Takeuchi Y, Birckbichler P J, Patterson M K, Lee K N
Samuel Roberts Noble Foundation Inc., Biomedical Division, Ardmore, OK 73402.
FEBS Lett. 1992 Jul 28;307(2):177-80. doi: 10.1016/0014-5793(92)80762-6.
Three peptides corresponding to glycine-rich internal sequences of the guinea pig liver transglutaminase molecule were synthesized. These were peptide 1 (amino acid residues 520-544), peptide 2 (amino acid residues 345-367) and peptide 3 (amino acid residues 45-69). All of the synthetic peptides demonstrated significant binding ability for both ATP and GTP. Peptide 1 was the best protector of transglutaminase activity from both ATP and GTP inhibition, while peptides 2 and 3 protected the activity only from GTP inhibition. The data shown here lead us to propose putative binding site(s) for ATP and GTP guinea pig liver transglutaminase.
