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Literature summary extracted from

  • Goore, M.Y.; Thompson, J.F.
    gamma-Glutamyl transpeptidase from kidney bean fruit. I. Purification and mechanism of action (1967), Biochim. Biophys. Acta, 132, 15-26.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.2.2 carboxylic acids
-
 Phaseolus vulgaris

General Stability

EC Number General Stability Organism
2.3.2.2 freezing or lyophilization inactivates purified enzyme Phaseolus vulgaris

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.2 additional information inhibition by diverse amino acids, overview Phaseolus vulgaris

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.2 additional information
-
 additional information
-
 Phaseolus vulgaris

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.2.2 180000
-
 gel filtration Phaseolus vulgaris

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Phaseolus vulgaris
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.2
-
 Phaseolus vulgaris

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid mechanism Phaseolus vulgaris
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.2 fruit
-
 Phaseolus vulgaris
-

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 3.1
-
 purified enzyme Phaseolus vulgaris

Storage Stability

EC Number Storage Stability Organism
2.3.2.2 0°C, at least 3 weeks Phaseolus vulgaris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 (5-L-glutamyl)-peptide + acceptor + H+ concurrent reaction: hydrolase reaction with H2O as acceptor Phaseolus vulgaris peptide + 5-L-glutamyl amino acid
-
 ?
2.3.2.2 (5-L-glutamyl)-peptide + acceptor + H+ concurrent reaction: autotranspeptidation with another donor molecule as acceptor Phaseolus vulgaris peptide + 5-L-glutamyl amino acid
-
 ?
2.3.2.2 (5-L-glutamyl)-peptide + acceptor + H+ donor specificity, overview Phaseolus vulgaris peptide + 5-L-glutamyl amino acid
-
 ?
2.3.2.2 5-L-glutamylaniline + 5-L-glutamylaniline
-
 Phaseolus vulgaris aniline + 5-L-glutamyl-5-L-glutamylaniline
-
 ir
2.3.2.2 5-L-glutamylaniline + H2O
-
 Phaseolus vulgaris aniline + L-glutamic acid
-
 ir
2.3.2.2 5-L-glutamylaniline + S-methyl-L-cysteine
-
 Phaseolus vulgaris aniline + 5-L-glutamyl-S-methyl-L-cysteine
-
 ir

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.2 37
-
 assay at Phaseolus vulgaris

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 additional information
-
 pH-dependence of reaction kinetics Phaseolus vulgaris
2.3.2.2 9.5
-
-
 Phaseolus vulgaris