NanA, also known as N-acetylneuraminate lyase, belongs to the family of lyases, specifically the oxoacid- lyases, which cleave carbon-carbon bonds. NanA catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetyl-D-mannosamine. This protein was inhibited by reduction with NaBH4 in the presence of the substrate, indicating that it belongs to the Schiff-base-forming Class I aldolases.