Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase.
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.[1]References
- Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase. Lawrence, M.C., Barbosa, J.A., Smith, B.J., Hall, N.E., Pilling, P.A., Ooi, H.C., Marcuccio, S.M. J. Mol. Biol. (1997) [Pubmed]
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