In vitro reconstruction of tetronate RK-682 biosynthesis.
The protein phosphatase inhibitor RK-682 is one of a number of potentially valuable tetronate polyketide natural products. Understanding how the tetronate ring is formed has been frustrated by the inaccessibility of the putative substrates. We report the heterologous expression of rk genes in Saccharopolyspora erythraea and reconstitution of the RK-682 pathway using recombinant enzymes, and we show that RkD is the enzyme required for RK-682 formation from acyl carrier protein-bound substrates.
Sun
Yuhui
Y
Department of Biochemistry, University of Cambridge, Cambridge, UK. ys293@mole.bio.cam.ac.uk
Hahn
Frank
F
Demydchuk
Yuliya
Y
Chettle
James
J
Tosin
Manuela
M
Osada
Hiroyuki
H
Leadlay
Peter F
PF
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D005810:Multigene Family; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors* / Q000096:biosynthesis / Q000737:chemistry; D016930:Saccharopolyspora / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; C094097:RK 682; D010749:Phosphoprotein Phosphatases