{"metadata":{"accession":"cd05666","entry_id":null,"type":"domain","go_terms":null,"source_database":"cdd","member_databases":null,"integrated":null,"hierarchy":null,"name":{"name":"M20 Peptidase aminoacylase 1 subfamily","short":"M20_Acy1-like"},"description":[{"text":"<p>Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). [[cite:PUB00003579], [cite:PUB00081397], [cite:PUB00030157], [cite:PUB00079894], [cite:PUB00081399], [cite:PUB00081404]]</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00079894":{"PMID":16313167,"ISBN":null,"volume":"44","issue":"48","year":2005,"title":"Roles of dimerization domain residues in binding and catalysis by aminoacylase-1.","URL":null,"raw_pages":"15645-51","medline_journal":"Biochemistry","ISO_journal":"Biochemistry","authors":["Lindner HA","Alary A","Boju LI","Sulea T","Menard R."],"DOI_URL":"http://dx.doi.org/10.1021/bi051180y"},"PUB00081399":{"PMID":15927344,"ISBN":null,"volume":"87","issue":"8","year":2005,"title":"Catabolism of intracellular N-terminal acetylated proteins: involvement of acylpeptide hydrolase and acylase.","URL":null,"raw_pages":"673-85","medline_journal":"Biochimie","ISO_journal":"Biochimie","authors":["Perrier J","Durand A","Giardina T","Puigserver A."],"DOI_URL":"http://dx.doi.org/10.1016/j.biochi.2005.04.002"},"PUB00081404":{"PMID":15196915,"ISBN":null,"volume":"568","issue":"1-3","year":2004,"title":"Aminoacylase 1 is a sphingosine kinase 1-interacting protein.","URL":null,"raw_pages":"30-4","medline_journal":"FEBS Lett","ISO_journal":"FEBS Lett.","authors":["Maceyka M","Nava VE","Milstien S","Spiegel S."],"DOI_URL":"http://dx.doi.org/10.1016/j.febslet.2004.04.093"},"PUB00003579":{"PMID":7674922,"ISBN":null,"volume":"248","issue":null,"year":1995,"title":"Evolutionary families of metallopeptidases.","URL":null,"raw_pages":"183-228","medline_journal":"Methods Enzymol","ISO_journal":"Meth. Enzymol.","authors":["Rawlings ND","Barrett AJ."],"DOI_URL":"http://dx.doi.org/10.1016/0076-6879(95)48015-3"},"PUB00030157":{"PMID":12933810,"ISBN":null,"volume":"278","issue":"45","year":2003,"title":"Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family.","URL":null,"raw_pages":"44496-504","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Lindner HA","Lunin VV","Alary A","Hecker R","Cygler M","Menard R."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M304233200"},"PUB00081397":{"PMID":16465618,"ISBN":null,"volume":"78","issue":"3","year":2006,"title":"Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism.","URL":null,"raw_pages":"401-9","medline_journal":"Am J Hum Genet","ISO_journal":"Am. J. Hum. Genet.","authors":["Sass JO","Mohr V","Olbrich H","Engelke U","Horvath J","Fliegauf M","Loges NT","Schweitzer-Krantz S","Moebus R","Weiler P","Kispert A","Superti-Furga A","Wevers RA","Omran H."],"DOI_URL":"http://dx.doi.org/10.1086/500563"}},"set_info":{"accession":"cl14876","name":"Zinc_peptidase_like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":11475,"pathways":0,"proteins":11474,"proteomes":3380,"sets":1,"structural_models":{"alphafold":8618,"bfvd":0},"structures":0,"taxa":5278},"entry_annotations":{},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}