Molecular cloning of a peptidylglycine alpha-hydroxylating monooxygenase from sea anemones

Biochemical and Biophysical Research Communications
F HauserC J Grimmelikhuijzen

Abstract

Cnidarians are the lowest animal group having a nervous system. The primitive nervous systems of cnidarians produce large amounts of a variety of neuropeptides, of which many or perhaps all are amidated at their C terminus. In vertebrates, peptide amidation is catalyzed by two enzymes acting sequentially, peptidyl-glycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL). In mammals both enzymatic activities are contained within a bifunctional protein that is coded for by a single gene. Using PCR and degenerated oligonucleotides derived from conserved regions of PHM, we have now cloned a PHM from the sea anemone Calliactis parasitica showing 42% amino acid sequence identity with rat PHM. Among the conserved (identical) amino acid residues are five histidine and one methionine residue, which bind two Cu2+ atoms that are essential for PHM activity. No cDNA coding for PAL could be identified, suggesting that sea anemone PAL is coded for by a gene that is different from the sea anemone PHM gene, a situation similar to the one found in insects. This is the first report on the molecular cloning of a cnidarian PHM.

Citations

Apr 13, 2012·Molecular Biology and Evolution·Rosalind M F AttenboroughEldon E Ball
Jun 17, 2004·Journal of Neurochemistry·Mei HanPaul H Taghert
Nov 15, 2006·Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology·G Kass-Simon, Paola Pierobon
Sep 3, 2013·Toxicon : Official Journal of the International Society on Toxinology·Sabah Ul-HasanPradip K Bandyopadhyay
Mar 30, 2006·Parasitology·P McVeighT A Day
Nov 5, 2003·Journal of Neuroscience Research·Traci A CzyzykJohn E Pintar
Mar 1, 2018·The Journal of Biological Chemistry·Sven Van BaelLiesbet Temmerman
Feb 21, 2019·Scientific Reports·Mareen MoellerPeter J Schupp
Jan 14, 2004·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Gunnar R MairTim A Day
Aug 29, 1998·The Journal of Biological Chemistry·A S KolhekarB A Eipper
May 30, 2015·Journal of Enzyme Inhibition and Medicinal Chemistry·Neil R McIntyreDavid J Merkler
Mar 30, 1999·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·S SpijkerW P Geraerts
Oct 12, 2000·Biochemical and Biophysical Research Communications·M WilliamsonC J Grimmelikhuijzen
Oct 24, 2000·Brain Research. Molecular Brain Research·X FanG T Nagle
Mar 27, 2007·Progress in Neurobiology·Steven J HussonLiliane Schoofs

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