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Literature summary for 6.3.2.3 extracted from

  • Kato, H.; Tanaka, T.; Yamaguchi, H.; Hara, T.; Nishioka, T.; Katsube, Y.; Oda, J.
    Flexible loop that is novel catalytic machinery in a ligase. Atomic structure and function of the loopless glutathione synthetase (1994), Biochemistry, 33, 4995-4999.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure of the loopless mutant, in which the loop is replaced by 3 Gly residues, is identical with that of the wild-type enzyme Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information the crystal structure of the loopless mutant, in which the loop is replaced by 3 Gly residues, is identical with that of the wild-type enzyme. Replacement of the loop increases the Km-values, especially for glycine, and a 930fold decrease in turnover number. The loopless mutant shows gamma-Glu-L-Cys-dependent ATP hydrolase activity to almost the same extent as its glutathione synthetase activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information loopless mutant with increased Km-values, especially for Gly Escherichia coli
0.24
-
ATP gamma-Glu-Cys, wild-type enzyme Escherichia coli
0.7
-
gamma-Glu-Cys loopless mutant Escherichia coli
0.91
-
Gly wild-type enzyme Escherichia coli
1.54
-
ATP loopless mutant Escherichia coli
29.8
-
Gly loopless mutant Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
B
-
Escherichia coli
-
wild-type and loopless mutant, in which the loop (Ile226-Arg241) is replaced with 3 Gly residues
-
Escherichia coli B / ATCC 11303
-
B
-

Reaction

Reaction Comment Organism Reaction ID
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione the catalytic mechanism is proposed to proceed via phosphorylation of the dipeptide substrate to yield an acyl phosphate intermediate. This intermediate is subsequently attacked by glycine, followed by loss of inorganic phosphate, leading to glutathione formation Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + gamma-Glu-L-Cys + Gly
-
Escherichia coli ADP + phosphate + glutathione
-
?
ATP + gamma-Glu-L-Cys + Gly
-
Escherichia coli B / ATCC 11303 ADP + phosphate + glutathione
-
?
additional information the loopless mutant shows gamma-Glu-L-Cys-dependent ATP hydrolase activity to almost the same extent as its glutathione synthetase activity Escherichia coli ?
-
?
additional information the loopless mutant shows gamma-Glu-L-Cys-dependent ATP hydrolase activity to almost the same extent as its glutathione synthetase activity Escherichia coli B / ATCC 11303 ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information loopless mutant with a 930fold decrease in turnover number Escherichia coli