AADAC

Arylacetamide deacetylase (esterase), also known as AADAC, is a human gene.cite web | title = Entrez Gene: AADAC arylacetamide deacetylase (esterase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=13| accessdate = ]

PBB_Summary
section_title =
summary_text = 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 carcinogenscite web | title = Entrez Gene: AADAC arylacetamide deacetylase (esterase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=13| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Probst MR, Jenö P, Meyer UA |title=Purification and characterization of a human liver arylacetamide deacetylase. |journal=Biochem. Biophys. Res. Commun. |volume=177 |issue= 1 |pages= 453–9 |year= 1991 |pmid= 2043131 |doi=
*cite journal | author=Probst MR, Beer M, Beer D, "et al." |title=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. |journal=J. Biol. Chem. |volume=269 |issue= 34 |pages= 21650–6 |year= 1994 |pmid= 8063807 |doi=
*cite journal | author=Yamazaki K, Kusano K, Tadano K, Tanaka I |title=Radiation hybrid mapping of human arylacetamide deacetylase (AADAC) locus to chromosome 3. |journal=Genomics |volume=44 |issue= 2 |pages= 248–50 |year= 1997 |pmid= 9299245 |doi= 10.1006/geno.1997.4879
*cite journal | author=Ozols J |title=Determination of lumenal orientation of microsomal 50-kDa esterase/N-deacetylase. |journal=Biochemistry |volume=37 |issue= 28 |pages= 10336–44 |year= 1998 |pmid= 9665742 |doi= 10.1021/bi9807916
*cite journal | author=Mziaut H, Korza G, Hand AR, "et al." |title=Targeting proteins to the lumen of endoplasmic reticulum using N-terminal domains of 11beta-hydroxysteroid dehydrogenase and the 50-kDa esterase. |journal=J. Biol. Chem. |volume=274 |issue= 20 |pages= 14122–9 |year= 1999 |pmid= 10318829 |doi=
*cite journal | author=Trickett JI, Patel DD, Knight BL, "et al." |title=Characterization of the rodent genes for arylacetamide deacetylase, a putative microsomal lipase, and evidence for transcriptional regulation. |journal=J. Biol. Chem. |volume=276 |issue= 43 |pages= 39522–32 |year= 2001 |pmid= 11481320 |doi= 10.1074/jbc.M101764200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Saito S, Iida A, Sekine A, "et al." |title=Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. |journal=J. Hum. Genet. |volume=48 |issue= 5 |pages= 249–70 |year= 2003 |pmid= 12721789 |doi= 10.1007/s10038-003-0021-7
*cite journal | author=Frick C, Atanasov AG, Arnold P, "et al." |title=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. |journal=J. Biol. Chem. |volume=279 |issue= 30 |pages= 31131–8 |year= 2004 |pmid= 15152005 |doi= 10.1074/jbc.M313666200
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504

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