Prolyl endopeptidase cleaves the apoptosis rescue peptide humanin and exhibits an unknown post-cysteine cleavage specificity.
Bär
Joachim Wolfgang
JW
Departments of Molecular Biology & Enzymology, Probiodrug AG, Weinbergweg 22, 06120 Halle (Saale), Germany.
Rahfeld
Jens-Ulrich
JU
Schulz
Ingo
I
Gans
Kathrin
K
Ruiz-Carrillo
David
D
Manhart
Susanne
S
Rosche
Fred
F
Demuth
Hans-Ulrich
HU
D000595:Amino Acid Sequence; D000818:Animals; D017209:Apoptosis / Q000502:physiology; D002460:Cell Line; D003545:Cysteine / Q000378:metabolism*; D018819:Dipeptidyl Peptidase 4 / Q000235:genetics / Q000378:metabolism; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
D047908:Intracellular Signaling Peptides and Proteins; C427211:humanin; D018819:Dipeptidyl Peptidase 4; D012697:Serine Endopeptidases; C000705287:PREPL protein, human; D000085822:Prolyl Oligopeptidases; D003545:Cysteine