AADAC

AADAC
Identifiers
AliasesAADAC, CES5A1, DAC, arylacetamide deacetylase
External IDsMGI: 1915008 HomoloGene: 37436 GeneCards: AADAC
EC number3.1.1.3
Gene location (Human)
Chr.Chromosome 3 (human)[1]
Band3q25.1Start151,814,037 bp[1]
End151,828,488 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

13

67758

Ensembl

ENSG00000114771

ENSMUSG00000027761

UniProt

P22760

Q99PG0

RefSeq (mRNA)

NM_001086

NM_023383

RefSeq (protein)

NP_001077

NP_075872

Location (UCSC)Chr 3: 151.81 – 151.83 MbChr 3: 60.03 – 60.04 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Arylacetamide deacetylase is an enzyme that in humans is encoded by the AADAC gene.[5][6]

Microsomal arylacetamide deacetylase competes against the activity of cytosolic arylamine N-acetyltransferase, which catalyzes one of the initial biotransformation pathways for arylamine and heterocyclic amine carcinogens[6]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000114771 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027761 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Probst MR, Beer M, Beer D, Jeno P, Meyer UA, Gasser R (Sep 1994). "Human liver arylacetamide deacetylase. Molecular cloning of a novel esterase involved in the metabolic activation of arylamine carcinogens with high sequence similarity to hormone-sensitive lipase". J Biol Chem. 269 (34): 21650–6. PMID 8063807.
  6. 1 2 "Entrez Gene: AADAC arylacetamide deacetylase (esterase)".

Further reading

  • Probst MR, Jenö P, Meyer UA (1991). "Purification and characterization of a human liver arylacetamide deacetylase". Biochem. Biophys. Res. Commun. 177 (1): 453–9. doi:10.1016/0006-291X(91)92005-5. PMID 2043131.
  • Yamazaki K, Kusano K, Tadano K, Tanaka I (1997). "Radiation hybrid mapping of human arylacetamide deacetylase (AADAC) locus to chromosome 3". Genomics. 44 (2): 248–50. doi:10.1006/geno.1997.4879. PMID 9299245.
  • Ozols J (1998). "Determination of lumenal orientation of microsomal 50-kDa esterase/N-deacetylase". Biochemistry. 37 (28): 10336–44. doi:10.1021/bi9807916. PMID 9665742.
  • Mziaut H, Korza G, Hand AR, et al. (1999). "Targeting proteins to the lumen of endoplasmic reticulum using N-terminal domains of 11beta-hydroxysteroid dehydrogenase and the 50-kDa esterase". J. Biol. Chem. 274 (20): 14122–9. doi:10.1074/jbc.274.20.14122. PMID 10318829.
  • Trickett JI, Patel DD, Knight BL, et al. (2001). "Characterization of the rodent genes for arylacetamide deacetylase, a putative microsomal lipase, and evidence for transcriptional regulation". J. Biol. Chem. 276 (43): 39522–32. doi:10.1074/jbc.M101764200. PMID 11481320.
  • 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. PMC 139241. PMID 12477932.
  • Saito S, Iida A, Sekine A, et al. (2003). "Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population". J. Hum. Genet. 48 (5): 249–70. doi:10.1007/s10038-003-0021-7. PMID 12721789.
  • Frick C, Atanasov AG, Arnold P, et al. (2004). "Appropriate function of 11beta-hydroxysteroid dehydrogenase type 1 in the endoplasmic reticulum lumen is dependent on its N-terminal region sharing similar topological determinants with 50-kDa esterase". J. Biol. Chem. 279 (30): 31131–8. doi:10.1074/jbc.M313666200. PMID 15152005.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.


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