TY - JOUR

T1 - Molecular cloning of a peptidylglycine alpha-hydroxylating monooxygenase from sea anemones.

AU - Hauser, F

AU - Williamson, M

AU - Grimmelikhuijzen, C J

N1 - Keywords: Amino Acid Sequence; Animals; Base Sequence; Glycine; Mixed Function Oxygenases; Molecular Sequence Data; Multienzyme Complexes; Nervous System; Neuropeptides; Oxygenases; Peptides; Sea Anemones; Sequence Homology, Amino Acid; Species Specificity

PY - 1997

Y1 - 1997

N2 - 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. Udgivelsesdato: 1997-Dec-18

AB - 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. Udgivelsesdato: 1997-Dec-18

U2 - 10.1006/bbrc.1997.7854

DO - 10.1006/bbrc.1997.7854

M3 - Journal article

C2 - 9425301

VL - 241

SP - 509

EP - 512

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -