An active carbonyl formed during glycosylphosphatidylinositol addition to a protein is evidence of catalysis by a transamidase.

@article{Maxwell1995AnAC,
  title={An active carbonyl formed during glycosylphosphatidylinositol addition to a protein is evidence of catalysis by a transamidase.},
  author={Stephen E. Maxwell and Sandhya Ramalingam and Louise Diekmann Gerber and Larry Brink and Sidney Udenfriend},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 33},
  pages={
          19576-82
        }
}
Glycosylphosphatidylinositol (GPI) substitution is now recognized to be a ubiquitous method of anchoring a protein to membranes in eukaryotes. The structure of GPI and its biosynthetic pathways are known and the signals in a nascent protein for GPI addition have been elucidated. The enzyme(s) responsible for GPI addition with release of a COOH-terminal signal peptide has been considered to be a transamidase but has yet to be isolated, and evidence that it is a transamidase is indirect. The… CONTINUE READING

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