View source for 2bkx


==Structure and kinetics of a monomeric glucosamine-6-phosphate deaminase: missing link of the NagB superfamily==
<StructureSection load='2bkx' size='340' side='right'caption='[[2bkx]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bkx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BKX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F6R:FRUCTOSE+-6-PHOSPHATE'>F6R</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2bkv|2bkv]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucosamine-6-phosphate_deaminase Glucosamine-6-phosphate deaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.6 3.5.99.6] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bkx OCA], [https://pdbe.org/2bkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bkx RCSB], [https://www.ebi.ac.uk/pdbsum/2bkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bkx ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/NAGB_BACSU NAGB_BACSU]] Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion (By similarity). 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bk/2bkx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bkx ConSurf].
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== Publication Abstract from PubMed ==
Glucosamine 6-phosphate is converted to fructose 6-phosphate and ammonia by the action of the enzyme glucosamine 6-phosphate deaminase, NagB. This reaction is the final step in the specific GlcNAc utilization pathway and thus decides the metabolic fate of GlcNAc. Sequence analyses suggest that the NagB "superfamily" consists of three main clusters: multimeric and allosterically regulated glucosamine-6-phosphate deaminases (exemplified by Escherichia coli NagB), phosphogluconolactonases, and monomeric hexosamine-6-phosphate deaminases. Here we present the three-dimensional structure and kinetics of the first member of this latter group, the glucosamine-6-phosphate deaminase, NagB, from Bacillus subtilis. The structures were determined in ligand-complexed forms at resolutions around 1.4 Angstroms. BsuNagB is monomeric in solution and as a consequence is active (k(cat) 28 s(-1), K(m(app)) 0.13 mM) without the need for allosteric activators. A decrease in activity at high substrate concentrations may reflect substrate inhibition (with K(i) of approximately 4 mM). The structure completes the NagB superfamily structural landscape and thus allows further interrogation of genomic data in terms of the regulation of NagB and the metabolic fate(s) of glucosamine 6-phosphate.

Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase: missing link of the NagB superfamily?,Vincent F, Davies GJ, Brannigan JA J Biol Chem. 2005 May 20;280(20):19649-55. Epub 2005 Mar 8. PMID:15755726<ref>PMID:15755726</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2bkx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Deaminase 3D structures|Deaminase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Vibrio subtilis ehrenberg 1835]]
[[Category: Glucosamine-6-phosphate deaminase]]
[[Category: Large Structures]]
[[Category: Brannigan, J A]]
[[Category: Davies, G J]]
[[Category: Vincent, F]]
[[Category: Fructose-6-phosphate]]
[[Category: Hydrolase]]
[[Category: Substrate inhibition]]