Literature summary for 2.3.2.2 extracted from

Bindal, S.; Dagar, V.; Saini, M.; Khasa, Y.; Gupta, R.
High level extracellular production of recombinant gamma-glutamyl transpeptidase from Bacillus licheniformis in Escherichia coli fed-batch culture (2018), Enzyme Microb. Technol., 116, 23-32 .

Application

Application	Comment	Organism
diagnostics	the GGT enzyme is known as a diagnostic enzyme for liver and biliary related diseases	Bacillus licheniformis
food industry	GGT has gained importance as a biotechnologically important catalyst in food sector. In food sector, GGT enzyme finds application in soy sauce industry, debittering of amino acids, synthesis of flavor enhancer, and nutraceutical peptides such as L-theanine	Bacillus licheniformis
synthesis	in pharmaceutical and medical sectors GGT enzyme can be exploited in the synthesis of pro-drugs and therapeutic compounds such as gamma-glutamyl DOPA, gamma-D-glutamyl-L-tryptophan, and gamma-glutamyl-taurine	Bacillus licheniformis

Cloned(Commentary)

Cloned (Comment)	Organism
gene blggt, recombinant overexpression of extracellular enzyme in Escherichia coli strain BL21(DE3) in bioreactor under batch and fed-batch condition, development and optimization of a cost-effective method for overexpression and preparation of bacterial GGT enzyme for its industrial applications, method optimization, overview. The native signal is used for extracellular expression of the enzyme in Escherichia coli. Enzyme activity of 24500 U/l in the extracellular medium after 24 h. Subcloning in Escherichia coli strain DH5alpha, expression studies in Escherichia coli strains M!5 and BL21(DE3)	Bacillus licheniformis

Cloned (Comment)

Organism

gene blggt, recombinant overexpression of extracellular enzyme in Escherichia coli strain BL21(DE3) in bioreactor under batch and fed-batch condition, development and optimization of a cost-effective method for overexpression and preparation of bacterial GGT enzyme for its industrial applications, method optimization, overview. The native signal is used for extracellular expression of the enzyme in Escherichia coli. Enzyme activity of 24500 U/l in the extracellular medium after 24 h. Subcloning in Escherichia coli strain DH5alpha, expression studies in Escherichia coli strains M!5 and BL21(DE3)

Bacillus licheniformis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	-	Bacillus licheniformis	-	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
a (5-L-glutamyl)-peptide + an amino acid	Bacillus licheniformis	-	a peptide + a 5-L-glutamyl amino acid	-	?
a (5-L-glutamyl)-peptide + an amino acid	Bacillus licheniformis ER15	-	a peptide + a 5-L-glutamyl amino acid	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus licheniformis	A9YTT0	-	-
Bacillus licheniformis ER15	A9YTT0	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
(gamma-L-glutamyl)-4-nitroanilide + glycylglycine	quantitative measurement of release of 4-nitroaniline	Bacillus licheniformis	4-nitroaniline + gamma-glutamylglycylglycine	-	?
(gamma-L-glutamyl)-4-nitroanilide + glycylglycine	quantitative measurement of release of 4-nitroaniline	Bacillus licheniformis ER15	4-nitroaniline + gamma-glutamylglycylglycine	-	?
a (5-L-glutamyl)-peptide + an amino acid	-	Bacillus licheniformis	a peptide + a 5-L-glutamyl amino acid	-	?
a (5-L-glutamyl)-peptide + an amino acid	-	Bacillus licheniformis ER15	a peptide + a 5-L-glutamyl amino acid	-	?

Synonyms

Synonyms	Comment	Organism
gamma-glutamyl transpeptidase	-	Bacillus licheniformis
GGT	-	Bacillus licheniformis
SBLGGT	-	Bacillus licheniformis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	60	assay at	Bacillus licheniformis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
9	-	assay at	Bacillus licheniformis

General Information

General Information	Comment	Organism
physiological function	gamma-glutamyl transpeptidase (GGT) catalyzes the transfer of gamma-glutamyl moiety from a donor molecule to an acceptor molecule by cleavage and subsequent formation of a gamma-amide bond. The acceptor can be an amino acid, a peptide or a water molecule. Under physiological conditions, GGT enzyme expression from wild strains of bacteria, such as Escherichia coli and Bacillus, is tightly regulated because of the involvement of the enzyme in various stress and starvation conditions	Bacillus licheniformis