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Literature summary for 2.3.2.2 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
Search for more literature for 2.3.2.2

Activating Compound

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

Inhibitors

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

Metals/Ions

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

Organism

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

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
bulb
-
 Allium cepa
-
bulb dormant Allium sativum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
-
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

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

Synonyms

Synonyms Comment Organism
AsGGT1
-
 Allium sativum
gamma-glutamyltranspeptidase
-
 Allium sativum
gamma-glutamyltranspeptidase
-
 Allium cepa
GGT
-
 Allium sativum
GGT
-
 Allium cepa

Temperature Optimum [°C]

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

Temperature Range [°C]

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

pH Optimum

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

pH Range

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

General Information

General Information Comment Organism
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
physiological function gamma-glutamyltranspeptidases (GGTs) catalyze the transfer of gamma-glutamyl groups from gamma-glutamylpeptides to other peptides, amino acids, or water Allium cepa