.
  • Ghosh S, Natarajan R (2001). "Cloning of the human cholesteryl ester hydrolase promoter: identification of functional peroxisomal proliferator-activated receptor responsive elements". Biochem. Biophys. Res. Commun. 284 (4): 1065–70. doi:10.1006/bbrc.2001.5078. PMID 11409902.
  • Alam M, Ho S, Vance DE, Lehner R (2002). "Heterologous expression, purification, and characterization of human triacylglycerol hydrolase". Protein Expr. Purif. 24 (1): 33–42. doi:10.1006/prep.2001.1553. PMID 11812220.
  • Satoh T, Taylor P, Bosron WF; et al. (2002). "Current progress on esterases: from molecular structure to function". Drug Metab. Dispos. 30 (5): 488–93. PMID 11950776.
  • Alam M, Vance DE, Lehner R (2002). "Structure-function analysis of human triacylglycerol hydrolase by site-directed mutagenesis: identification of the catalytic triad and a glycosylation site". Biochemistry. 41 (21): 6679–87. PMID 12022871.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Bencharit S, Morton CL, Xue Y; et al. (2003). "Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme". Nat. Struct. Biol. 10 (5): 349–56. doi:10.1038/nsb919. PMID 12679808.

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