2yda: Difference between revisions

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<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=2yda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yda OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yda RCSB], [http://www.ebi.ac.uk/pdbsum/2yda PDBsum]</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=2yda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yda OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yda RCSB], [http://www.ebi.ac.uk/pdbsum/2yda PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/O54288_SULSO O54288_SULSO]] Involved in the degradation of glucose and galactose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze the reversible cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-deoxygalactonate (KDGal). It is equally active with both D- and L-glyceraldehyde.<ref>PMID:10527934</ref> <ref>PMID:12824170</ref> <ref>PMID:16330030</ref> 
==See Also==
*[[Aldolase|Aldolase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 2-dehydro-3-deoxyglucarate aldolase]]
[[Category: 2-dehydro-3-deoxyglucarate aldolase]]
[[Category: Sulfolobus solfataricus]]
[[Category: Sulfolobus solfataricus]]
[[Category: Angelopoulou, M.]]
[[Category: Angelopoulou, M]]
[[Category: Bull, S D.]]
[[Category: Bull, S D]]
[[Category: Crennell, S J.]]
[[Category: Crennell, S J]]
[[Category: Danson, M J.]]
[[Category: Danson, M J]]
[[Category: Hough, D W.]]
[[Category: Hough, D W]]
[[Category: Royer, S F.]]
[[Category: Royer, S F]]
[[Category: Biocatalysis]]
[[Category: Biocatalysis]]
[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]

Revision as of 17:27, 24 December 2014

Sulfolobus sulfataricus 2-keto-3-deoxygluconate aldolase Y103F,Y130F, A198F variantSulfolobus sulfataricus 2-keto-3-deoxygluconate aldolase Y103F,Y130F, A198F variant

Structural highlights

2yda is a 2 chain structure with sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:2-dehydro-3-deoxyglucarate aldolase, with EC number 4.1.2.20
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[O54288_SULSO] Involved in the degradation of glucose and galactose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze the reversible cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-deoxygalactonate (KDGal). It is equally active with both D- and L-glyceraldehyde.[1] [2] [3]

See Also

References

  1. ↑ Buchanan CL, Connaris H, Danson MJ, Reeve CD, Hough DW. An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates. Biochem J. 1999 Nov 1;343 Pt 3:563-70. PMID:10527934
  2. ↑ Lamble HJ, Heyer NI, Bull SD, Hough DW, Danson MJ. Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase. J Biol Chem. 2003 Sep 5;278(36):34066-72. Epub 2003 Jun 24. PMID:12824170 doi:http://dx.doi.org/10.1074/jbc.M305818200
  3. ↑ Lamble HJ, Theodossis A, Milburn CC, Taylor GL, Bull SD, Hough DW, Danson MJ. Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeon Sulfolobus solfataricus. FEBS Lett. 2005 Dec 19;579(30):6865-9. Epub 2005 Dec 1. PMID:16330030 doi:http://dx.doi.org/10.1016/j.febslet.2005.11.028

2yda, resolution 1.91Å

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