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6.3.2.3: glutathione synthase

This is an abbreviated version!
For detailed information about glutathione synthase, go to the full flat file.

Word Map on EC 6.3.2.3

Reaction

ATP
+
gamma-L-glutamyl-L-cysteine
+
glycine
=
ADP
+
phosphate
+
glutathione

Synonyms

Asuc_1947, bifunctional glutathione synthetase, bifunctional GSH synthetase, bifunctional L-glutathione synthetase, gamma -glutamate-cysteine ligase-glutathione synthetase, gamma-GCS, gamma-GCS-GS, gamma-glutamate-cysteine ligase/glutathione synthetase, gamma-glutamylcysteine synthetase-glutathione synthetase, GCL, GCSGS, ghF, glutamate cysteine ligase, glutathione biosynthesis bifunctional protein GshAB, Glutathione synthase, Glutathione synthetase, Glutathione synthetase (tripeptide), GS, GSH synthase, GSH synthetase, GSH-S, GSH2, gshAB, GSHase, gshB, GshF, GshFAp, GshFAs, GSHII, GSHS, GSHS1, GSS, hGS, L-glutathione synthetase, More, Phytochelatin synthetase, StGCL-GS, Synthetase, glutathione, TAGS1, TaGS2, TbGS, ZmGS

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.2 Acid—amino-acid ligases (peptide synthases)
                6.3.2.3 glutathione synthase

General Stability

General Stability on EC 6.3.2.3 - glutathione synthase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol is required for stabilization of the enzyme during freezing
-
loss of activity by exposure to Mn2+ for long periods
-
proteolysis by arginyl endopeptidase or trypsin causes a time-dependent decrease in activity. Only one peptide bond between Arg233 and Gly234 in the loop is cleaved
-
relatively stable at all stages of purification
-
several successive freezings and thawings of the cell-free extract have no effect on enzyme activity
-
the remaining activity after arginyl-endopeptidase treatment is higher in the presence of ATP and/or gamma-Glu-Cys than in their absence
-