Stadelmann B, Bütikofer P, König A, Brodbeck U
Institute of Biochemistry and Molecular Biology, University of Bern, Switzerland.
Biochim Biophys Acta. 1997 Feb 4;1355(2):107-13. doi: 10.1016/s0167-4889(96)00119-x.
Glycosylphosphatidylinositol-specific phospholipase D (GPI-PLD) (EC 3.1.4.50) from mammalian serum is a 115 kDa glycoprotein consisting of 816 amino acids. We found that C-terminal deletions of only two to five amino acids reduced GPI-PLD enzymatic activity by roughly 70% as compared to wild-type protein. C-terminal deletions of more than five amino acids resulted in a complete loss of GPI-PLD enzymatic activity. Point mutations at position 811 indicate that Tyr-811 may play a major role in maintaining the biological activity of GPI-PLD.