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{
"metadata": {
"accession": "IPR015654",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0018838",
"name": "mandelate racemase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"sfld": {
"SFLDF00004": "mandelate racemase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR046945",
"name": "L-rhamnonate dehydratase-like",
"type": "Family",
"children": [
{
"accession": "IPR015654",
"name": "Mandelate racemase",
"type": "Family",
"children": []
},
{
"accession": "IPR023444",
"name": "L-rhamnonate dehydratase",
"type": "Family",
"children": [
{
"accession": "IPR034619",
"name": "L-lyxonate dehydratase",
"type": "Family",
"children": []
}
]
},
{
"accession": "IPR033978",
"name": "L-talarate/galactarate dehydratase",
"type": "Family",
"children": []
},
{
"accession": "IPR034382",
"name": "3,6-anhydro-alpha-L-galactonate cycloisomerase",
"type": "Family",
"children": []
},
{
"accession": "IPR034610",
"name": "L-fuconate dehydratase",
"type": "Family",
"children": []
},
{
"accession": "IPR034618",
"name": "D-galactarolactone cycloisomerase",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Mandelate racemase",
"short": "Mandelate_racemase"
},
"description": [
{
"text": "<p>Mandelate racemase ([ec:5.1.2.2]) (MR) in certain bacteria, including Pseudomonas putida, utilise D or L mandelic acid as sole carbon source for energy. Mandelate racemase and muconate lactonizing enzyme ([ec:5.5.1.1]) (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures [[cite:PUB00004081], [cite:PUB00005404]]. A crystal structure has been described [[cite:PUB00034787]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00004081": {
"PMID": 2215699,
"ISBN": null,
"volume": "347",
"issue": "6294",
"year": 1990,
"title": "Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous.",
"URL": null,
"raw_pages": "692-4",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Neidhart DJ",
"Kenyon GL",
"Gerlt JA",
"Petsko GA."
],
"DOI_URL": "http://dx.doi.org/10.1038/347692a0"
},
"PUB00005404": {
"PMID": 8256284,
"ISBN": null,
"volume": "18",
"issue": "10",
"year": 1993,
"title": "On the origin of enzymatic species.",
"URL": null,
"raw_pages": "372-6",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Petsko GA",
"Kenyon GL",
"Gerlt JA",
"Ringe D",
"Kozarich JW."
],
"DOI_URL": "http://dx.doi.org/10.1016/0968-0004(93)90091-Z"
},
"PUB00034787": {
"PMID": 1892834,
"ISBN": null,
"volume": "30",
"issue": "38",
"year": 1991,
"title": "Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-A resolution: identification of the active site and possible catalytic residues.",
"URL": null,
"raw_pages": "9264-73",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Neidhart DJ",
"Howell PL",
"Petsko GA",
"Powers VM",
"Li RS",
"Kenyon GL",
"Gerlt JA."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi00102a019"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036849",
"name": "Enolase-like, C-terminal domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 8,
"pathways": 0,
"proteins": 8,
"proteomes": 2,
"sets": 0,
"structural_models": {
"alphafold": 7,
"bfvd": 0
},
"structures": 10,
"taxa": 22
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "2mnr",
"name": "MECHANISM OF THE REACTION CATALYZED BY MANDELATE RACEMASE. 2. CRYSTAL STRUCTURE OF MANDELATE RACEMASE AT 2.5 ANGSTROMS RESOLUTION: IDENTIFICATION OF THE ACTIVE SITE AND POSSIBLE CATALYTIC RESIDUES"
}
}
}
