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Literature summary extracted from

  • Hwang, T.S.; Hung, C.H.; Teo, C.F.; Chen, G.T.; Chang, L.S.; Chen, S.F.; Chen, Y.J.; Lin, C.H.
    Structural characterization of Escherichia coli sialic acid synthase (2002), Biochem. Biophys. Res. Commun., 295, 167-173.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.5.1.56 a specific cleavage by endogenous proteases at Lys280 of the 40000 Da enzyme. Cleavage results in the formation of two inactive fragments of 33000 Da and 7000 Da. The fragmentation is associated with a significant change of the enzyme from a tetrameric to trimeric form, and alterations in both secondary and native quarternary structures Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.56 40538
-
4 * 40538, LC-MS analysis Escherichia coli
2.5.1.56 135000
-
recombinant protein containing a hexahistidine tag at the N-terminus, gel filtration Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.56 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.56 N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
-
Escherichia coli N-acetylneuraminate + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
2.5.1.56 tetramer 4 * 40538, LC-MS analysis Escherichia coli