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Literature summary extracted from

  • Rajput, R.; Verma, V.V.; Chaudhary, V.; Gupta, R.
    A hydrolytic gamma-glutamyl transpeptidase from thermo-acidophilic archaeon Picrophilus torridus: binding pocket mutagenesis and transpeptidation (2012), Extremophiles, 17, 29-41.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.2 expression in Escherichia coli Picrophilus torridus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.2 H369N mutation introduces significant transpeptidase activity. Mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate Picrophilus torridus
2.3.2.2 R346A mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate Picrophilus torridus
2.3.2.2 R346E mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate Picrophilus torridus
2.3.2.2 Y327E mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate Picrophilus torridus
2.3.2.2 Y327N mutation introduces significant transpeptidase activity. Mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate. The mutant enzyme retains more than 90% transpeptidase activity in the presence of Ba2+, Ca2+, Cu2+, Mg2+, Mn2+, and Zn2+ and is completely inhibited by Cd2+, Co2+, Fe2+, Hg2+, Ni2+ and Pb2+ Picrophilus torridus
2.3.2.2 Y349D mutation results in lowering of KM in hydrolysis of gamma-L-glutamyl-4-nitroanilide and in decline in hydrolytic rate Picrophilus torridus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.2 6-diazo-4 oxonorleucine 1 mM, complete inhibition of hydrolysis of gamma-L-glutamyl-4-nitroanilide Picrophilus torridus
2.3.2.2 azaserine 1 mM, complete inhibition of hydrolysis of gamma-L-glutamyl-4-nitroanilide Picrophilus torridus
2.3.2.2 Cu2+
-
 Picrophilus torridus
2.3.2.2 additional information the enzyme retains more than 90% of the gamma-L-glutamyl-4-nitroanilide hydrolase activity in the presence of most of divalent cations like Ba2+, Ca2+, Co2+, Cd2+, Fe2+, Hg2+, Mg2+, Mn2+ and Zn2+. The enzyme retains more than 90% of the gamma-L-glutamyl-4-nitroanilide hydrolase activity in the presence of 10 mM chelating agents like EDTA, EGTA and 1,10-phenanthroline and is not inhibited by N-bromosuccinimide and iodoacetic acid. Reducing agents like dithiothreitol and 2-mercaptoethanol have no significant effect on the activity Picrophilus torridus
2.3.2.2 Ni2+
-
 Picrophilus torridus
2.3.2.2 phenylmethylsulfonyl fluoride 1 mM, complete inhibition of hydrolysis of gamma-L-glutamyl-4-nitroanilide Picrophilus torridus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.2 0.0143
-
 gamma-L-glutamyl-4-nitroanilide pH 7.0, temperature not specified in the publication, hydrolytic activity, mutant enzyme H368S Picrophilus torridus
2.3.2.2 0.025
-
 gamma-L-glutamyl-4-nitroanilide pH 7.0, temperature not specified in the publication, transpeptidase activity with Gly-Gly as acceptor, mutant enzyme H368S Picrophilus torridus
2.3.2.2 0.025
-
 gamma-L-glutamyl-4-nitroanilide pH 7.0, temperature not specified in the publication, transpeptidase activity with Gly-Gly as acceptor, mutant enzyme Y327N Picrophilus torridus
2.3.2.2 0.067
-
 gamma-L-glutamyl-4-nitroanilide pH 7.0, temperature not specified in the publication, hydrolytic activity, mutant enzyme Y327N Picrophilus torridus
2.3.2.2 0.1
-
 gamma-L-glutamyl-4-nitroanilide pH 7.0, temperature not specified in the publication, hydrolytic activity, wild-type enzyme Picrophilus torridus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.2.2 17000
-
 1 * 17000 + 1 * 30000, SDS-PAGE Picrophilus torridus
2.3.2.2 30000
-
 1 * 17000 + 1 * 30000, SDS-PAGE Picrophilus torridus
2.3.2.2 47000
-
 unprocessed precursor, SDS-PAGE Picrophilus torridus

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Picrophilus torridus Q6KZT2
-
-
2.3.2.2 Picrophilus torridus DSM 9790 Q6KZT2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.2
-
 Picrophilus torridus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 gamma-L-glutamyl-4-nitroanilide + Gly-Gly the enzyme also catalyzes the hydrolase reaction: gamma-L-glutamyl-4-nitroanilide + H2O = L-glutamate + 4-nitroaniline Picrophilus torridus 4-nitroaniline + gamma-L-glutamyl-Gly-Gly
-
 ?
2.3.2.2 gamma-L-glutamyl-4-nitroanilide + Gly-Gly the enzyme also catalyzes the hydrolase reaction: gamma-L-glutamyl-4-nitroanilide + H2O = L-glutamate + 4-nitroaniline Picrophilus torridus DSM 9790 4-nitroaniline + gamma-L-glutamyl-Gly-Gly
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.2.2 heterodimer 1 * 17000 + 1 * 30000, SDS-PAGE Picrophilus torridus

Synonyms

EC Number Synonyms Comment Organism
2.3.2.2 gamma-glutamyl transpeptidase
-
 Picrophilus torridus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.2 55
-
 hydrolysis of gamma-L-glutamyl-4-nitroanilide Picrophilus torridus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.3.2.2 40 60 more than 40% of maximal activity, hydrolysis of gamma-L-glutamyl-4-nitroanilide Picrophilus torridus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.2.2 45
-
 24 h, no loss of gamma-L-glutamyl-4-nitroanilide hydrolase activity Picrophilus torridus
2.3.2.2 50
-
 t1/2: 1 h, gamma-L-glutamyl-4-nitroanilide hydrolase activity Picrophilus torridus
2.3.2.2 60
-
 t1/2: 30 min, gamma-L-glutamyl-4-nitroanilide hydrolase activity Picrophilus torridus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 7
-
 hydrolysis of gamma-L-glutamyl-4-nitroanilide Picrophilus torridus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.2.2 4 9 more than 40% of maximal activity, hydrolysis of gamma-glutamyl-4-nitroanilide Picrophilus torridus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.3.2.2 3 10 25°C, 1 h, more than 50% residual activity Picrophilus torridus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.2.2 25
-
 gamma-L-glutamyl-4-nitroanilide pH 7.0, temperature not specified in the publication, hydrolytic activity, mutant enzyme Y327N Picrophilus torridus
2.3.2.2 39.3
-
 gamma-L-glutamyl-4-nitroanilide pH 7.0, temperature not specified in the publication, hydrolytic activity, wild-type enzyme Picrophilus torridus
2.3.2.2 101
-
 gamma-L-glutamyl-4-nitroanilide pH 7.0, temperature not specified in the publication, hydrolytic activity, mutant enzyme H368S Picrophilus torridus
2.3.2.2 172.8
-
 gamma-L-glutamyl-4-nitroanilide pH 7.0, temperature not specified in the publication, transpeptidase activity with Gly-Gly as acceptor, mutant enzyme H368S Picrophilus torridus
2.3.2.2 182.3
-
 gamma-L-glutamyl-4-nitroanilide pH 7.0, temperature not specified in the publication, transpeptidase activity with Gly-Gly as acceptor, mutant enzyme Y327N Picrophilus torridus