N-acetylneuraminate lyase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate. [EC:4.1.3.3, RHEA:23296]

N-acetylneuraminate lyase activity catalyzes the cleavage of N-acetylneuraminic acid (Neu5Ac), a sialic acid, into pyruvate and N-acetylmannosamine (ManNAc). This reaction is an important step in the metabolism of sialic acids, which are found in various glycoconjugates, including glycoproteins and glycolipids. The enzyme utilizes a mechanism involving a Schiff base intermediate formed between the substrate and a lysine residue in the active site. This intermediate is then hydrolyzed to release the products. N-acetylneuraminate lyase activity is essential for the biosynthesis of sialic acids and their derivatives, which are involved in a wide range of biological processes, including cell adhesion, signal transduction, and immune recognition. The enzyme plays a crucial role in the degradation of sialic acids, contributing to the recycling of these sugars within the cell. It is also involved in the production of ManNAc, which serves as a precursor for the synthesis of other important molecules, such as glycosaminoglycans and hyaluronic acid.'
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Proteins (1)

Compounds (2)