1NAL

THE THREE-DIMENSIONAL STRUCTURE OF N-ACETYLNEURAMINATE LYASE FROM ESCHERICHIA COLI

Summary for 1NAL

• Entry DOI: 10.2210/pdb1nal/pdb
• Descriptor: N-ACETYLNEURAMINATE LYASE, SULFATE ION (3 entities in total)
• Functional Keywords: lyase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6L4
• Total number of polymer chains: 4
• Total formula weight: 131065.64

Authors

Izard, T.,Lawrence, M.C.,Malby, R.L.,Lilley, G.G.,Colman, P.M. (deposition date: 1994-02-28, release date: 1995-09-15, Last modification date: 2024-02-14)

Primary citation

Izard, T.,Lawrence, M.C.,Malby, R.L.,Lilley, G.G.,Colman, P.M.
The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli.
Structure, 2:361-369, 1994

PubMed Abstract: 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.

PubMed: 8081752
DOI: 10.1016/S0969-2126(00)00038-1

Experimental method

X-RAY DIFFRACTION (2.2 Å)