Literature summary for 2.3.2.13 extracted from

Ohtake, K.; Mukai, T.; Iraha, F.; Takahashi, M.; Haruna, K.I.; Date, M.; Yokoyama, K.; Sakamoto, K.
Engineering an automaturing transglutaminase with enhanced thermostability by genetic code expansion with two codon reassignments (2018), ACS Synth. Biol., 7, 2170-2176 .

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Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of engineered mutant enzyme in Escherichia coli	Streptomyces mobaraensis

Protein Variants

Protein Variants	Comment	Organism
additional information	engineering an automaturing transglutaminase with enhanced thermostability by genetic code expansion with two codon reassignments. The first amino acid, 3-chloro-L-tyrosine, is incorporated into microbial transglutaminase (MTG) in response to in-frame UAG codons to substitute for the 15 tyrosine residues separately. The two substitutions at positions 20 and 62 are found to each increase thermostability of the enzyme, while the seven substitutions at positions 24, 34, 75, 146, 171, 217, and 310 exhibit neutral effects. Then, these two stabilizing chlorinations are combined with one of the neutral ones, and the most stabilized variant is found to contain 3-chlorotyrosines at positions 20, 62, and 171, exhibiting a half-life 5.1fold longer than that of the wild-type enzyme at 60°C. Next, this MTG variant is further modified by incorporating the alpha-hydroxy acid analogue of Nepsilon-allyloxycarbonyl-L-lysine (AlocKOH), specified by the AGG codon, at the end of the N-terminal inhibitory peptide. The ester bond, thus incorporated into the main chain, efficiently self-cleaves under alkaline conditions (pH 11.0), achieving the autonomous maturation of the thermostabilized MTG in transformed Escherichia coli. Method, overview	Streptomyces mobaraensis

Organism

Organism	UniProt	Comment	Textmining
Streptomyces mobaraensis	P81453	-	-

Synonyms

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

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Release 2023.1 (January 2023)