Identification by protein microsequencing of a proteinase-V8-cleavage site in a folding intermediate of chick muscle creatine kinase.
We have identified by protein microsequencing a glutamic acid residue (Glu-166) in a folding intermediate of chick muscle creatine kinase that is very sensitive to cleavage by staphylococcal proteinase V8. Most other glutamic acid residues, including Glu-168, are already partly protected from proteolytic attack at this stage. After the final stages of protein refolding, when enzyme activity is recovered, Glu-166 is also resistant to proteolysis.
Research Division, N.E. Wales Institute, Deeside, U.K.
G E
GE
Morris
P J
PJ
Jackson
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D003402:Creatine Kinase / Q000737:chemistry*; D005971:Glutamates / Q000737:chemistry; D018698:Glutamic Acid; D008969:Molecular Sequence Data; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments / Q000378:metabolism; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases / Q000378:metabolism*
D005971:Glutamates; D010446:Peptide Fragments; D018698:Glutamic Acid; D003402:Creatine Kinase; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase