4nhd
From Proteopedia
(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=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [http://www.ebi.ac.uk/pdbsum/4nhd 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=4nhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nhd RCSB], [http://www.ebi.ac.uk/pdbsum/4nhd PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FABH1_VIBCH FABH1_VIBCH]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity). | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 04:44, 25 December 2014
Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Vibrio Cholerae in complex with Coenzyme A
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Categories: Vibch | Anderson, W F | Structural genomic | Hou, J | Langner, K | Minor, W | Zheng, H | Csgid | Transferase | Vibrio cholerae
