Literature summary for 2.3.2.2 extracted from

Lin, L.L.; Yang, L.Y.; Hu, H.Y.; Lo, H.F.
Influence of N-terminal truncations on the functional expression of Bacillus licheniformis gamma-glutamyltranspeptidase in recombinant Escherichia coli (2008), Curr. Microbiol., 57, 603-608.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Bacillus licheniformis

Protein Variants

Protein Variants	Comment	Organism
additional information	expression of full length gene and six truncations lacking 36, 129, 132, 135, 144, and 174 bp, respectively, at the 5' end in Escherichia coli. Mutant proteins derived from genes lacking 135 and 144 bp show no enzymatic activity. Mutants derived of truncations of 36. 129, 132 process autocatalytically their precursors into alpha- und beta-subunits at 4°C	Bacillus licheniformis

Organism

Organism	UniProt	Comment	Textmining
Bacillus licheniformis	-	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.2	-	mutant derived from truncation of 132 bp at the 5' end, pH 8.0, 40°C	Bacillus licheniformis
0.8	-	mutant derived from truncation of 129 bp at the 5' end, pH 8.0, 40°C	Bacillus licheniformis
1.3	-	mutant derived from truncation of 36 bp at the 5' end, pH 8.0, 40°C	Bacillus licheniformis
51.9	-	wild-type, pH 8.0, 40°C	Bacillus licheniformis

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)