Preferred substrate sequences for transglutaminase 2: screening using a phage-displayed peptide library.
A large number of substrate proteins for tissue transglutaminase (TGase 2) have been identified in vivo and in vitro. Preference in primary sequence or secondary structure around the reactive glutamine residues in the substrate governs the reactivity for TGase 2. We established a screening system to identify preferable sequence as a glutamine-donor substrate using a phage-displayed peptide library. The results showed that several peptide sequences have higher reactivity and specificity to TGase 2 than those of preferable sequences previously reported. By analysis of the most reactive 12-amino acid sequence, T26 (HQSYVDPWMLDH), residues crucial to the enzymatic reaction were investigated. The following review summarizes the screening system and also the preference in substrate sequences that were obtained by this method and those previously reported.
Hitomi
Kiyotaka
K
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601, Japan. hitomi@agr.nagoya-u.ac.jp
Kitamura
Miyako
M
Sugimura
Yoshiaki
Y
D000595:Amino Acid Sequence; D019204:GTP-Binding Proteins / Q000378:metabolism*; D019151:Peptide Library; D000091345:Protein Glutamine gamma Glutamyltransferase 2; D020539:Sequence Analysis, Protein; D013379:Substrate Specificity; D011503:Transglutaminases / Q000378:metabolism*
D019151:Peptide Library; D000091345:Protein Glutamine gamma Glutamyltransferase 2; D011503:Transglutaminases; D019204:GTP-Binding Proteins