Extended Data Fig. 2: Purified enzymes used in this study. | Nature Catalysis

Extended Data Fig. 2: Purified enzymes used in this study.

From: A polyketoacyl-CoA thiolase-dependent pathway for the synthesis of polyketide backbones

Extended Data Fig. 2

The sources of enzymes are as follows. PKS III 2-PS was from Gerbera hybrid; DcaF was from Acinetobacter sp. ADP1; FadAx was from Pseudomonas putida; PcaF was from Pseudomonas putida; BktB was from Ralstonia eutropha; AtoB was from E. coli; EcFadA was from E. coli; PaaJ was from E. coli; HMGS was from Staphylococcus aureus; FadB was from E. coli; PaaH was from E. coli; The expected molecular weights of enzymes with N terminal 6 x His-tag calculated by tool from ExPASy, (https://web.expasy.org/compute_pi/) are indicated in parentheses. BktB (5#, 11#, 16#), PaaJ (8#, 14#) and EcFadA (7#, 12#) appeared more than once as we initially employed them for in vitro TAL biosynthesis tests (Fig. 2), and then we further purified and used them for the in vitro assay of ketoacyl-CoA thiolase, 3-ketoadipyl-CoA thiolase and PKT activities (see Fig. 6a). For EcFadA WT (7#, 12#) and EcFadA_BktB (21#), the expected MWs from ExPASy calculations are 41.9 kDa and 43.2 kDa, while actual sizes on SDS-PAGE appear ~40 kDa and ~41 kDa.

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