Purification and characterization of glycerol‐3‐phosphate dehydrogenase of Saccharomyces cerevisiae

@article{Albertyn1992PurificationAC,
  title={Purification and characterization of glycerol‐3‐phosphate dehydrogenase of Saccharomyces cerevisiae},
  author={Jacobus Albertyn and A. van Tonder and Bernard Alexander Prior},
  journal={FEBS Letters},
  year={1992},
  volume={308}
}
The NAD‐dependent glycerol‐3‐phosphate dehydrogenase (glycerol‐3‐phosphate:NAD??? oxidoreductase; EC 1.1.1.8; G3P DHG) was purified 178‐fold to homogeneity from Saceharomyces cerevisiue strain H44‐3D by affinity‐ and ion‐exchange chromatography, SDS‐PAGE indicited that the enzyme had a molecular mass of approximately 42,000 (± 1.000) whereas a molecular mass of 68,000 was observed using gel filtration, implying that the enzyme may exist as a dimer, The pH optimum for the reduction or… 
Fast purification and kinetic studies of the glycerol-3-phosphate dehydrogenase from the yeast Saccharomyces cerevisiae.
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Cloning and characterization of CmGPD1, the Candida magnoliae homologue of glycerol-3-phosphate dehydrogenase.
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In a complementation study, CmGpd1p rescued the ability of glycerol synthesis and salt tolerance in a Saccharomyces cerevisiae GPD1DeltaGPD2Delta mutant strain, indicating that CMGPD1 encodes a functional homologue of S. cerevisia GPDH.
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The two isoenzymes for yeast NAD+‐dependent glycerol 3‐phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation
TLDR
It is concluded that expression of GPD2 is controlled by a novel, oxygen‐independent, signalling pathway which is required to regulate metabolism under anoxic conditions.
Expression of glycerol 3‐phosphate dehydrogenase gene (CvGPD1) in salt‐tolerant yeast Candida versatilis is stimulated by high concentrations of NaCl
TLDR
The glycerol 3‐phosphate dehydrogenase (GPDH) gene (CvGPD1) is cloned from salt‐tolerant yeast Candida versatilis from which the salt tolerance of the recombinant strain was enhanced, and NADP+‐dependent GPDH (EC 1.1.94), Cvgpd1p synthesis and recovery of Glycerol synthesis were confirmed.
Metabolic Engineering of Glycerol Production in Saccharomyces cerevisiae
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It is hypothesized that the growth defect of tpi1-null mutants is caused by mitochondrial reoxidation of cytosolic NADH, thus rendering it unavailable for dihydroxyacetone-phosphate reduction, and a quadruple mutant was constructed, which grew on glucose as the sole carbon source.
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TLDR
It is proposed that the NAD-dependent Glycerol-3-phosphate dehydrogenase functions in cellular osmoregulation by providing glycerol 3-ph phosphate for the biosynthesis of glycersol, the main compatible solute in D. hansenii, and that the enzyme is well adapted to function in yeast cells exposed to osmotic stress.
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The results are consistent with the notion that the enzyme may regulate the redox potential of the NAD+/NADH couple during fermentation.
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The effective control of dihydroxyacetone reduction catalysed via this enzyme by ATP, P 1 and NAD gave evidence for a physiological role of the enzyme in plastidic glycolysis.
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The membrane-extrinsic anaerobic glycerol-3-phosphate dehydrogenase from Escherichia coli is purified using a strain harboring a recombinant ColE1:E.
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It is shown that protein synthesis was required to establish the osmotolerance state in Saccharomyces cerevisiae, and the increased glycerol accumulation was shown to be not merely a result of enhanced production rate but also of increased retention of Glycerol.
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TLDR
An NAD-dependent glycerol-3-phosphate dehydrogenase has been isolated and purified from Saccharomyces cerevisiae by affinity and exclusion chromatography and was purified 5100-fold to a specific activity of 158.1.
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TLDR
A rapid purification procedure for glycerol-3-phosphate dehydrogenase from Dunaliella tertiolecta (strain 19-6) has been developed on the basis of affinity chromatography on Blue Sepharose and subsequent desalting by Sephadex G-50.
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TLDR
The purification procedure for isolating sn-glycerol-3-phosphate dehydrogenase from Saccharomyces cerevisiae was improved by the introduction of an ion-exchange step and a new value of 42,000 was obtained for the molecular weight by several denaturing methods.
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TLDR
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