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Literature summary extracted from

  • Chi, M.; Lin, M.; Huang, Y.; Chen, Y.; Wang, T.; Lin, L.
    Enzymatic synthesis of L-theanine from L-glutamine and ethylamine by Bacillus licheniformis gamma-glutamyltranspeptidase and its mutants specialized in transpeptidase activity (2019), Biocatal. Agricult. Biotechnol., 22, 101393 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.2 gene ggt, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain M15, the recombinant BlGGT confers the ability to catalyze the synthesis of gamma-L-glutamyl-S-allyl-L-cysteine, gamma-glutamyl-L-phenylalanine, and gamma-glutamyl-L-leucine Bacillus licheniformis

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.2 additional information the transpeptidase-specialized mutants (N450D and N450Q) of enzyme GGT are employed for the biocatalytic synthesis of L-theanine (gamma-glutamyl-L-ethylamide). Preparative biocatalytic synthesis of L-theanine from a reaction mixture of L-Gln, ethanolamine, and borate buffer, pH 10.5, 37°C. Use of L-theanine as one kind of gamma-glutamyl donor for the transpeptidation action by the enzyme. The L-theanine production by wild-type BlGGT, mutant N450D, and mutant N450Q at pH 10.5 results in the individual yields of 56, 88, and 61%, respectively. The product yield is proportionally increased with the L-Gln concentration and reaches a maximum at a donor substrate concentration of 250 mM Bacillus licheniformis
2.3.2.2 N450D site-directed mutagenesis, the mutant shows increased theanine biosynthetic activity compared to wild-type Bacillus licheniformis
2.3.2.2 N450Q site-directed mutagenesis, the mutant's theanine biosynthetic activity is similar to wild-type Bacillus licheniformis
2.3.2.2 T399A site-directed mutagenesis, precursor mimic mutant, structure analysis Bacillus licheniformis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid Bacillus licheniformis
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 a peptide + a 5-L-glutamyl amino acid
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 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Bacillus licheniformis A0A415J2H1
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-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.2 recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain M15 to near homogeneity by nickel affinity chromatography Bacillus licheniformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid
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 Bacillus licheniformis a peptide + a 5-L-glutamyl amino acid
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 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-phenylalanine
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 Bacillus licheniformis 4-nitroaniline + 5-L-glutamyl-L-phenylalanine
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 ?
2.3.2.2 additional information the recombinantly expressed BlGGT confers the ability to catalyze the synthesis of gamma-L-glutamyl-S-allyl-L-cysteine, gamma-glutamyl-L-phenylalanine, and gamma-glutamyl-L-leucine. The transpeptidation activity of recombinant enzyme BlGGT and mutants N450D and N450Q is assayed in triplicate with L-gamma-glutamyl-4-nitroanilide and Gly-Gly as the substrates. Preparative biocatalytic synthesis of L-theanine from a reaction mixture of L-Gln, ethanolamine, and borate buffer, pH 10.5, 37°C. Use of L-theanine as one kind of gamma-glutamyl donor for the transpeptidation action by the enzyme. The L-theanine production by wild-type BlGGT, mutant N450D, and mutant N450Q at pH 10.5 results in the individual yields of 56, 88, and 61%, respectively Bacillus licheniformis ?
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Synonyms

EC Number Synonyms Comment Organism
2.3.2.2 gamma-glutamyltranspeptidase
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 Bacillus licheniformis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.2 37
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 assay at Bacillus licheniformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 10.5
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-
 Bacillus licheniformis