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Literature summary 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

Crystallization (Commentary)

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.5.4 additional information
-
 additional information kinetic mechanism, kinetic model Escherichia coli
6.3.5.4 0.26
-
 ATP
-
 Escherichia coli
6.3.5.4 0.69
-
 L-glutamine glutamine-dependent synthetase activity Escherichia coli
6.3.5.4 0.85
-
 L-aspartate
-
 Escherichia coli
6.3.5.4 1.67
-
 L-glutamine glutaminase activity Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.4 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.5.4
-
 Escherichia coli

Reaction

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.4 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
6.3.5.4 ATP + L-aspartate + L-glutamine glutamine is the in vivo nitrogen source Escherichia coli AMP + diphosphate + L-asparagine + L-glutamate
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.5.4 37
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.5.4 1.56
-
 L-aspartate
-
 Escherichia coli
6.3.5.4 2.18
-
 ATP
-
 Escherichia coli
6.3.5.4 2.73
-
 L-glutamine glutamine-dependent synthetase activity Escherichia coli
6.3.5.4 2.94
-
 ATP
-
 Escherichia coli
6.3.5.4 2.94
-
 L-aspartate
-
 Escherichia coli
6.3.5.4 3 6 L-glutamine glutaminase activity Escherichia coli
6.3.5.4 3 6 L-glutamine glutamine-dependent synthetase activity Escherichia coli
6.3.5.4 3.38
-
 L-glutamine glutaminase activity Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.5.4 8
-
 assay at Escherichia coli