1fdz

<StructureSection load='1fdz' size='340' side='right' caption='[[1fdz]], [[Resolution|resolution]] 2.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[1fdz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FDZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FDZ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NPL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylneuraminate_lyase N-acetylneuraminate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.3 4.1.3.3] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdz OCA], [http://pdbe.org/1fdz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fdz RCSB], [http://www.ebi.ac.uk/pdbsum/1fdz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fdz ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/NANA_ECOLI NANA_ECOLI]] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate.[HAMAP-Rule:MF_01237]

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:9047371</ref>

 

[[Category: Bacillus coli migula 1895]]

[[Category: N-acetylneuraminate lyase]]

[[Category: Barbosa, J A.R G]]

[[Category: Hall, N E]]

[[Category: Lawrence, M C]]

[[Category: Marcuccio, S M]]

[[Category: Ooi, H C]]

[[Category: Pilling, P A]]

[[Category: Smith, B J]]

[[Category: Oxo-acid lyase]]