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GUT2  -  glycerol-3-phosphate dehydrogenase

Saccharomyces cerevisiae S288c

Synonyms: GPD-M, GPDH-M, Glycerol-3-phosphate dehydrogenase, mitochondrial, YIL155C
 
 
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High impact information on GUT2

  • Studies on the functionally isolated enzymes demonstrated that neither Nde1p nor Nde2p directly inhibits Gut2p [1].
  • Subsequently, glycerol 3-phosphate donates electrons to the respiratory chain via mitochondrial glycerol-3-phosphate dehydrogenase (Gut2p) [1].
  • Second, the activation of NADH dehydrogenase inhibited the Gut2p in such a manner that, at a saturating concentration of NADH, glycerol 3-phosphate is not used as respiratory substrate [2].
  • Mass spectrometric analysis of a tryptic digest of the corresponding 2D-gel spot identified the protein as the GUT2 gene product, the FAD-dependent mitochondrial glycerol-3-phosphate dehydrogenase [3].
  • This was confirmed by the lack of specific labeling in mitochondria from a gut2 deletion strain [3].
 

Biological context of GUT2

 

Associations of GUT2 with chemical compounds

 

Other interactions of GUT2

  • In that mutant, transcript levels from GUT1 and GUT2 are highly attenuated compared with those of the wild-type parent when both are grown on glycerol-based medium [7].
  • NDE1 and NDE2 encode isoenzymes of mitochondrial external NADH dehydrogenase; GUT2 encodes a key enzyme of the glycerol-3-phosphate shuttle [8].
  • DAR1 is distinct from GUT2, which encodes a glucose-repressed mitochondrial G3PDase, but is identical to GPD1 from S. cerevisiae, a close relative of S. diastaticus [9].
  • In addition, we have identified Gut2, the mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase, as a new substrate for Imp1 [10].

References

  1. Competition of electrons to enter the respiratory chain: a new regulatory mechanism of oxidative metabolism in Saccharomyces cerevisiae. Bunoust, O., Devin, A., Avéret, N., Camougrand, N., Rigoulet, M. J. Biol. Chem. (2005) [Pubmed]
  2. Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. Påhlman, I.L., Larsson, C., Averét, N., Bunoust, O., Boubekeur, S., Gustafsson, L., Rigoulet, M. J. Biol. Chem. (2002) [Pubmed]
  3. Photolabeling identifies an interaction between phosphatidylcholine and glycerol-3-phosphate dehydrogenase (Gut2p) in yeast mitochondria. Janssen, M.J., van Voorst, F., Ploeger, G.E., Larsen, P.M., Larsen, M.R., de Kroon, A.I., de Kruijff, B. Biochemistry (2002) [Pubmed]
  4. Carbon source-dependent transcriptional regulation of the mitochondrial glycerol-3-phosphate dehydrogenase gene, GUT2, from Saccharomyces cerevisiae. Grauslund, M., Rønnow, B. Can. J. Microbiol. (2000) [Pubmed]
  5. Cloning and characterisation of the Saccharomyces cerevisiae glycerol-3-phosphate dehydrogenase (GUT2) promoter. Sleep, D., Ogden, J.E., Roberts, N.A., Goodey, A.R. Gene (1991) [Pubmed]
  6. GUT2, a gene for mitochondrial glycerol 3-phosphate dehydrogenase of Saccharomyces cerevisiae. Rønnow, B., Kielland-Brandt, M.C. Yeast (1993) [Pubmed]
  7. Rsf1p, a protein required for respiratory growth of Saccharomyces cerevisiae. Lu, L., Roberts, G., Simon, K., Yu, J., Hudson, A.P. Curr. Genet. (2003) [Pubmed]
  8. Metabolic engineering of glycerol production in Saccharomyces cerevisiae. Overkamp, K.M., Bakker, B.M., Kötter, P., Luttik, M.A., Van Dijken, J.P., Pronk, J.T. Appl. Environ. Microbiol. (2002) [Pubmed]
  9. Cloning, sequence, and disruption of the Saccharomyces diastaticus DAR1 gene encoding a glycerol-3-phosphate dehydrogenase. Wang, H.T., Rahaim, P., Robbins, P., Yocum, R.R. J. Bacteriol. (1994) [Pubmed]
  10. The mitochondrial IMP peptidase of yeast: functional analysis of domains and identification of Gut2 as a new natural substrate. Esser, K., Jan, P.S., Pratje, E., Michaelis, G. Mol. Genet. Genomics (2004) [Pubmed]
 
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