{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Atkinson LE"],"funding":["NIH Grant","NIDDK NIH HHS","Department of Employment and Learning","NIAID NIH HHS"],"pagination":["97-106"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2908762"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["173(2)"],"pubmed_abstract":["Parasitic helminth neuromuscular function is a proven target for chemotherapeutic control. Although neuropeptide signalling plays a key role in helminth motor function, it has not yet provided targets for known anthelmintics. The majority of biologically active neuropeptides display a C-terminal amide (NH(2)) motif, generated exclusively by the sequential action of two enzymes, peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidylglycine alpha-amidating lyase (PAL). Further to our previous description of a monofunctional PHM enzyme (SmPHM) from the human blood fluke Schistosoma mansoni, here we describe a cDNA encoding S. mansoni PAL (SmPAL). SmPAL is a monofunctional enzyme which, following heterologous expression, we find to have functionally similar catalytic activity and"],"journal":["Molecular and biochemical parasitology"],"pubmed_title":["A PAL for Schistosoma mansoni PHM."],"pmcid":["PMC2908762"],"funding_grant_id":["R01 DK032949","R01 AI049162","DK-32949","R37 DK032949","R56 DK032949","AI49162"],"pubmed_authors":["Kimber MJ","Maule AG","Atkinson LE","McVeigh P","Day TA","Eipper BA","Marks NJ","Mains RE"],"additional_accession":[]},"is_claimable":false,"name":"A PAL for Schistosoma mansoni PHM.","description":"Parasitic helminth neuromuscular function is a proven target for chemotherapeutic control. Although neuropeptide signalling plays a key role in helminth motor function, it has not yet provided targets for known anthelmintics. The majority of biologically active neuropeptides display a C-terminal amide (NH(2)) motif, generated exclusively by the sequential action of two enzymes, peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidylglycine alpha-amidating lyase (PAL). Further to our previous description of a monofunctional PHM enzyme (SmPHM) from the human blood fluke Schistosoma mansoni, here we describe a cDNA encoding S. mansoni PAL (SmPAL). SmPAL is a monofunctional enzyme which, following heterologous expression, we find to have functionally similar catalytic activity and","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Oct","modification":"2025-04-18T11:45:04.814Z","creation":"2019-03-27T00:32:38Z"},"accession":"S-EPMC2908762","cross_references":{"pubmed":["20488212"],"doi":["10.1016/j.molbiopara.2010.05.009"]}}