Literature summary for 2.3.2.2 extracted from

Chi, M.; Lin, M.; Chen, Y.; Lin, L.; Wang, T.
Functional role of the conserved glycine residues, Gly481 and Gly482, of the gamma-glutamyltranspeptidase from Bacillus licheniformis (2018), Int. J. Biol. Macromol., 109, 1182-1188 .

Search for more literature for 2.3.2.2

Cloned(Commentary)

Cloned (Comment)	Organism
gene ggt, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain M15, subcloning in Escherichia coli strain XL-1 Blue	Bacillus licheniformis

Protein Variants

Protein Variants	Comment	Organism
G481A	site-directed mutagenesis, the mutation affects both autocatalytic processing and catalytic activity of the enzyme, and causes a significant change in the functional integrity of the enzyme, the fluorescence and circular dichroism properties of the mutant proteins are basically consistent with those of BlGGT. The mutant shows increased catalytic activity	Bacillus licheniformis
G481E	site-directed mutagenesis, the mutation affects both autocatalytic processing and catalytic activity of the enzyme, and causes a significant change in the functional integrity of the enzyme, the fluorescence and circular dichroism properties of the mutant proteins are basically consistent with those of BlGGT. The mutant shows increased catalytic activity	Bacillus licheniformis
G481R	site-directed mutagenesis, the mutant shows increased catalytic activity, but abolished processing	Bacillus licheniformis
G482A	site-directed mutagenesis, the mutant shows increased catalytic activity	Bacillus licheniformis
G482E	site-directed mutagenesis, the mutant shows increased catalytic activity	Bacillus licheniformis
G482R	site-directed mutagenesis, the mutation leads to a marked reduction in the autocatalytic processing and results in an unprocessed enzyme with insignificant catalytic activity, the fluorescence and circular dichroism properties of the mutant proteins are basically consistent with those of BlGGT. The mutant shows increased catalytic activity	Bacillus licheniformis
T399A	site-directed mutagenesis, like the wild-type protein, T399A-BlGGT has a stacked alphabetaalphabeta core structure comprising two central beta-sheets and surrounding alpha-helices	Bacillus licheniformis

Organism

Organism	UniProt	Comment	Textmining
Bacillus licheniformis	A0A415J2H1	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	maturation mechanism of autocatalytic processing of BlGGT proceeds with residue Thr417 functioning as the activator. In the structure of T399A-BlGGT, the side-chain of Thr417 is located at a competent position to activate the catalytic threonine (Thr399) and the main chain atoms of this residue is held in position by the side chain of Arg571, which in turn interacts with the side chain of Glu398 through electrostatic interactions. Then, the side chains of Glu398 and Arg571 are held in their spatial positions by the hydrogen bond networks involving His401, Ser479, Gly481, Gly482, Thr484, Asn550, and two water molecules. In this respect, residues Gly481 and Gly482 may play a role in the autocatalytic processing of BlGGT	Bacillus licheniformis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.55	-	purified recombinant mutant G482E, pH 9.0, 40°C	Bacillus licheniformis
1.52	-	purified recombinant mutant G481E, pH 9.0, 40°C	Bacillus licheniformis
7.97	-	purified recombinant mutant G482A, pH 9.0, 40°C	Bacillus licheniformis
9.03	-	purified recombinant mutant G481A, pH 9.0, 40°C	Bacillus licheniformis
11.42	-	purified recombinant wild-type enzyme, pH 9.0, 40°C	Bacillus licheniformis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-gamma-glutamyl-4-nitroanilide + glycylglycine	-	Bacillus licheniformis	4-nitroaniline + 5-L-glutamyl-glycylglycine	-	?

Synonyms

Synonyms	Comment	Organism
BlGGT	-	Bacillus licheniformis
gamma-glutamyltranspeptidase	-	Bacillus licheniformis
GGT	-	Bacillus licheniformis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
40	-	-	Bacillus licheniformis

pH Optimum

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

General Information

General Information	Comment	Organism
additional information	functional role of the conserved glycine residues, Gly481 and Gly482, in gamma-glutamyltranspeptidase reaction. Several residues, including Arg109, Thr399, Glu438, Asp441, Ser460, Ser461, Gly481, and Gly482, are proposed to be involved in the binding of the substrate	Bacillus licheniformis

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)