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Literature summary for 2.7.7.43 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
Search for more literature for 2.7.7.43

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
[Haemophilus] ducreyi
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

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

Turnover Number [1/s]

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