EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
6.3.2.2 | L-buthionine-S-sulfoximine | mechanism-based inhibitor, in contrary to the mammalian enzyme form, the Escherichia coli enzyme is inhibited more weakly and slowly in presence of Mg2+, replacement of the metal by Mn2+ leads to increased binding affinity and inactivation rate | Escherichia coli | |
6.3.2.2 | additional information | no inhibition by L-buthionine-R-sulfoximine | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.2.2 | additional information | - |
additional information | Km values for diverse substrates in presence of Mg2+, or Mn2+, or both, kinetics | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.3.2.2 | Cu2+ | 2 divalent metal ions per enzyme molecule are bound, can be replaced by Mn2+ and Mg2+, binding mechanism and kinetics, overview | Escherichia coli | |
6.3.2.2 | Mg2+ | 2 divalent metal ions per enzyme molecule are bound, Mg2+ sharpens the substrate specificity, increases the resistance to L-buthionine-S,R-sulfoximine, can be replaced by Mn2+ and Cu2+, binding mechanism and kinetics, overview | Escherichia coli | |
6.3.2.2 | Mn2+ | 2 divalent metal ions per enzyme molecule are bound, Mg2+ broadens the substrate specificity, decreases the resistance to L-buthionine-S,R-sulfoximine, can be replaced by Mg2+ and Cu2+, binding mechanism and kinetics, overview | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.2.2 | ATP + L-Glu + L-Cys | Escherichia coli | first and rate-limiting step in the GSH biosynthesis | ADP + phosphate + gamma-L-Glu-L-Cys | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-Cys | Escherichia coli JM109 | first and rate-limiting step in the GSH biosynthesis | ADP + phosphate + gamma-L-Glu-L-Cys | - |
ir |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.2.2 | Escherichia coli | P0A6W9 | - |
- |
6.3.2.2 | Escherichia coli JM109 | P0A6W9 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.3.2.2 | from strain JM109, to homogeneity | Escherichia coli |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
6.3.2.2 | ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine | reaction mechanism | Escherichia coli |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
6.3.2.2 | 51 | - |
purified enzyme | Escherichia coli |
EC Number | Storage Stability | Organism |
---|---|---|
6.3.2.2 | -20°C, purified enzyme, 25% glycerol, stable for several months | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.2.2 | ATP + alpha-ethyl-L-glutamate + L-alpha-aminobutyrate | - |
Escherichia coli | ADP + phosphate + alpha-ethyl-L-glutamyl-L-alpha-aminobutyrate | - |
ir | |
6.3.2.2 | ATP + alpha-methyl-L-glutamate + L-alpha-aminobutyrate | - |
Escherichia coli | ADP + phosphate + alpha-methyl-L-glutamyl-L-alpha-aminobutyrate | - |
ir | |
6.3.2.2 | ATP + D-Glu + L-alpha-aminobutyrate | - |
Escherichia coli | ADP + phosphate + gamma-D-Glu-L-alpha-aminobutyrate | - |
ir | |
6.3.2.2 | ATP + L-Glu + allo-L-threonine | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-allo-L-threonine | - |
ir | |
6.3.2.2 | ATP + L-Glu + beta-amino-iso-butyrate | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-beta-amino-iso-butyrate | - |
ir | |
6.3.2.2 | ATP + L-Glu + beta-chloro-L-alanine | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-beta-chloro-L-alanine | - |
ir | |
6.3.2.2 | ATP + L-Glu + beta-cyano-L-alanine | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-beta-cyano-L-alanine | - |
ir | |
6.3.2.2 | ATP + L-Glu + Gly | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-Gly | - |
ir | |
6.3.2.2 | ATP + L-Glu + Gly | - |
Escherichia coli JM109 | ADP + phosphate + gamma-L-Glu-Gly | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-alanine | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-L-alanine | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-alpha-aminobutyrate | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-L-alpha-aminobutyrate | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-C-allylglycine | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-L-C-allylglycine | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-Cys | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-L-Cys | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-Cys | first and rate-limiting step in the GSH biosynthesis | Escherichia coli | ADP + phosphate + gamma-L-Glu-L-Cys | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-Cys | - |
Escherichia coli JM109 | ADP + phosphate + gamma-L-Glu-L-Cys | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-Cys | first and rate-limiting step in the GSH biosynthesis | Escherichia coli JM109 | ADP + phosphate + gamma-L-Glu-L-Cys | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-isoleucine | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-L-isoleucine | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-leucine | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-L-leucine | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-norleucine | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-L-norleucine | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-norvaline | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-L-norvaline | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-norvaline | - |
Escherichia coli JM109 | ADP + phosphate + gamma-L-Glu-L-norvaline | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-serine | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-L-serine | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-threonine | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-L-threonine | - |
ir | |
6.3.2.2 | ATP + L-Glu + L-valine | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-L-valine | - |
ir | |
6.3.2.2 | ATP + L-Glu + O-methyl-DL-serine | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-O-methyl-DL-serine | - |
ir | |
6.3.2.2 | ATP + L-Glu + S-methyl-L-Cys | - |
Escherichia coli | ADP + phosphate + gamma-L-Glu-L-S-methyl-Cys | - |
ir | |
6.3.2.2 | ATP + N-methyl-L-glutamate + L-alpha-aminobutyrate | - |
Escherichia coli | ADP + phosphate + N-methyl-L-glutamyl-L-alpha-aminobutyrate | - |
ir | |
6.3.2.2 | additional information | substrate specificity, poor substrates are beta-glutamate, (R,S)-beta-methyl-DL-glutamate, (R,S)-gamma-methyl-glutamate, L-aspartate, and DL-alpha-aminoadipate | Escherichia coli | ? | - |
? | |
6.3.2.2 | additional information | substrate specificity, poor substrates are beta-glutamate, (R,S)-beta-methyl-DL-glutamate, (R,S)-gamma-methyl-glutamate, L-aspartate, and DL-alpha-aminoadipate | Escherichia coli JM109 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.3.2.2 | gamma-GCS | - |
Escherichia coli |
6.3.2.2 | gamma-Glutamylcysteine synthetase | - |
Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.3.2.2 | 37 | - |
assay at | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
6.3.2.2 | 8.2 | - |
assay at | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.3.2.2 | ATP | - |
Escherichia coli |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.2.2 | additional information | - |
additional information | inhibition kinetics | Escherichia coli |