AADAC

From Wikipedia, the free encyclopedia

Arylacetamide deacetylase (esterase)

Identifiers

AADAC; CES5A1; DAC

External IDs

OMIM: 600338 MGI: 1915008 HomoloGene: 37436

Gene ontology
Molecular Function:	• lipase activity • deacetylase activity
Cellular Component:	• endoplasmic reticulum • endoplasmic reticulum membrane • microsome • membrane • integral to membrane
Biological Process:	• metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001086 (mRNA)
NP_001077 (protein)

NM_023383 (mRNA)
NP_075872 (protein)

Location

Chr 3: 153.01 - 153.03 Mb

Chr 3: 60.12 - 60.13 Mb

Pubmed search

[1]

[2]

Arylacetamide deacetylase (esterase), also known as AADAC, is a human gene.^[1]

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^[1]

[edit] References

^ ^a ^b Entrez Gene: AADAC arylacetamide deacetylase (esterase).

[edit] 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. PMID 2043131.
Probst MR, Beer M, Beer D, et al. (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.
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. 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. 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. PMID 15489334.