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Literature summary for 6.3.2.2 extracted from

  • Gromes, R.; Hothorn, M.; Lenherr, E.D.; Rybin, V.; Scheffzek, K.; Rausch, T.
    The redox switch of gamma-glutamylcysteine ligase via a reversible monomer-dimer transition is a mechanism unique to plants (2008), Plant J., 54, 1063-1075.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information GCL forms a homodimer under oxidizing conditions, and is activated more than threefold Nicotiana tabacum

Protein Variants

Protein Variants Comment Organism
C356A the mutant shows reduced inhibition by DTT, but increased inhibition by glutathione Brassica juncea

Inhibitors

Inhibitors Comment Organism Structure
buthionine sulfoximine specific inhibitor of GCL Agrobacterium tumefaciens
buthionine sulfoximine specific inhibitor of GCL Nicotiana tabacum
buthionine sulfoximine specific inhibitor of GCL Xanthomonas campestris
DTT
-
Brassica juncea
DTT
-
Nicotiana tabacum
glutathione feedback inhibition Agrobacterium tumefaciens
glutathione feedback inhibition Brassica juncea
glutathione feedback inhibition Nicotiana tabacum
glutathione feedback inhibition Xanthomonas campestris
additional information no inhibition by DTT Agrobacterium tumefaciens
additional information no inhibition by buthionine sulfoximine Brassica juncea
additional information no inhibition by DTT Xanthomonas campestris
Na+ 72.7% inhibition at 300 mM Agrobacterium tumefaciens
Na+ 69.2% inhibition at 300 mM Brassica juncea
Na+ 79.6% inhibition at 300 mM Xanthomonas campestris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
L-cysteine
-
Xanthomonas campestris
0.12
-
L-cysteine
-
Brassica juncea
0.14
-
L-cysteine
-
Agrobacterium tumefaciens
0.59
-
ATP
-
Agrobacterium tumefaciens
1.3
-
ATP
-
Brassica juncea
1.9
-
L-glutamate
-
Agrobacterium tumefaciens
2.3
-
L-glutamate
-
Xanthomonas campestris
3.1
-
ATP
-
Xanthomonas campestris
8.5
-
L-glutamate
-
Brassica juncea

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Xanthomonas campestris
Mg2+
-
Agrobacterium tumefaciens
Mg2+
-
Brassica juncea
Mg2+
-
Nicotiana tabacum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamate + L-cysteine Brassica juncea redox regulation of the enzyme, a redox switch based on CC2-mediated homodimerization is unique to plant GCL enzymes, overview ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
?
ATP + L-glutamate + L-cysteine Nicotiana tabacum redox regulation of the enzyme, a redox switch based on CC2-mediated homodimerization is unique to plant GCL enzymes, overview ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
?
ATP + L-glutamate + L-cysteine Xanthomonas campestris redox regulation of the enzyme, overview ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
?
ATP + L-glutamate + L-cysteine Agrobacterium tumefaciens redox regulation of the enzyme, overview ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
?

Organism

Organism UniProt Comment Textmining
Agrobacterium tumefaciens
-
-
-
Brassica juncea O23736
-
-
Nicotiana tabacum Q1W2L8
-
-
Xanthomonas campestris
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.405
-
-
Xanthomonas campestris
2.585
-
-
Agrobacterium tumefaciens
3.336
-
-
Brassica juncea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate + L-cysteine
-
Xanthomonas campestris ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
?
ATP + L-glutamate + L-cysteine
-
Agrobacterium tumefaciens ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
?
ATP + L-glutamate + L-cysteine
-
Brassica juncea ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
?
ATP + L-glutamate + L-cysteine
-
Nicotiana tabacum ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
?
ATP + L-glutamate + L-cysteine redox regulation of the enzyme, a redox switch based on CC2-mediated homodimerization is unique to plant GCL enzymes, overview Brassica juncea ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
?
ATP + L-glutamate + L-cysteine redox regulation of the enzyme, a redox switch based on CC2-mediated homodimerization is unique to plant GCL enzymes, overview Nicotiana tabacum ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
?
ATP + L-glutamate + L-cysteine redox regulation of the enzyme, overview Xanthomonas campestris ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
?
ATP + L-glutamate + L-cysteine redox regulation of the enzyme, overview Agrobacterium tumefaciens ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
?
additional information the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, CC2 plays a role in GCL redox regulation, overview Nicotiana tabacum ?
-
?
additional information the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, CC2 plays no role in GCL redox regulation, overview Xanthomonas campestris ?
-
?
additional information the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, CC2 plays no role in GCL redox regulation, overview Agrobacterium tumefaciens ?
-
?
additional information the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, which both strongly impact on GCL activity in vitro, cysteines of CC2 involved in the monomer-dimer transition in GCL. CC2 plays a role in GCL redox regulation, overview Brassica juncea ?
-
?

Subunits

Subunits Comment Organism
dimer the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, amino acids contributing to the homodimer interface in GCL are highly conserved among plant GCLs, but not in related proteobacterial GCLs. NtGCL forms a homodimer under oxidizing conditions Nicotiana tabacum
monomer proteobacterial GCLs remain monomeric under oxidizing and reducing conditions, overview Xanthomonas campestris
monomer proteobacterial GCLs remain monomeric under oxidizing and reducing conditions, overview Agrobacterium tumefaciens
More the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, which both strongly impact on GCL activity in vitro, cysteines of CC2 involved in the monomer-dimer transition in GCL. Amino acids contributing to the homodimer interface in BjGCL are highly conserved among plant GCLs, but not in related proteobacterial GCLs Brassica juncea

Synonyms

Synonyms Comment Organism
gamma-glutamylcysteine ligase
-
Xanthomonas campestris
gamma-glutamylcysteine ligase
-
Agrobacterium tumefaciens
gamma-glutamylcysteine ligase
-
Brassica juncea
gamma-glutamylcysteine ligase
-
Nicotiana tabacum
GCL
-
Xanthomonas campestris
GCL
-
Agrobacterium tumefaciens
GCL
-
Brassica juncea
GCL
-
Nicotiana tabacum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7350
-
L-glutamate
-
Xanthomonas campestris
7350
-
L-cysteine
-
Xanthomonas campestris
7920
-
L-glutamate
-
Agrobacterium tumefaciens
7920
-
L-cysteine
-
Agrobacterium tumefaciens
10190
-
L-glutamate
-
Brassica juncea
10190
-
L-cysteine
-
Brassica juncea

Cofactor

Cofactor Comment Organism Structure
ATP
-
Xanthomonas campestris
ATP
-
Agrobacterium tumefaciens
ATP
-
Brassica juncea
ATP
-
Nicotiana tabacum

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.2
-
wild-type enzyme Brassica juncea DTT
3.8
-
mutant C356A enzyme Brassica juncea glutathione
4.1
-
-
Nicotiana tabacum glutathione
5.1
-
-
Nicotiana tabacum DTT
5.5
-
wild-type enzyme Brassica juncea glutathione
5.5
-
mutant C356A enzyme Brassica juncea DTT
6.4
-
-
Xanthomonas campestris glutathione
7.9
-
-
Xanthomonas campestris buthionine sulfoximine
8.1
-
-
Agrobacterium tumefaciens glutathione
10.8
-
-
Agrobacterium tumefaciens buthionine sulfoximine
11.5
-
-
Nicotiana tabacum buthionine sulfoximine