CES1
From Wikipedia, the free encyclopedia
Carboxylesterase 1 (monocyte/macrophage serine esterase 1)
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PDB rendering based on 1mx1. | ||||||||||||||
Available structures: 1mx1, 1mx5, 1mx9, 1ya4, 1ya8, 1yah, 1yaj, 2dqy, 2dqz, 2dr0, 2h7c, 2hrq, 2hrr | ||||||||||||||
Identifiers | ||||||||||||||
Symbol(s) | CES1; ACAT; CEH; CES2; HMSE; HMSE1; MGC117365; PCE-1; SES1; TGH | |||||||||||||
External IDs | OMIM: 114835 MGI: 2148202 HomoloGene: 35606 | |||||||||||||
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Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 1066 | 104158 | ||||||||||||
Ensembl | n/a | ENSMUSG00000056973 | ||||||||||||
Uniprot | n/a | Q8VCT4 | ||||||||||||
Refseq | XM_001130190 (mRNA) XP_001130190 (protein) |
NM_053200 (mRNA) NP_444430 (protein) |
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Location | n/a | Chr 8: 96.06 - 96.09 Mb | ||||||||||||
Pubmed search | [1] | [2] |
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]
[edit] References
[edit] 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: . 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: . 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: . 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: . 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: . 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: . 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: . PMID 12679808.