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Literature summary for 2.5.1.55 extracted from

  • Howe, D.L.; Sundaram, A.K.; Wu, J.; Gatti, D.L.; Woodard, R.W.
    Mechanistic insight into 3-deoxy-D-manno-octulosonate-8-phosphate synthase and 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase utilizing phosphorylated monosaccharide analogues (2003), Biochemistry, 42, 4843-4854.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.019
-
 D-arabinose 5-phosphate pH 7.6, 37°C Escherichia coli
0.05
-
 2-deoxyribose 5-phosphate pH 7.6, 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in presence of D-erythrose 4-phosphate or D-ribose 5-phosphate the enzyme catalyzes the rapid consumption of approximately 1 mol of phosphoenolpyruvate per active site, after which consumption of phosphoenolpyruvate slows to a negligible but measurable rate Escherichia coli ?
-
 ?
phosphoenolpyruvate + 2-deoxyribose 5-phosphate
-
 Escherichia coli ?
-
 ?
phosphoenolpyruvate + D-arabinose 5-phosphate
-
 Escherichia coli 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
 ?
phosphoenolpyruvate + erythrose 4-phosphate the enzyme does not catalyze the condensation of D-erythrose 4-phosphate and phosphoenolpyruvate to form 3-deoxy-D-ribo-heptulosonate 7-phosphate Escherichia coli 3-deoxy-D-ribo-heptulosonate 7-phosphate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.12
-
 2-deoxyribose 5-phosphate pH 7.6, 37°C Escherichia coli
6.8
-
 D-arabinose 5-phosphate pH 7.6, 37°C Escherichia coli