"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"cd05666"	"{'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}"	"{}"	"[{'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}]"	""	""	""	""	False	False	False	"{'PUB00079894': {'PMID': 16313167, 'ISBN': None, 'volume': '44', 'issue': '48', 'year': 2005, 'title': 'Roles of dimerization domain residues in binding and catalysis by aminoacylase-1.', 'URL': None, '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': None, 'volume': '87', 'issue': '8', 'year': 2005, 'title': 'Catabolism of intracellular N-terminal acetylated proteins: involvement of acylpeptide hydrolase and acylase.', 'URL': None, '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': None, 'volume': '568', 'issue': '1-3', 'year': 2004, 'title': 'Aminoacylase 1 is a sphingosine kinase 1-interacting protein.', 'URL': None, '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': None, 'volume': '248', 'issue': None, 'year': 1995, 'title': 'Evolutionary families of metallopeptidases.', 'URL': None, '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': None, 'volume': '278', 'issue': '45', 'year': 2003, 'title': 'Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family.', 'URL': None, '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': None, 'volume': '78', 'issue': '3', 'year': 2006, 'title': 'Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism.', 'URL': None, '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'}}"	""	"{'name': 'M20 Peptidase aminoacylase 1 subfamily', 'short': 'M20_Acy1-like'}"	""	""	"{'accession': 'cl14876', 'name': 'Zinc_peptidase_like'}"	"cdd"	"domain"	""