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Literature summary extracted from

  • Calvio, C.; Romagnuolo, F.; Vulcano, F.; Speranza, G.; Morelli, C.
    Data for the synthesis of oligo-gamma-glutamylglutamines as model compounds for gamma-glutamyltransferases (GGTs) and for normalization of activities of different GGTs (2018), Data Brief, 21, 576-581 .
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid Bacillus subtilis
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 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid Bacillus subtilis 168
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 a peptide + a 5-L-glutamyl amino acid
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Bacillus subtilis P54422
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-
2.3.2.2 Bacillus subtilis 168 P54422
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 (gamma-L-glutamyl)-4-nitroanilide + glycylglycine chromogenic gamma-glutamyl-4-nitroanilide (GPNA) reacts as the donor substrate affording the gamma-glutamyl-enzyme intermediate through reaction with the catalytically active threonine residue at the N-terminus of the small subunit of the enzyme. In this step 4-nitroaniline (PNA) is liberated, which can be spectrophotometrically detected at 410 nm. The gamma-glutamyl-enzyme intermediate is then resolved by nucleophilic attack of the free amino group of glycylglycine, present in solution in excess amount. The transpeptidation product gamma-glutamylglycylglycine is formed and the enzyme is restored in its free state, able to start a new catalytic cycle. The reaction of the gamma-glutamyl enzyme intermediate with a nucleophile is the rate-determining step of the process, thus the rate of liberation of PNA is usually considered a measure of the rate of the transpeptidase activity Bacillus subtilis 4-nitroaniline + gamma-glutamylglycylglycine
-
 ?
2.3.2.2 (gamma-L-glutamyl)-4-nitroanilide + glycylglycine chromogenic gamma-glutamyl-4-nitroanilide (GPNA) reacts as the donor substrate affording the gamma-glutamyl-enzyme intermediate through reaction with the catalytically active threonine residue at the N-terminus of the small subunit of the enzyme. In this step 4-nitroaniline (PNA) is liberated, which can be spectrophotometrically detected at 410 nm. The gamma-glutamyl-enzyme intermediate is then resolved by nucleophilic attack of the free amino group of glycylglycine, present in solution in excess amount. The transpeptidation product gamma-glutamylglycylglycine is formed and the enzyme is restored in its free state, able to start a new catalytic cycle. The reaction of the gamma-glutamyl enzyme intermediate with a nucleophile is the rate-determining step of the process, thus the rate of liberation of PNA is usually considered a measure of the rate of the transpeptidase activity Bacillus subtilis 168 4-nitroaniline + gamma-glutamylglycylglycine
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid
-
 Bacillus subtilis a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid
-
 Bacillus subtilis 168 a peptide + a 5-L-glutamyl amino acid
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.2 gamma-glutamyltransferase
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 Bacillus subtilis
2.3.2.2 GGT
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 Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 8.2
-
 assay at Bacillus subtilis

General Information

EC Number General Information Comment Organism
2.3.2.2 physiological function gamma-glutamyltransferases (GGTs) are widespread, conserved enzymes that catalyze the transfer of the gamma-glutamyl moiety from a donor substrate to water (hydrolysis, EC 3.4.19.13) or to an acceptor amino acid (transpeptidation)through the formation of a gamma-glutamyl enzyme intermediate Bacillus subtilis