Mc. Lawrence et al., STRUCTURE AND MECHANISM OF A SUBFAMILY OF ENZYMES RELATED TO N-ACETYLNEURAMINATE LYASE, Journal of Molecular Biology, 266(2), 1997, pp. 381-399
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 kno
wn three-dimensional structures and we now proceed to show their struc
tural and functional relationship to two further proteins, trans-o-hyd
roxybenzylidenepyruvate hydratase-aldolase and D-4-deoxy-5-oxoglucarat
e dehydratase. These enzymes are all thought to involve intermediate S
chiff-base formation with their respective substrates. In order to und
erstand the nature of this intermediate, we have determined the three-
dimensional structure of N-acetylneuraminate lyase in complex with hyd
roxypyruvate (a product analogue) and in complex with one of its produ
cts (pyruvate). From these structures we deduce the presence of a clos
ely similar Schiff-base forming motif in all members of the N-acetylne
uraminate lyase sub-family. A fifth protein, MosA, is also confirmed t
o be a member of the sub-family although the involvement of an interme
diate Schiff-base in its proposed reaction is unclear. (C) 1997 Academ
ic Press Limited.