1FDZ

N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION

Summary for 1FDZ

• Entry DOI: 10.2210/pdb1fdz/pdb
• Descriptor: N-ACETYLNEURAMINATE LYASE, PYRUVIC ACID (3 entities in total)
• Functional Keywords: lyase, aldolase, oxo-acid lyase, alpha-keto-acid lyase, carbon-carbon lyase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6L4
• Total number of polymer chains: 4
• Total formula weight: 130857.75

Authors

Lawrence, M.C.,Barbosa, J.A.R.G.,Smith, B.J.,Hall, N.E.,Pilling, P.A.,Ooi, H.C.,Marcuccio, S.M. (deposition date: 1996-07-08, release date: 1997-10-22, Last modification date: 2024-10-16)

Primary citation

Lawrence, M.C.,Barbosa, J.A.R.G.,Smith, B.J.,Hall, N.E.,Pilling, P.A.,Ooi, H.C.,Marcuccio, S.M.
Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase.
J.Mol.Biol., 266:381-399, 1997

PubMed Abstract: We describe here a sub-family of enzymes related both structurally and functionally to N-acetylneuraminate lyase. Two members of this family (N-acetylneuraminate lyase and dihydrodipicolinate synthase) have known three-dimensional structures and we now proceed to show their structural and functional relationship to two further proteins, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase and D-4-deoxy-5-oxoglucarate dehydratase. These enzymes are all thought to involve intermediate Schiff-base formation with their respective substrates. In order to understand the nature of this intermediate, we have determined the three-dimensional structure of N-acetylneuraminate lyase in complex with hydroxypyruvate (a product analogue) and in complex with one of its products (pyruvate). From these structures we deduce the presence of a closely similar Schiff-base forming motif in all members of the N-acetylneuraminate lyase sub-family. A fifth protein, MosA, is also confirmed to be a member of the sub-family although the involvement of an intermediate Schiff-base in its proposed reaction is unclear.

PubMed: 9047371
DOI: 10.1006/jmbi.1996.0769

Experimental method

X-RAY DIFFRACTION (2.6 Å)