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Literature summary for 3.4.19.13 extracted from

  • Bindal, S.; Sharma, S.; Singh, T.P.; Gupta, R.
    Evolving transpeptidase and hydrolytic variants of gamma-glutamyl transpeptidase from Bacillus licheniformis by targeted mutations of conserved residue Arg109 and their biotechnological relevance (2017), J. Biotechnol., 249, 82-90 .
    View publication on PubMed
Search for more literature for 3.4.19.13

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 (DE3) Bacillus licheniformis

General Stability

General Stability Organism
mutant enzyme R109M shows high salt stability with almost no loss in activity even in the presence of 20% (w/v) NaCl whereas wild-type enzyme and mutant enzyme R109K retain only 50% of residual activity Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis A9YTT0
-
-
Bacillus licheniformis ER-15 A9YTT0
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus licheniformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
gamma-glutamyl-p-nitroanilide + H2O hydrolytic activity Bacillus licheniformis L-glutamate + p-nitroaniline
-
 ?
additional information the enzyme also shows transpeptidase activity Bacillus licheniformis ?
-
 ?
additional information the enzyme also shows transpeptidase activity Bacillus licheniformis ER-15 ?
-
 ?
additional information the enzyme also shows transpeptidase activity Bacillus licheniformis ER15 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 45000 + x * 22000, SDS-PAGE, all the enzyme variants are of the same molecular weight with large subunit located around 45 kDa and small subunit at 22 kDa Bacillus licheniformis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 optimum of wild-type enzyme, mutant enzyme R109K and R109M Bacillus licheniformis
70
-
 optimum of mutant enzyme R109S Bacillus licheniformis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 t1/2: 176 min (mutant enzyme R109M), 16.5 min (mutant enzyme R109S), 69.3 min (wild-type enzyme), 19.8 min (mutant enzyme R109K) Bacillus licheniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 pH-optimum of mutant enzyme R109M Bacillus licheniformis
9
-
 comparable activities at both pH 9.0 and pH 10.0. A similar pattern is observed for R109S. Mutant enzyme R109K shows a sharp pH-optimum at pH 9.0 Bacillus licheniformis
10
-
 comparable activities at both pH 9.0 and pH 10.0. A similar pattern is observed for R109S Bacillus licheniformis