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Literature summary 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

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.2.2 0.07
-
 L-cysteine
-
 Xanthomonas campestris
6.3.2.2 0.12
-
 L-cysteine
-
 Brassica juncea
6.3.2.2 0.14
-
 L-cysteine
-
 Agrobacterium tumefaciens
6.3.2.2 0.59
-
 ATP
-
 Agrobacterium tumefaciens
6.3.2.2 1.3
-
 ATP
-
 Brassica juncea
6.3.2.2 1.9
-
 L-glutamate
-
 Agrobacterium tumefaciens
6.3.2.2 2.3
-
 L-glutamate
-
 Xanthomonas campestris
6.3.2.2 3.1
-
 ATP
-
 Xanthomonas campestris
6.3.2.2 8.5
-
 L-glutamate
-
 Brassica juncea

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.2 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
-
 ?
6.3.2.2 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
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine Xanthomonas campestris redox regulation of the enzyme, overview ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine Agrobacterium tumefaciens redox regulation of the enzyme, overview ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?

Organism

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.2.2 2.405
-
-
 Xanthomonas campestris
6.3.2.2 2.585
-
-
 Agrobacterium tumefaciens
6.3.2.2 3.336
-
-
 Brassica juncea

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.2 ATP + L-glutamate + L-cysteine
-
 Xanthomonas campestris ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine
-
 Agrobacterium tumefaciens ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine
-
 Brassica juncea ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine
-
 Nicotiana tabacum ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 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
-
 ?
6.3.2.2 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
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine redox regulation of the enzyme, overview Xanthomonas campestris ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine redox regulation of the enzyme, overview Agrobacterium tumefaciens ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 additional information the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, CC2 plays a role in GCL redox regulation, overview Nicotiana tabacum ?
-
 ?
6.3.2.2 additional information the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, CC2 plays no role in GCL redox regulation, overview Xanthomonas campestris ?
-
 ?
6.3.2.2 additional information the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, CC2 plays no role in GCL redox regulation, overview Agrobacterium tumefaciens ?
-
 ?
6.3.2.2 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

EC Number Subunits Comment Organism
6.3.2.2 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
6.3.2.2 monomer proteobacterial GCLs remain monomeric under oxidizing and reducing conditions, overview Xanthomonas campestris
6.3.2.2 monomer proteobacterial GCLs remain monomeric under oxidizing and reducing conditions, overview Agrobacterium tumefaciens
6.3.2.2 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

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.2.2 7350
-
 L-glutamate
-
 Xanthomonas campestris
6.3.2.2 7350
-
 L-cysteine
-
 Xanthomonas campestris
6.3.2.2 7920
-
 L-glutamate
-
 Agrobacterium tumefaciens
6.3.2.2 7920
-
 L-cysteine
-
 Agrobacterium tumefaciens
6.3.2.2 10190
-
 L-glutamate
-
 Brassica juncea
6.3.2.2 10190
-
 L-cysteine
-
 Brassica juncea

Cofactor

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

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
6.3.2.2 1.2
-
 wild-type enzyme Brassica juncea DTT
6.3.2.2 3.8
-
 mutant C356A enzyme Brassica juncea glutathione
6.3.2.2 4.1
-
-
 Nicotiana tabacum glutathione
6.3.2.2 5.1
-
-
 Nicotiana tabacum DTT
6.3.2.2 5.5
-
 wild-type enzyme Brassica juncea glutathione
6.3.2.2 5.5
-
 mutant C356A enzyme Brassica juncea DTT
6.3.2.2 6.4
-
-
 Xanthomonas campestris glutathione
6.3.2.2 7.9
-
-
 Xanthomonas campestris buthionine sulfoximine
6.3.2.2 8.1
-
-
 Agrobacterium tumefaciens glutathione
6.3.2.2 10.8
-
-
 Agrobacterium tumefaciens buthionine sulfoximine
6.3.2.2 11.5
-
-
 Nicotiana tabacum buthionine sulfoximine