1fdz: Difference between revisions

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[[Image:1fdz.gif|left|200px]]
{{Seed}}
[[Image:1fdz.png|left|200px]]


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{{STRUCTURE_1fdz|  PDB=1fdz  |  SCENE=  }}  
{{STRUCTURE_1fdz|  PDB=1fdz  |  SCENE=  }}  


'''N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION'''
===N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_9047371}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_9047371}}


==About this Structure==
==About this Structure==
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[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Oxo-acid lyase]]
[[Category: Oxo-acid lyase]]
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