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- W1870996849 abstract "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 β-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." @default.
- W1870996849 created "2016-06-24" @default.
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- W1870996849 date "2015-09-07" @default.
- W1870996849 modified "2023-09-27" @default.
- W1870996849 title "Structure-directed construction of a high-performance version of the enzyme FabG from the photosynthetic microorganism<i>Synechocystis</i> sp. PCC 6803" @default.
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- W1870996849 doi "https://doi.org/10.1016/j.febslet.2015.09.001" @default.
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