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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1994-3-30
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pubmed:abstractText |
We have used a complete, synthetic precursor to adipokinetic hormone I (AKH I) and oligopeptides derived from this precursor as substrates for prohormone-processing enzymes extracted from AKH-synthesizing neurosecretory cells to reconstitute the post-translational steps in AKH biosynthesis in vitro. The results demonstrate the existence of endoproteolytic activity which cleaves the precursor only at the appropriate processing site (at the C-terminal side of Arg13). Further proteolytic processing of C-terminally extended AKH I (AKH-Gly-Lys-Arg) by a carboxypeptidase H-like activity removes the basic residues producing AKH-Gly-Lys, followed by AKH-Gly. Finally, a peptidylglycine-alpha-amidating-monooxygenase activity produces the amidated bioactive product from the glycine-extended peptide in a two-step process, the first of which requires ascorbate and Cu2+. Our results show that all steps in AKH precursor processing can be reconstituted and studied in vitro, providing a system to characterize the processing enzymes and to investigate the development of enzyme inhibitors for use as potential insecticides.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrrolidonecarboxylic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/adipokinetic hormone,
http://linkedlifedata.com/resource/pubmed/chemical/peptidylglycine monooxygenase
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-2956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
219
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
781-9
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:8112329-Amino Acid Sequence,
pubmed-meshheading:8112329-Animals,
pubmed-meshheading:8112329-Carboxypeptidases,
pubmed-meshheading:8112329-Chromatography, High Pressure Liquid,
pubmed-meshheading:8112329-Endopeptidases,
pubmed-meshheading:8112329-Grasshoppers,
pubmed-meshheading:8112329-Insect Hormones,
pubmed-meshheading:8112329-Mixed Function Oxygenases,
pubmed-meshheading:8112329-Molecular Sequence Data,
pubmed-meshheading:8112329-Multienzyme Complexes,
pubmed-meshheading:8112329-Neurosecretory Systems,
pubmed-meshheading:8112329-Oligopeptides,
pubmed-meshheading:8112329-Protease Inhibitors,
pubmed-meshheading:8112329-Protein Precursors,
pubmed-meshheading:8112329-Protein Processing, Post-Translational,
pubmed-meshheading:8112329-Pyrrolidonecarboxylic Acid,
pubmed-meshheading:8112329-Substrate Specificity
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pubmed:year |
1994
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pubmed:articleTitle |
Reconstitution of adipokinetic hormone biosynthesis in vitro indicates steps in prohormone processing.
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pubmed:affiliation |
Sussex Centre for Neuroscience, School of Biological Sciences, University of Sussex, England.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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