Literature summary for 2.3.2.13 extracted from

Spolaore, B.; Raboni, S.; Satwekar, A.A.; Grigoletto, A.; Mero, A.; Montagner, I.M.; Rosato, A.; Pasut, G.; Fontana, A.
Site-specific transglutaminase-mediated conjugation of interferon alpha-2b at glutamine or lysine residues (2016), Bioconjug. Chem., 27, 2695-2706 .

Search for more literature for 2.3.2.13

Application

Application	Comment	Organism
synthesis	TGase can be used for the development of site-specific derivatives of IFN alpha-2b possessing interesting antiviral and pharmacokinetic properties	Streptomyces mobaraensis

Protein Variants

Protein Variants	Comment	Organism
additional information	site-specific transglutaminase-mediated conjugation of interferon alpha-2b at glutamine or lysine residues	Streptomyces mobaraensis

Organism

Organism	UniProt	Comment	Textmining
Streptomyces mobaraensis	P81453	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	site-specific transglutaminase-mediated conjugation of interferon alpha-2b at glutamine or lysine residues. Reactivity of IFN alpha-2b to microbial transglutaminase (TGase) allows site-specific conjugation of this protein drug. Production of two monoderivatized isomers of IFN with high yields, mass spectrometry analysis of the two conjugates indicating that they are exclusively modified at the level of Gln101 if the protein is reacted in the presence of an amino-containing ligand (i.e. dansylcadaverine) or at the level of Lys164 if a glutamine-containing molecule is used (i.e. carbobenzoxy-L-glutaminyl-glycine, ZQG). The enzyme is absolutely specific, among the 10 Lys and 12 Gln residues of the protein, only Gln101 and Lys164 are located in highly flexible protein regions	Streptomyces mobaraensis	?	-	-

Synonyms

Synonyms	Comment	Organism
microbial transglutaminase	-	Streptomyces mobaraensis
TGase	-	Streptomyces mobaraensis

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Release 2023.1 (January 2023)