Literature summary for 2.5.1.56 extracted from

Gunawan, J.; Simard, D.; Gilbert, M.; Lovering, A.L.; Wakarchuk, W.W.; Tanner, M.E.; Strynadka, N.C.
Structural and mechanistic analysis of sialic acid synthase NeuB from Neisseria meningitidis in complex with Mn2+, phosphoenolpyruvate, and N-acetylmannosaminitol (2005), J. Biol. Chem., 280, 3555-3563.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
malate-bound enzyme and with phosphoenolpyruvate or the substrate analogue N-acetylmannosaminitol	Neisseria meningitidis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	coupled assay to monitor enzyme kinetics	Neisseria meningitidis

Organism

Organism	UniProt	Comment	Textmining
Neisseria meningitidis	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O = phosphate + N-acetylneuraminate	mechanism, essential role for divalent metal ion as an electrophilic catalyst that activates the N-acetylmannosamine carbonyl prior to the addition of phosphoenolpyruvate	Neisseria meningitidis	a

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Release 2023.1 (January 2023)