Conversion of the dynorphins to Leu-enkephalin in human spinal cord.
This study describes three different endopeptidases in human spinal cord with high affinity for the dynorphins. The enzymes, with strict specificity towards paired basic residues, release Leu-enkephalin and its C-terminal extensions - Arg6 and -Arg6 -Arg7 from the substrate peptides. They differ with regard to molecular size, charge properties, and inhibitory profile. Two of the enzymes show optimal activity at neutral pH, whereas the third enzyme has its activity optimum at pH 5.6. They are all suggested to be of importance for the formation of Leu-enkephalin from prodynorphin.
Nyberg
F
F
Department of Pharmacology, University of Uppsala, Sweden.
Silberring
J
J
D000595:Amino Acid Sequence; D004399:Dynorphins / Q000378:metabolism*; D004743:Enkephalin, Leucine / Q000096:biosynthesis*; D004745:Enkephalins / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011498:Protein Precursors / Q000378:metabolism; D012697:Serine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism; D015842:Serine Proteinase Inhibitors; D013116:Spinal Cord / Q000378:metabolism*
D004745:Enkephalins; D011498:Protein Precursors; D015842:Serine Proteinase Inhibitors; D004743:Enkephalin, Leucine; D004399:Dynorphins; C033660:preproenkephalin; D012697:Serine Endopeptidases; C054870:dynorphin-converting endopeptidase