Literature summary for 4.1.3.3 extracted from

Lee, J.O.; Yi, J.K.; Lee, S.G.; Takahashi, S.; Kim, B.G.
Production of N-acetylneuraminic acid from N-acetylglucosamine and pyruvate using recombinant human renin binding protein and sialic acid aldolase in one pot (2004), Enzyme Microb. Technol., 35, 121-125.

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Application

Application	Comment	Organism
synthesis	method to produce N-acetylneuraminic acid efficiently. Using a recombinant human renin binding protein (rhRnBp) showing GlcNAc-2-epimerase activity and Escherichia coli sialic acid aldolase, about 80% conversion yield of Neu5Ac is obtained in the coupling reaction under 10fold excess of pyruvate to GlcNAc based on the initial concentration of GlcNAc. The equilibrium of GlcNAc-2-epimerase reaction is not affected by temperature, whereas that of sialic acid aldolase reaction is shifted toward Neu5Ac by lowering the reaction temperature. Low temperatures improve the conversion yield of Neu5Ac, but decrease the reaction rate in the coupling reaction. A high reaction rate as well as a high conversion yield can be achieved by shifting the temperature of the coupling reaction during the reaction	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	BL21(DE3)	-

Synonyms

Synonyms	Comment	Organism
Sialic acid aldolase	-	Escherichia coli

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Release 2023.1 (January 2023)