title: Substrate specificities of microbial transglutaminase for primary amines.
abstract: Transglutaminase (epsilon-glutaminyl-peptide:amine gamma-glutaminyl-transferase, EC 2.3.2.13) (TGase) is an enzyme that catalyzes acyl transfer reactions between primary amines and Gln residues in proteins and peptides. The substrate specificity of TGase for primary amines was investigated to incorporate various functional groups into proteins and peptides. In this study, microbial transglutaminase and guinea pig liver transglutaminase were used. For the primary amines to be incorporated into benzyloxycarbonyl-L-Gln-Gly (Z-Gln-Gly), they were required to have more than four carbon chains without side chains between the functional groups. These results suggest that with appropriate primary amines as spacers, various functional groups, carboxyl groups, phosphate groups, saccharides, and so on, can be incorporated into proteins by using TGase.
authors.affiliation: Food Research and Development Laboratories, Ajinomoto Company, Inc., 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki-shi, 210-8681 Japan. tomoko_ootsuka@ajinomoto.com
authors.forename: T
authors.initials: T
authors.lastname: Ohtsuka
authors.forename: A
authors.initials: A
authors.lastname: Sawa
authors.forename: R
authors.initials: R
authors.lastname: Kawabata
authors.forename: N
authors.initials: N
authors.lastname: Nio
authors.forename: M
authors.initials: M
authors.lastname: Motoki
mesh_terms: D000588:Amines; D000818:Animals; D001419:Bacteria / Q000201:enzymology*; D006168:Guinea Pigs; D008099:Liver / Q000201:enzymology*; D013379:Substrate Specificity; D011503:Transglutaminases / Q000378:metabolism*
chemical_list: D000588:Amines; D011503:Transglutaminases