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Literature summary extracted from

  • Walter, F.; Grenz, S.; Ortseifen, V.; Persicke, M.; Kalinowski, J.
    Corynebacterium glutamicum ggtB encodes a functional gamma-glutamyl transpeptidase with gamma-glutamyl dipeptide synthetic and hydrolytic activity (2016), J. Biotechnol., 232, 99-109 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.2 gene ggtB, recombinat expression of GgtB with an N-terminal fusion of the chitin-binding domain and intein tag to the target protein, subcloning in Escherichia coli strain DH5alphaMCR and subsequently transformation into and expression in Escherichia coli strain ER25669 Corynebacterium glutamicum

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.2 additional information deletion of the complete coding sequence of ggtB in the chromosome of Corynebacterium glutamicum. Intracellular concentrations of gamma-glutamyl dipeptides upon deletion and overexpression of gene ggtB in Corynebacterium glutamicum strain ATCC 13032 Corynebacterium glutamicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.2 NaCl at 10% NaCl, GgtBCg still retains 70% of its initial activity. Further addition of NaCl to concentrations of 15%, 20%, and 22.5% reduces the activity to 30%, 27%, and 20%, respectively. For all tested salt concentrations, activity is higher in the presence of glycyl-glycine than in its absence Corynebacterium glutamicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.2 0.123
-
 L-gamma-glutamyl-4-nitroanilide pH 9.6, 37°C, recombinant enzyme Corynebacterium glutamicum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.2.2 cell surface the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane Corynebacterium glutamicum 9986
-
2.3.2.2 membrane the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane Corynebacterium glutamicum 16020
-
2.3.2.2 additional information prediction of signal peptides in protein sequences of the N-terminus with a putative SpI and a SpII cleavage site, overview Corynebacterium glutamicum
-
-

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 Corynebacterium glutamicum
-
 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid Corynebacterium glutamicum LMG 3730
-
 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid Corynebacterium glutamicum ATCC 13032
-
 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid Corynebacterium glutamicum JCM 1318
-
 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid Corynebacterium glutamicum NCIMB 10025
-
 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid Corynebacterium glutamicum DSM 20300
-
 a peptide + a 5-L-glutamyl amino acid
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Corynebacterium glutamicum Q8NRT7
-
-
2.3.2.2 Corynebacterium glutamicum ATCC 13032 Q8NRT7
-
-
2.3.2.2 Corynebacterium glutamicum DSM 20300 Q8NRT7
-
-
2.3.2.2 Corynebacterium glutamicum JCM 1318 Q8NRT7
-
-
2.3.2.2 Corynebacterium glutamicum LMG 3730 Q8NRT7
-
-
2.3.2.2 Corynebacterium glutamicum NCIMB 10025 Q8NRT7
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.2.2 lipoprotein the enzyme is a lipoprotein and is attached to the outer side of the cytoplasmic membrane Corynebacterium glutamicum
2.3.2.2 proteolytic modification the enzyme is expressed as a single inactive pre-protein that undergoes posttranslational proteolytic self-cleavage Corynebacterium glutamicum

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.2 recombinat GgtB N-terminally tagged with chitin-binding domain and intein tag from Escherichia coli strain ER25669 by chitin affinity chromatography and ultrafiltration Corynebacterium glutamicum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.2.2 additional information
-
 quantitation of dipeptides and amino acids by HPLC in whole-cell assays Corynebacterium glutamicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid
-
 Corynebacterium glutamicum a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid
-
 Corynebacterium glutamicum LMG 3730 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid
-
 Corynebacterium glutamicum ATCC 13032 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid
-
 Corynebacterium glutamicum JCM 1318 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid
-
 Corynebacterium glutamicum NCIMB 10025 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid
-
 Corynebacterium glutamicum DSM 20300 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + glycylglycine
-
 Corynebacterium glutamicum 4-nitroaniline + 5-L-glutamyl-glycylglycine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + glycylglycine
-
 Corynebacterium glutamicum LMG 3730 4-nitroaniline + 5-L-glutamyl-glycylglycine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + glycylglycine
-
 Corynebacterium glutamicum ATCC 13032 4-nitroaniline + 5-L-glutamyl-glycylglycine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + glycylglycine
-
 Corynebacterium glutamicum JCM 1318 4-nitroaniline + 5-L-glutamyl-glycylglycine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + glycylglycine
-
 Corynebacterium glutamicum NCIMB 10025 4-nitroaniline + 5-L-glutamyl-glycylglycine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + glycylglycine
-
 Corynebacterium glutamicum DSM 20300 4-nitroaniline + 5-L-glutamyl-glycylglycine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-glutamate
-
 Corynebacterium glutamicum 4-nitroaniline + 5-L-glutamyl-L-glutamate
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-glutamate
-
 Corynebacterium glutamicum LMG 3730 4-nitroaniline + 5-L-glutamyl-L-glutamate
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-glutamate
-
 Corynebacterium glutamicum ATCC 13032 4-nitroaniline + 5-L-glutamyl-L-glutamate
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-glutamate
-
 Corynebacterium glutamicum JCM 1318 4-nitroaniline + 5-L-glutamyl-L-glutamate
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-glutamate
-
 Corynebacterium glutamicum NCIMB 10025 4-nitroaniline + 5-L-glutamyl-L-glutamate
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-glutamate
-
 Corynebacterium glutamicum DSM 20300 4-nitroaniline + 5-L-glutamyl-L-glutamate
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-glutamine
-
 Corynebacterium glutamicum 4-nitroaniline + 5-L-glutamyl-L-glutamine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-glutamine
-
 Corynebacterium glutamicum LMG 3730 4-nitroaniline + 5-L-glutamyl-L-glutamine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-glutamine
-
 Corynebacterium glutamicum ATCC 13032 4-nitroaniline + 5-L-glutamyl-L-glutamine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-glutamine
-
 Corynebacterium glutamicum JCM 1318 4-nitroaniline + 5-L-glutamyl-L-glutamine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-glutamine
-
 Corynebacterium glutamicum NCIMB 10025 4-nitroaniline + 5-L-glutamyl-L-glutamine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-glutamine
-
 Corynebacterium glutamicum DSM 20300 4-nitroaniline + 5-L-glutamyl-L-glutamine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-leucine
-
 Corynebacterium glutamicum 4-nitroaniline + 5-L-glutamyl-L-leucine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-methionine
-
 Corynebacterium glutamicum 4-nitroaniline + 5-L-glutamyl-L-methionine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + L-valine
-
 Corynebacterium glutamicum 4-nitroaniline + 5-L-glutamyl-L-valine
-
 ?
2.3.2.2 additional information L-gamma-glutamyl-4-nitroanilide is a chromogenic substrate. With the isolated recombinant enzyme, it is determined that besides GPNA also the dipeptides gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-Val, and gamma-Glu-Leu are hydrolyzed, cf. EC 3.4.19.13 Corynebacterium glutamicum ?
-
-
2.3.2.2 additional information L-gamma-glutamyl-4-nitroanilide is a chromogenic substrate. With the isolated recombinant enzyme, it is determined that besides GPNA also the dipeptides gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-Val, and gamma-Glu-Leu are hydrolyzed, cf. EC 3.4.19.13 Corynebacterium glutamicum LMG 3730 ?
-
-
2.3.2.2 additional information L-gamma-glutamyl-4-nitroanilide is a chromogenic substrate. With the isolated recombinant enzyme, it is determined that besides GPNA also the dipeptides gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-Val, and gamma-Glu-Leu are hydrolyzed, cf. EC 3.4.19.13 Corynebacterium glutamicum ATCC 13032 ?
-
-
2.3.2.2 additional information L-gamma-glutamyl-4-nitroanilide is a chromogenic substrate. With the isolated recombinant enzyme, it is determined that besides GPNA also the dipeptides gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-Val, and gamma-Glu-Leu are hydrolyzed, cf. EC 3.4.19.13 Corynebacterium glutamicum JCM 1318 ?
-
-
2.3.2.2 additional information L-gamma-glutamyl-4-nitroanilide is a chromogenic substrate. With the isolated recombinant enzyme, it is determined that besides GPNA also the dipeptides gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-Val, and gamma-Glu-Leu are hydrolyzed, cf. EC 3.4.19.13 Corynebacterium glutamicum NCIMB 10025 ?
-
-
2.3.2.2 additional information L-gamma-glutamyl-4-nitroanilide is a chromogenic substrate. With the isolated recombinant enzyme, it is determined that besides GPNA also the dipeptides gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-Val, and gamma-Glu-Leu are hydrolyzed, cf. EC 3.4.19.13 Corynebacterium glutamicum DSM 20300 ?
-
-

Subunits

EC Number Subunits Comment Organism
2.3.2.2 heterodimer bacterial gamma-glutamyl transpeptidase (GGT) is a heterodimeric enzyme, consisting of one large and one small subunit Corynebacterium glutamicum

Synonyms

EC Number Synonyms Comment Organism
2.3.2.2 Cgl0954
-
 Corynebacterium glutamicum
2.3.2.2 gamma-glutamyl transpeptidase
-
 Corynebacterium glutamicum
2.3.2.2 ggtB
-
 Corynebacterium glutamicum
2.3.2.2 More see also EC 3.4.19.13 Corynebacterium glutamicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.2 45
-
-
 Corynebacterium glutamicum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.3.2.2 22 60 the optimal temperature of GgtBCg is 45°C. The enzyme exhibits 85% and 60% of the maximal activity at 37°C and 22°C, respectively. Whereas GgtBCg retains 50% activity at 60°C, it is completely inactivated at 70°C, recombinant enzyme Corynebacterium glutamicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 9.6
-
-
 Corynebacterium glutamicum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.2.2 4 11 activity range, recombinant enzyme Corynebacterium glutamicum

General Information

EC Number General Information Comment Organism
2.3.2.2 evolution the enzyme belongs to the superfamily of N-terminal nucleophile (NTN-)aminohydrolases Corynebacterium glutamicum
2.3.2.2 malfunction gamma-glutamyl transpeptidase activity is abolished upon deletion of ggtB. But although deletion and overexpression of ggtB has significant effects on intracellular dipeptide concentrations, it is neither essential for biosynthesis nor catabolismof these dipeptides in vivo Corynebacterium glutamicum
2.3.2.2 physiological function gamma-glutamyl transpeptidase activity is associated with intact cells of Corynebacterium glutamicum. Enzyme GgtB catalyzes the concentration-dependent synthesis and hydrolysis of gamma-glutamyl dipeptides and shows strong glutaminase activity. The intracellular concentrations of five gamma-glutamyl dipeptides, i.e. gamma-Glu-Glu, gamma-Glu-Gln, gamma-Glu-Val, gamma-Glu-Leu, gamma-Glu-Met, are determined by HPLC-MS. Metabolic profiling reveals that ggtB is not essential for theformation of intracellular gamma-glutamyl dipeptides. GgtBCg might contribute to catabolism by hydrolyzing L-glutamine to glutamate and ammonia Corynebacterium glutamicum