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Literature summary for 2.5.1.54 extracted from

  • Furdui, C.M.; Sau, A.K.; Yaniv, O.; Belakhov, V.; Woodard, R.W.; Baasov, T.; Anderson, K.S.
    The use of (E)- and (Z)-phosphoenol-3-fluoropyruvate as mechanistic probes reveals significant differences between the active sites of KDO8P and DAHP synthases (2005), Biochemistry, 44, 7326-7335.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.009
-
phosphoenolpyruvate pH 7.5 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenol-3-fluoropyruvate + D-erythrose 4-phosphate + H2O enzyme does not discriminate between (E) and (Z)-form of phosphoenol-3-fluoropyruvate Escherichia coli 3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
-
Escherichia coli 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
32
-
phosphoenolpyruvate pH 7.5 Escherichia coli