HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept
{
"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
}
}
