Literature summary for 2.3.2.13 extracted from

Rachel, N.M.; Quaglia, D.; Levesque, E.; Charette, A.B.; Pelletier, J.N.
Engineered, highly reactive substrates of microbial transglutaminase enable protein labeling within various secondary structure elements (2017), Protein Sci., 26, 2268-2279 .

Search for more literature for 2.3.2.13

Application

Application	Comment	Organism
synthesis	microbial transglutaminase (MTG) is a practical tool to enzymatically form isopeptide bonds between peptide or protein substrates, crosslinking the side-chains of reactive glutamine and lysine residues is solidly rooted in food and textile processing. MTG-reactive glutamines can be readily introduced into a protein domain for fluorescent labeling, method evaluation, overview	Streptomyces mobaraensis

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)	Streptomyces mobaraensis

Protein Variants

Protein Variants	Comment	Organism
additional information	introducing point mutations within MTG's active site increases reactivity toward the most reactive substrate variant, I6Q-GB1, enhancing MTG's capacity to fluorescently label an engineered, highly reactive glutamine substrate	Streptomyces mobaraensis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
protein glutamine + alkylamine	Streptomyces mobaraensis	-	protein N5-alkylglutamine + NH3	-	?

Organism

Organism	UniProt	Comment	Textmining
Streptomyces mobaraensis	P81453	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Streptomyces mobaraensis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	microbial transglutaminase (MTG) is a practical tool to enzymatically form isopeptide bonds between peptide or protein substrates. Engineered, highly reactive substrates of microbial transglutaminase enable protein labeling within various secondary structure elements. MTG can react readily with glutamines in alpha-helical, beta-sheet, and unstructured loop elements and does not favor one type of secondary structure. Building of a GB1 library where each variant contains a single glutamine at positions covering all secondary structure elements, detailed overview. The most reactive and selective variants display an over 100fold increase in incorporation compared to another developed aminated benzo[a]imidazo[2,1,5-cd]indolizine-type fluorophore, relative to native GB1	Streptomyces mobaraensis	?	-	-
N-CBZ-Glu-Gly + hydroxylamine	-	Streptomyces mobaraensis	CBZ-Glu-(gamma-monohydroxamate)-Gly + NH3	-	?
protein glutamine + alkylamine	-	Streptomyces mobaraensis	protein N5-alkylglutamine + NH3	-	?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Streptomyces mobaraensis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	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)