tautomycin and glycerate-1-3-biphosphate

tautomycin has been researched along with glycerate-1-3-biphosphate* in 1 studies

Other Studies

1 other study(ies) available for tautomycin and glycerate-1-3-biphosphate

Article	Year
The bifunctional glyceryl transferase/phosphatase OzmB belonging to the HAD superfamily that diverts 1,3-bisphosphoglycerate into polyketide biosynthesis. Journal of the American Chemical Society, 2006, Aug-16, Volume: 128, Issue:32 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 steps-activation 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 protein-was monitored by nanospray Fourier transform mass spectrometry. This activation of phosphoglycerate represents a general mechanism of diverting glycolytic metabolites into glyceryl-derived polyketides. Topics: Amino Acid Sequence; Diphosphoglyceric Acids; Enzyme Activation; Macrolides; Methyltransferases; Molecular Sequence Data; Oxazoles; Phosphoric Monoester Hydrolases; Pyrans; Pyrrolidinones; Sequence Alignment; Spiro Compounds; Substrate Specificity; Transferases	2006

Article

Year

The bifunctional glyceryl transferase/phosphatase OzmB belonging to the HAD superfamily that diverts 1,3-bisphosphoglycerate into polyketide biosynthesis.

Journal of the American Chemical Society, 2006, Aug-16, Volume: 128, Issue:32

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 steps-activation 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 protein-was monitored by nanospray Fourier transform mass spectrometry. This activation of phosphoglycerate represents a general mechanism of diverting glycolytic metabolites into glyceryl-derived polyketides.

Topics: Amino Acid Sequence; Diphosphoglyceric Acids; Enzyme Activation; Macrolides; Methyltransferases; Molecular Sequence Data; Oxazoles; Phosphoric Monoester Hydrolases; Pyrans; Pyrrolidinones; Sequence Alignment; Spiro Compounds; Substrate Specificity; Transferases

2006