AADAC

Arylacetamide deacetylase
Identifiers
Symbols	AADAC ; CES5A1; DAC
External IDs	OMIM: 600338 MGI: 1915008 HomoloGene: 37436 GeneCards: AADAC Gene
EC number	3.1.1.3
Gene ontology Molecular function • catalytic activity • triglyceride lipase activity • lipase activity • serine hydrolase activity • deacetylase activity Cellular component • endoplasmic reticulum membrane • integral component of membrane Biological process • metabolic process • positive regulation of triglyceride catabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
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 Mb	Chr 3: 60.03 – 60.04 Mb
PubMed search

Arylacetamide deacetylase is an enzyme that in humans is encoded by the AADAC gene.^[1][2]

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^[2]

References

1. 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.
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.

External links

• AADAC human gene location in the UCSC Genome Browser.
• AADAC human gene details in the UCSC Genome Browser.