The three-dimensional structure of N -acetylneuraminate lyase from Escherichia coli

Abstract

Background N -acetylneuraminate lyase catalyzes the cleavage of N -acetylneuraminic acid (sialic acid) to form pyruvate and N - acetyl- d -mannosamine. The enzyme plays an important role in the regulation of sialic acid metabolism in bacteria. The reverse reaction can be exploited for the synthesis of sialic acid and some of its derivatives. Results The structure of the enzyme from Escherichia coli has been determined to 2.2 å resolution by X-ray crystallography. The enzyme is shown to be a tetramer, in which each subunit consists of an α/β-barrel domain followed by a carboxy-terminal extension of three α-helices. Conclusions The active site of the enzyme is tentatively identified as a pocke..