biostudies-literatureAtkinson LENIH GrantNIDDK NIH HHSDepartment of Employment and LearningNIAID NIH HHS97-106https://www.ebi.ac.uk/biostudies/studies/S-EPMC2908762biostudies-literatureUnknown173(2)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 andMolecular and biochemical parasitologyA PAL for Schistosoma mansoni PHM.PMC2908762R01 DK032949R01 AI049162DK-32949R37 DK032949R56 DK032949AI49162Kimber MJMaule AGAtkinson LEMcVeigh PDay TAEipper BAMarks NJMains REfalseA PAL for Schistosoma mansoni PHM.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 and2010-01-01T00:00:00Z2010 Oct2025-04-18T11:45:04.814Z2019-03-27T00:32:38ZS-EPMC29087622048821210.1016/j.molbiopara.2010.05.009