4rzi

</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=4rzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rzi OCA], [https://pdbe.org/4rzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rzi RCSB], [https://www.ebi.ac.uk/pdbsum/4rzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rzi ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

PhaB (acetoacetyl-CoA reductase) catalyzes the reduction of acetoacetyl-CoA to (R)-3-hydroxybutyryl-CoA in polyhydroxybutyrate (PHB) synthesis and FabG (3-ketoacyl-acyl-carrier-protein reductase) catalyzes the beta-ketoacyl-ACP to yield (R)-3-hydroxyacyl-ACP in fatty acid biosynthesis. Both of them have been classified into the same group EC 1.1.1. PhaB is limited with substrate specificities, while FabG was considered as a potential PhaB due to broad substrate selectivity despite of low activity. Here, X-ray crystal structures of FabG and PhaB from the photosynthetic microorganism Synechocystis sp. PCC 6803 were resolved. Based on them, a high-performance FabG on acyl-CoA directed by structural evolution was constructed that may serve as a critical enzyme to partition carbon flow from fatty acid synthesis to PHA.

Structure-directed construction of a high-performance version of the enzyme FabG from the photosynthetic microorganism Synechocystis sp. PCC 6803.,Liu Y, Feng Y, Cao X, Li X, Xue S FEBS Lett. 2015 Sep 7. pii: S0014-5793(15)00815-7. doi:, 10.1016/j.febslet.2015.09.001. PMID:26358291<ref>PMID:26358291</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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