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Literature summary for 2.5.1.55 extracted from

  • Kohen, A.; Jakob, A.; Baasov, T.
    Mechanistic studies of 3-deoxy-D-manno-2-octulosonate-8-phosphate synthase from Escherichia coli (1992), Eur. J. Biochem., 208, 443-449.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.026
-
D-arabinose 5-phosphate pH 7.3, 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 3-deoxy-D-manno-octulosonate 8-phosphate + phosphate steady-state kinetic mechanism, where phosphoenolpyruvate binding precedes that of D-arabinose-5-phosphate, followed by the ordered release of phosphate and 3-deoxy-D-manno-2-octulosonate 8-phosphate Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + D-arabinose 5-phosphate
-
Escherichia coli 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
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