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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1998-1-26
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pubmed:databankReference | |
pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/peptidylglycine monooxygenase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
241
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
509-12
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9425301-Amino Acid Sequence,
pubmed-meshheading:9425301-Animals,
pubmed-meshheading:9425301-Base Sequence,
pubmed-meshheading:9425301-Glycine,
pubmed-meshheading:9425301-Mixed Function Oxygenases,
pubmed-meshheading:9425301-Molecular Sequence Data,
pubmed-meshheading:9425301-Multienzyme Complexes,
pubmed-meshheading:9425301-Nervous System,
pubmed-meshheading:9425301-Neuropeptides,
pubmed-meshheading:9425301-Oxygenases,
pubmed-meshheading:9425301-Peptides,
pubmed-meshheading:9425301-Sea Anemones,
pubmed-meshheading:9425301-Sequence Homology, Amino Acid,
pubmed-meshheading:9425301-Species Specificity
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pubmed:year |
1997
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pubmed:articleTitle |
Molecular cloning of a peptidylglycine alpha-hydroxylating monooxygenase from sea anemones.
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pubmed:affiliation |
Department of Cell Biology and Anatomy, University of Copenhagen, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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