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Literature summary extracted from

  • Sun, Y.; Hu, J.; Wang, W.; Zhang, B.; Shen, Y.
    Characterization of gamma-glutamyltranspeptidases from dormant garlic and onion bulbs (2019), Food Sci. Nutr., 7, 499-505 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.2.2 D-glucose
-
 Allium sativum
2.3.2.2 L-aspartic acid
-
 Allium sativum
2.3.2.2 L-cysteine
-
 Allium sativum
2.3.2.2 L-lysine
-
 Allium cepa
2.3.2.2 L-proline
-
 Allium cepa

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.2 Cu2+ at 2 mM Allium cepa
2.3.2.2 D-glucose
-
 Allium cepa
2.3.2.2 L-aspartic acid
-
 Allium cepa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.2.2 Cu2+ activates at 2 mM Allium sativum
2.3.2.2 Fe2+ activates at 2 mM Allium sativum
2.3.2.2 Mg2+ activates at 2 mM Allium sativum
2.3.2.2 Mn2+ activates at 2 mM Allium sativum
2.3.2.2 additional information no significant effect by Ca2+ and Zn2+ at 2 mM Allium sativum
2.3.2.2 additional information no significant effect by Mn2+, Zn2+, Ca2+, and Mg2+ at 2 mM Allium cepa

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Allium cepa Q6R2X1 var. agrogatum
-
2.3.2.2 Allium sativum A0A0B6VSN3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.2 native enzyme from bulbs by ammonium sulfate fractionation, hydrophobic interaction chromatography, and gel filtration Allium sativum
2.3.2.2 native enzyme from bulbs by ammonium sulfate fractionation, hydrophobic interaction chromatography, and gel filtration Allium cepa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.2 bulb
-
 Allium cepa
-
2.3.2.2 bulb dormant Allium sativum
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 additional information the transpeptidase activity of BlGGT towards the acceptor substrate is evaluated using the chromophoric substrate, L-gamma-Glu-4-NA, as a gamma-glutamyl donor, quantitative measurement of release of 4-nitroaniline Allium sativum ?
-
-
2.3.2.2 additional information the transpeptidase activity of BlGGT towards the acceptor substrate is evaluated using the chromophoric substrate, L-gamma-Glu-4-NA, as a gamma-glutamyl donor, quantitative measurement of release of 4-nitroaniline Allium cepa ?
-
-

Subunits

EC Number Subunits Comment Organism
2.3.2.2 ? x * 53000, SDS-PAGE Allium sativum
2.3.2.2 ? x * 55000 + x * 22000, SDS-PAGE Allium cepa

Synonyms

EC Number Synonyms Comment Organism
2.3.2.2 AsGGT1
-
 Allium sativum
2.3.2.2 gamma-glutamyltranspeptidase
-
 Allium sativum
2.3.2.2 gamma-glutamyltranspeptidase
-
 Allium cepa
2.3.2.2 GGT
-
 Allium sativum
2.3.2.2 GGT
-
 Allium cepa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.2 50
-
-
 Allium cepa
2.3.2.2 70
-
-
 Allium sativum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.3.2.2 30 80 over 50% of maximal activity within this range, profile overview Allium sativum
2.3.2.2 30 75 active at, inactive above, profile overview Allium cepa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 5
-
-
 Allium sativum
2.3.2.2 7
-
-
 Allium cepa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.2.2 3 11 active at, inactive below, profile overview Allium cepa
2.3.2.2 4 11 active at, inactive above, profile overview Allium sativum

General Information

EC Number General Information Comment Organism
2.3.2.2 physiological function gamma-glutamyltranspeptidase is an organosulfur compound (GGT) and catalyzes the transfer of gamma-glutamyl groups from gamma-glutamylpeptides to other peptides, amino acids, or water Allium sativum
2.3.2.2 physiological function gamma-glutamyltranspeptidases (GGTs) catalyze the transfer of gamma-glutamyl groups from gamma-glutamylpeptides to other peptides, amino acids, or water Allium cepa