Putative nucleotide binding sites of guinea pig liver transglutaminase.
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.
Samuel Roberts Noble Foundation Inc., Biomedical Division, Ardmore, OK 73402.
Y
Y
Takeuchi
P J
PJ
Birckbichler
M K
MK
Patterson
K N
KN
Lee
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006168:Guinea Pigs; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000378:metabolism; D011503:Transglutaminases / Q000378:metabolism*
D010446:Peptide Fragments; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D011503:Transglutaminases