Download MendeleyStructure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase.
Lawrence, M.C., Barbosa, J.A.R.G., Smith, B.J., Hall, N.E., Pilling, P.A., Ooi, H.C., Marcuccio, S.M.(1997) J Mol Biol 266: 381-399
- PubMed: 9047371
- DOI: https://doi.org/10.1006/jmbi.1996.0769
- Primary Citation of Related Structures:
1FDY, 1FDZ - 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.
Organizational Affiliation:
Biomolecular Research Institute, Parkville, Victoria, Australia.
