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.
Takeuchi
Y
Y
Samuel Roberts Noble Foundation Inc., Biomedical Division, Ardmore, OK 73402.
Birckbichler
P J
PJ
Patterson
M K
MK
Lee
K N
KN
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