Literature summary for 2.3.2.13 extracted from

Plagmann, I.; Chalaris, A.; Kruglov, A.A.; Nedospasov, S.; Rosenstiel, P.; Rose-John, S.; Scheller, J.
Transglutaminase-catalyzed covalent multimerization of Camelidae anti-human TNF single domain antibodies improves neutralizing activity (2009), J. Biotechnol., 142, 170-178.

Search for more literature for 2.3.2.13

Organism

Organism	UniProt	Comment	Textmining
Streptomyces mobaraensis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	posttranslational dimerization and multimerization of Camelidae anti-human TNF single domain antibodies in vitro catalyzed by microbial transglutaminases. Ribonuclease S-tag-peptide acts as a peptidyl substrate in covalent protein cross-linking reactions catalyzed by MTG. C-terminally fusion of the S-tag sequence to the anti-hTNF-variable heavy chain-domain results in fusion proteins that are efficiently dimerized and multimerized by MTG whereas anti-hTNF-variable heavy chain domain is not susceptible to protein crosslinking	Streptomyces mobaraensis	?	-	?

Synonyms

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)