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Literature summary for 5.3.1.8 extracted from

  • Gao, H.; Chen, Y.; Leary, J.A.
    Kinetic measurements of phosphoglucose isomerase and phosphomannose isomerase by direct analysis of phosphorylated aldose-ketose isomers using tandem mass spectrometry (2005), Int. J. Mass Spectrom., 240, 291-299.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.15
-
D-fructose 6-phosphate 22°C, pH 7.4 Escherichia coli
1.21
-
D-mannose 6-phosphate 22°C, pH 7.4 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
mass spectrometry based method for the direct determination of kinetic konstants of enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 6-phosphate
-
Escherichia coli D-mannose 6-phosphate
-
r
D-Mannose 6-phosphate
-
Escherichia coli D-Fructose 6-phosphate
-
r