{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10(5)"],"submitter":["Riccio A"],"pubmed_abstract":["Acylpeptide hydrolase (APEH) is a ubiquitous cytosolic protease that plays an important role in the detoxification of oxidised proteins. In this work, to further explore the physiological role of this enzyme, two apeh cDNAs were isolated from the Chionodraco hamatus icefish, which lives in the highly oxygenated Antarctic marine environment. The encoded proteins (APEH-1(Ch) and APEH-2(Ch)) were characterised in comparison with the uniquely expressed isoform from the temperate fish Dicentrarchus labrax (APEH-1Dl) and the two APEHs from the red-blooded Antarctic fish Trematomus bernacchii (APEH-1(Tb) and APEH-2(Tb)). Homology modelling and kinetic characterisation of the APEH isoforms provided new insights into their structure/function properties. APEH-2 isoforms were the only ones capable of"],"journal":["PloS one"],"pagination":["e0125594"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4422685"],"repository":["biostudies-literature"],"pubmed_title":["A New APEH Cluster with Antioxidant Functions in the Antarctic Hemoglobinless Icefish Chionodraco hamatus."],"pmcid":["PMC4422685"],"pubmed_authors":["Facchiano A","Balestrieri M","Palmieri G","Monti G","Cocca E","Palumbo S","Rossi M","Gogliettino M","Riccio A"],"additional_accession":[]},"is_claimable":false,"name":"A New APEH Cluster with Antioxidant Functions in the Antarctic Hemoglobinless Icefish Chionodraco hamatus.","description":"Acylpeptide hydrolase (APEH) is a ubiquitous cytosolic protease that plays an important role in the detoxification of oxidised proteins. In this work, to further explore the physiological role of this enzyme, two apeh cDNAs were isolated from the Chionodraco hamatus icefish, which lives in the highly oxygenated Antarctic marine environment. The encoded proteins (APEH-1(Ch) and APEH-2(Ch)) were characterised in comparison with the uniquely expressed isoform from the temperate fish Dicentrarchus labrax (APEH-1Dl) and the two APEHs from the red-blooded Antarctic fish Trematomus bernacchii (APEH-1(Tb) and APEH-2(Tb)). Homology modelling and kinetic characterisation of the APEH isoforms provided new insights into their structure/function properties. APEH-2 isoforms were the only ones capable of","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015","modification":"2026-05-01T21:16:56.375Z","creation":"2019-03-26T23:32:32Z"},"accession":"S-EPMC4422685","cross_references":{"pubmed":["25946123"],"doi":["10.1371/journal.pone.0125594"]}}