Premium
Structure‐directed construction of a high‐performance version of the enzyme FabG from the photosynthetic microorganism Synechocystis sp. PCC 6803
Author(s) -
Liu Yinghui,
Feng Yanbin,
Cao Xupeng,
Li Xia,
Xue Song
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.09.001
Subject(s) - reductase , enzyme , biology , photosynthesis , stereochemistry , chemistry , biochemistry
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.