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Literature summary for 6.3.5.5 extracted from

  • Johnson, J.L.; West, J.K.; Nelson, A.D.; Reinhart, G.D.
    Resolving the fluorescence response of Escherichia coli carbamoyl phosphate synthetase: mapping intra- and intersubunit conformational changes (2007), Biochemistry, 46, 387-397.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
W170T increased Km compared to the wild type enzyme Escherichia coli
W175T increased Km compared to the wild type enzyme Escherichia coli
W213T increased Km compared to the wild type enzyme Escherichia coli
W437T increased Km compared to the wild type enzyme Escherichia coli
W461T increased Km compared to the wild type enzyme Escherichia coli
W71T increased Km compared to the wild type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.44
-
ATP wild type enzyme, at 25°C in 50 mM HEPES buffer, pH 7.5 Escherichia coli
0.51
-
ATP mutant enzyme W437T, at 25°C in 50 mM HEPES buffer, pH 7.5 Escherichia coli
0.75
-
ATP mutant enzyme W213T, at 25°C in 50 mM HEPES buffer, pH 7.5 Escherichia coli
1.28
-
ATP mutant enzyme W71T, at 25°C in 50 mM HEPES buffer, pH 7.5 Escherichia coli
1.34
-
ATP mutant enzyme W461T, at 25°C in 50 mM HEPES buffer, pH 7.5 Escherichia coli
1.57
-
ATP mutant enzyme W170T, at 25°C in 50 mM HEPES buffer, pH 7.5 Escherichia coli
1.94
-
ATP mutant enzyme W175T, at 25°C in 50 mM HEPES buffer, pH 7.5 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Sephacryl S-300 gel filtration and Resource-Q column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ATP + L-Gln + HCO3-
-
Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
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Synonyms

Synonyms Comment Organism
Carbamoylphosphate synthetase II
-
Escherichia coli
CPS
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli