Specificity of guinea pig liver transglutaminase for amine substrates.
The amine specificity of guinea pig liver transglutaminase, a model enzyme for endo-gamma-glutamine:epsilon-lysin transferases, was explored with the aid of synthetic substrates of high apparent affinities. As exemplified by dansyl- (5-dimethylamino-1-naphthalenesulfonyl), (2,4-dinitrobenzenesulfonyl)-, and (2,4,6-triisopropylbenzenesulfonyl)-cadaverines--each of which showed affinities of approximately 4 x 10(7) M-1--the best amine substrates carried a large hydrophobic substituent attached to an alkylamine side chain of about 7.2 A in length. Altogether, our results point to the importance of a hydrophobic binding region in the enzyme from where the alkyl side chain reaches into a narrow crevice toward the active center and positions the primary amine of the substrate for attacking the carbonyl group of the acyl enzyme intermediate.
D000588:Amines / Q000138:chemical synthesis; D000818:Animals; D006168:Guinea Pigs; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D013379:Substrate Specificity; D005723:gamma-Glutamyltransferase / Q000378:metabolism*
D000588:Amines; D005723:gamma-Glutamyltransferase