1fdy
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(New page: 200px<br /><applet load="1fdy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fdy, resolution 2.45Å" /> '''N-ACETYLNEURAMINATE ...)
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Revision as of 12:43, 20 November 2007
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N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE
Overview
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.
About this Structure
1FDY is a Single protein structure of sequence from Escherichia coli with 3PY as ligand. Active as N-acetylneuraminate lyase, with EC number 4.1.3.3 Full crystallographic information is available from OCA.
Reference
Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase., Lawrence MC, Barbosa JA, Smith BJ, Hall NE, Pilling PA, Ooi HC, Marcuccio SM, J Mol Biol. 1997 Feb 21;266(2):381-99. PMID:9047371
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