TY - JOUR
T1 - The bifunctional glyceryl transferase/phosphatase OzmB belonging to the HAD superfamily that diverts 1,3-bisphosphoglycerate into polyketide biosynthesis
AU - Dorrestein, Pieter C.
AU - Van Lanen, Steven G.
AU - Li, Wenli
AU - Zhao, Chunhua
AU - Deng, Zixin
AU - Shen, Ben
AU - Kellener, Neil L.
PY - 2006/8/16
Y1 - 2006/8/16
N2 - The HAD superfamily protein OzmB from the oxazolomycin biosynthetic pathway is shown to divert the primary metabolite 1,3-diphosphoglycerate into the polyketide biosynthetic pathway as glycerate via loading of a carrier protein. Each of the stepsactivation of d-3-phosphoglycerate, dephosphorylation while attached to a cysteine on OzmB, and subsequent transfer of glycerate to the phosphopantetheinyl thiol of an acyl carrier proteinwas monitored by nanospray Fourier transform mass spectrometry. This activation of phosphoglycerate represents a general mechanism of diverting glycolytic metabolites into glyceryl-derived polyketides.
AB - The HAD superfamily protein OzmB from the oxazolomycin biosynthetic pathway is shown to divert the primary metabolite 1,3-diphosphoglycerate into the polyketide biosynthetic pathway as glycerate via loading of a carrier protein. Each of the stepsactivation of d-3-phosphoglycerate, dephosphorylation while attached to a cysteine on OzmB, and subsequent transfer of glycerate to the phosphopantetheinyl thiol of an acyl carrier proteinwas monitored by nanospray Fourier transform mass spectrometry. This activation of phosphoglycerate represents a general mechanism of diverting glycolytic metabolites into glyceryl-derived polyketides.
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U2 - 10.1021/ja0639362
DO - 10.1021/ja0639362
M3 - Article
C2 - 16895402
AN - SCOPUS:33747607747
SN - 0002-7863
VL - 128
SP - 10386
EP - 10387
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 32
ER -