Post-translational processing in Xenopus oocytes includes carboxyl-terminal amidation.
Xenopus oocytes are versatile cells capable of carrying out many post-translational processes. Although previously reported not to be capable of C-terminal amidation, this report demonstrates that Xenopus oocytes do indeed have an amidating enzyme. The amidating activity from Xenopus ovaries is compared to the known amidating activity found in porcine pituitaries. The demonstration of C-terminal amidation by Xenopus oocytes extends their usefulness in studying post-translational events.
D000581:Amidohydrolases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D005260:Female; D009865:Oocytes / Q000201:enzymology*; D010053:Ovary / Q000201:enzymology; D010902:Pituitary Gland / Q000201:enzymology; D011499:Protein Processing, Post-Translational; D013552:Swine; D014982:Xenopus laevis
D000581:Amidohydrolases