4nmw
From Proteopedia
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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=4nmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nmw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nmw RCSB], [http://www.ebi.ac.uk/pdbsum/4nmw 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=4nmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nmw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nmw RCSB], [http://www.ebi.ac.uk/pdbsum/4nmw PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/BIOH_SALTY BIOH_SALTY]] The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters (By similarity). | ||
==See Also== | ==See Also== | ||
Revision as of 05:34, 25 December 2014
Crystal Structure of Carboxylesterase BioH from Salmonella enterica
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