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Literature summary for 6.3.5.4 extracted from

  • Tesson, A.R.; Soper, T.S.; Ciustea, M.; Richards, N.G.J.
    Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli (2003), Arch. Biochem. Biophys., 413, 23-31.
    View publication on PubMed
Search for more literature for 6.3.5.4

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray crystal structure of AS-B complexed with glutamine and AMP Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic mechanism, kinetic model Escherichia coli
0.26
-
 ATP
-
 Escherichia coli
0.69
-
 L-glutamine glutamine-dependent synthetase activity Escherichia coli
0.85
-
 L-aspartate
-
 Escherichia coli
1.67
-
 L-glutamine glutaminase activity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-aspartate + L-glutamine Escherichia coli glutamine is the in vivo nitrogen source AMP + diphosphate + L-asparagine + L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate + L-glutamine ATP-dependent, mechanism including an enzyme-ATP-Asp-Gln quarternary complex, AS-B structure, two active sites Escherichia coli AMP + diphosphate + L-asparagine + L-glutamate
-
 ir
ATP + L-aspartate + L-glutamine glutamine is the in vivo nitrogen source Escherichia coli AMP + diphosphate + L-asparagine + L-glutamate
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.56
-
 L-aspartate
-
 Escherichia coli
2.18
-
 ATP
-
 Escherichia coli
2.73
-
 L-glutamine glutamine-dependent synthetase activity Escherichia coli
2.94
-
 ATP
-
 Escherichia coli
2.94
-
 L-aspartate
-
 Escherichia coli
3 6 L-glutamine glutaminase activity Escherichia coli
3 6 L-glutamine glutamine-dependent synthetase activity Escherichia coli
3.38
-
 L-glutamine glutaminase activity Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli