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Literature summary for 6.3.2.2 extracted from

  • Hicks, L.M.; Cahoon, R.E.; Bonner, E.R.; Rivard, R.S.; Sheffield, J.; Jez, J.M.
    Thiol-based regulation of redox-active glutamate-cysteine ligase from Arabidopsis thaliana (2007), Plant Cell, 19, 2653-2661.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.2.2

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant enzymes are expressed in Escherichia coli Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
C186S mutation decreases activity by 20fold and abrogates the response to changes in redox environment Arabidopsis thaliana
C349S mutation reduces reaction rate by twofold Arabidopsis thaliana
C364S mutation reduces reaction rate by twofold Arabidopsis thaliana
C406S mutation decreases activity by 20fold and abrogates the response to changes in redox environment Arabidopsis thaliana
additional information mutation of Cys102, Cys251, Cys349, or Cys364 does not alter the response to redox environment Arabidopsis thaliana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4 5.4 L-Cys pH 7, mutant enzyme C364S Arabidopsis thaliana
7
-
 L-Glu pH 7, mutant enzyme C364S Arabidopsis thaliana
8.5
-
 L-Glu pH 7, mutant enzyme C102S Arabidopsis thaliana
9.1
-
 L-Glu pH 7, wild-type enzyme Arabidopsis thaliana
11.2
-
 L-Glu pH 7, mutant enzyme C349S Arabidopsis thaliana
13.9
-
 L-Glu pH 7, mutant enzyme C251S Arabidopsis thaliana
25.3
-
 ATP pH 7, mutant enzyme C364S Arabidopsis thaliana
31.6
-
 ATP pH 7, mutant enzyme C349S Arabidopsis thaliana
37.5
-
 ATP pH 7, mutant enzyme C251S Arabidopsis thaliana
39.2
-
 L-Cys pH 7, mutant enzyme C251S Arabidopsis thaliana
40.3
-
 ATP pH 7, mutant enzyme C102S Arabidopsis thaliana
42
-
 ATP pH 7, wild-type enzyme Arabidopsis thaliana
46.1
-
 L-Cys pH 7, mutant enzyme C349S Arabidopsis thaliana
46.9
-
 L-Cys pH 7, wild-type enzyme Arabidopsis thaliana
57.3
-
 L-Cys pH 7, mutant enzyme C102S Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamate + L-cysteine Arabidopsis thaliana the thiol-based regulation of glutamate-cysteine ligase provides a posttranslational mechanism for modulating enzyme activity in response to in vivo redox environment ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
root
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate + L-cysteine the thiol-based regulation of glutamate-cysteine ligase provides a posttranslational mechanism for modulating enzyme activity in response to in vivo redox environment Arabidopsis thaliana ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.6
-
 L-Cys pH 7, mutant enzyme C349S Arabidopsis thaliana
4
-
 L-Cys pH 7, mutant enzyme C251S Arabidopsis thaliana
4.1
-
 L-Glu pH 7, mutant enzyme C364S Arabidopsis thaliana
4.1
-
 L-Cys pH 7, mutant enzyme C364S Arabidopsis thaliana
4.4
-
 ATP pH 7, mutant enzyme C364S Arabidopsis thaliana
4.5
-
 L-Cys pH 7, wild-type enzyme Arabidopsis thaliana
4.6
-
 L-Glu pH 7, mutant enzyme C102S Arabidopsis thaliana
4.7
-
 L-Glu pH 7, mutant enzyme C349S Arabidopsis thaliana
5.5
-
 L-Cys pH 7, mutant enzyme C102S Arabidopsis thaliana
5.5
-
 ATP pH 7, mutant enzyme C349S Arabidopsis thaliana
5.8
-
 ATP pH 7, mutant enzyme C102S Arabidopsis thaliana
6.1
-
 L-Glu pH 7, wild-type enzyme Arabidopsis thaliana
6.3
-
 ATP pH 7, mutant enzyme C251S Arabidopsis thaliana
6.8
-
 ATP pH 7, wild-type enzyme Arabidopsis thaliana
7.1
-
 L-Glu pH 7, mutant enzyme C251S Arabidopsis thaliana