Abstract
It has been previously reported that both the cysteinyl-endo-oligopeptidase A and the metalloendopeptidase EC 3.4.24.15 are able to generate enkephalin from a number of enkephalin-containing peptides, including dynorphin A1-8. The present study shows that only endo-oligopeptidase A is able to generate [Leu5]enkephalin and [Met5]enkephalin from dynorphin A1-8 and from metorphamide respectively. It is also shown that endo-oligopeptidase A neither hydrolyses the specific EC 3.4.24.15 substrate alpha-N-benzoyl-Gly-Ala-Ala-Phe p-aminobenzoate, nor is inhibited by the specific EC 3.4.24.15 inhibitor N-[1(RS)-carboxy-2-phenylethyl]-alpha-Ala-Ala-Phe p-aminobenzoate.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Chemical Precipitation
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Cysteine Endopeptidases / immunology
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Cysteine Endopeptidases / metabolism*
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Cysteine Proteinase Inhibitors
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Dynorphins / metabolism*
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Enkephalin, Methionine / analogs & derivatives*
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Enkephalin, Methionine / metabolism
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Enkephalins / metabolism*
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Metalloendopeptidases / antagonists & inhibitors
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Metalloendopeptidases / immunology
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Metalloendopeptidases / metabolism*
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Peptide Fragments / metabolism*
Substances
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Cysteine Proteinase Inhibitors
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Enkephalins
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Peptide Fragments
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Enkephalin, Methionine
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Dynorphins
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dynorphin (1-8)
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adrenorphin
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Cysteine Endopeptidases
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Metalloendopeptidases
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thimet oligopeptidase