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Literature summary extracted from

  • Samuels, N.M.; Gibson, B.W.; Miller, S.M.
    Investigation of the kinetic mechanism of cytidine 5'-monophosphate N-acetylneuraminic acid synthetase from Haemophilus ducreyi with new insights on rate-limiting steps from product inhibition analysis (1999), Biochemistry, 38, 6195-6203.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.43 CMP-N-acylneuraminate
-
 [Haemophilus] ducreyi
2.7.7.43 diphosphate
-
 [Haemophilus] ducreyi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.43 0.0106
-
 CTP pH 7.1, 25°C [Haemophilus] ducreyi
2.7.7.43 0.076
-
 N-acetylneuraminate pH 7.1, 25°C [Haemophilus] ducreyi

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.43 [Haemophilus] ducreyi
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.7.43 CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate ordered bi-bi kinetic mechanism. CTP binds first and CMP-NeuAc dissociates last. The rate-limiting step appears to be dissociation of CMP-NeuAc [Haemophilus] ducreyi
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.43 CTP + N-acylneuraminate
-
 [Haemophilus] ducreyi diphosphate + CMP-N-acylneuraminate
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.7.43 1.8
-
 CTP pH 7.1, 25°C [Haemophilus] ducreyi