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Literature summary for 6.3.1.2 extracted from

  • Pearson, J.T.; Dabrowski, M.J.; Kung, I.; Atkins, W.M.
    The central loop of Escherichia coli glutamine synthetase is flexible and functionally passive (2005), Arch. Biochem. Biophys., 436, 397-405.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
E165C mutant yields inter-subunit disulfide bonds connecting central loops. Inter-subunit disulfide bonds between the central loops causes no detectable changes in the KM-values for glutamate or ATP, nor the KD for either ATP or the transition state analog L-methionine sulfoximine. Covalent and quantitative adduction of the E165C mutant with iodo-acetamido-pyrene yields nearly fully active enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 ATP wild-type enzyme Escherichia coli
0.25
-
 ATP oxidized mutant enzyme E165C Escherichia coli
0.26
-
 ATP reduced mutant enzyme E165C Escherichia coli
3.3
-
 L-Glu wild-type enzyme Escherichia coli
6
-
 L-Glu oxidized mutant enzyme E165C Escherichia coli
7
-
 L-Glu reduced mutant enzyme E165C Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-Glu + NH4+ Escherichia coli
-
 ADP + phosphate + L-Gln
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Glu + NH4+
-
 Escherichia coli ADP + phosphate + L-Gln
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3 6 ATP wild-type enzyme Escherichia coli
25
-
 ATP oxidized mutant enzyme E165C Escherichia coli
27
-
 L-Glu oxidized mutant enzyme E165C Escherichia coli
35
-
 ATP reduced mutant enzyme E165C Escherichia coli
40
-
 L-Glu reduced mutant enzyme E165C Escherichia coli