4e8g

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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=4e8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e8g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e8g RCSB], [http://www.ebi.ac.uk/pdbsum/4e8g 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=4e8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e8g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e8g RCSB], [http://www.ebi.ac.uk/pdbsum/4e8g PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/A1B198_PARDP A1B198_PARDP]] Catalyzes the 2-epimerization of trans-4-hydroxy-L-proline betaine (tHyp-B) to cis-4-hydroxy-D-proline betaine (cHyp-B). Is involved in a catabolic pathway that degrades tHyp-B to alpha-ketoglutarate. This pathway would permit the utilization of tHyp-B as a carbon and nitrogen source in the absence of osmotic stress, since tHyp-B functions as an osmolyte and is not catabolized when it is needed as osmoprotectant. Can also catalyze the racemization of L-proline betaine.<ref>PMID:24056934</ref>
==See Also==
==See Also==
*[[Mandelate racemase|Mandelate racemase]]
*[[Mandelate racemase|Mandelate racemase]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 07:17, 25 December 2014

Crystal structure of an enolase (mandelate racemase subgroup) from paracococus denitrificans pd1222 (target nysgrc-012907) with bound mg

4e8g, resolution 2.00Å

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