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Gene Review

GPD2  -  glycerol-3-phosphate dehydrogenase 2...

Homo sapiens

Synonyms: GDH2, GPD-M, GPDH-M, GPDM, Glycerol-3-phosphate dehydrogenase, mitochondrial, ...
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Disease relevance of GPD2


High impact information on GPD2

  • The gene frequencies of GDH1, GDH2, and GDH3 in these ethnic groups are significantly different from those reported in Caucasians [4].
  • Mitochondrial FAD-linked glycerophosphate dehydrogenase (mGPDH) is thought to be an important factor for glucose sensing in pancreatic beta cells [1].
  • Linkage group 7 consists of sSOD-1 (cytosolic superoxide dismutase), GPD-2 (glycerol-3-phosphate dehydrogenase), mME (mitochondrial malic enzyme), and the sex determining locus [5].
  • Study of structure-function relationships, using site-directed mutagenesis of GLUD1 at single sites differing from GLUD2, showed that the Arg443Ser and the Gly456Ala change reproduced some, but not all, of the properties of hGDH2 [6].
  • Functional analyses of highly purified recombinant wild-type hGDH2 revealed that this adaptive evolution dissociated the enzyme from GTP control, permitted regulation almost entirely by ADP and/or L-leucine, and fine-tuned its activity to the relatively low cellular pH that occurs in synaptic astrocytes during excitatory transmission [6].

Chemical compound and disease context of GPD2


Biological context of GPD2

  • Replacement of Ser by Arg at the 443 site by cassette mutagenesis abolished the heat lability of hGDH2 with a similar half-life of hGDH1 [2].
  • SUBJECTS: Diabetic patients identified by a population-based targeted screening procedure (SDM patients), consisting of a screening questionnaire and a fasting capillary glucose measurement followed by diagnostic testing, were compared with newly diagnosed diabetic patients in general practice (GPDM patients) [3].

Anatomical context of GPD2


Associations of GPD2 with chemical compounds

  • One-electron acceptor, potassium ferricyanide, highly stimulated the rate of GP-dependent antimycin A-insensitive oxygen uptake, which was prevented by inhibitors of mitochondrial GP dehydrogenase (mGPDH) or by coenzyme Q (CoQ) [8].
  • These results indicate that hydrogen peroxide is produced directly by mGPDH and reflect the differences in the transport of reducing equivalents from mGPDH and succinate dehydrogenase to the CoQ pool [8].
  • GDH2 varied similarly to PFK and IDHNADP during OC plant development, whereas it behaved like isocitrate lyase during RS plant development [9].
  • The mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase (mGPDH) is an essential component of the glycerol phosphate shuttle which transfers reduction equivalents from the cytoplasm into the mitochondria [11].
  • In the present study, the cassette mutagenesis at several putative positions (K94, G96, K118, K130, or D172) was performed to examine the residues involved in the glutamate-binding of the human glutamate dehydrogenase isozymes (hGDH1 and hGDH2) [12].

Other interactions of GPD2

  • Transcription of gpd1 could be detected during vegetative growth under both aerobic and anaerobic conditions, whereas neither gpd2 nor gpd3 transcription was detected, indicating that gpd1 is the major transcribed gpd gene [13].

Analytical, diagnostic and therapeutic context of GPD2


  1. Detection of variants in the mitochondrial glycerophosphate dehydrogenase gene in Japanese NIDDM patients. Takeuchi, Y., Matsutani, A., Oka, Y. Diabetologia (1997) [Pubmed]
  2. Important role of Ser443 in different thermal stability of human glutamate dehydrogenase isozymes. Yang, S.J., Huh, J.W., Hong, H.N., Kim, T.U., Cho, S.W. FEBS Lett. (2004) [Pubmed]
  3. Prevalence of macrovascular disease amongst type 2 diabetic patients detected by targeted screening and patients newly diagnosed in general practice: the Hoorn Screening Study. Spijkerman, A.M., Henry, R.M., Dekker, J.M., Nijpels, G., Kostense, P.J., Kors, J.A., Ruwaard, D., Stehouwer, C.D., Bouter, L.M., Heine, R.J. J. Intern. Med. (2004) [Pubmed]
  4. Glucose dehydrogenase polymorphism among ethnic groups of Singapore--with report of two additional alleles (GDH4 and GDH5). Saha, N., Bhattacharyya, S.P., Yeoh, S.C., Chua, S.P., Ratnam, S.S. Am. J. Hum. Genet. (1987) [Pubmed]
  5. Genetic mapping in Xenopus laevis: eight linkage groups established. Graf, J.D. Genetics (1989) [Pubmed]
  6. Properties and molecular evolution of human GLUD2 (neural and testicular tissue-specific) glutamate dehydrogenase. Kanavouras, K., Mastorodemos, V., Borompokas, N., Spanaki, C., Plaitakis, A. J. Neurosci. Res. (2007) [Pubmed]
  7. Genetic mapping and chromosome localization of the rat mitochondrial glycerol-3-phosphate dehydrogenase gene, a candidate for non-insulin-dependent diabetes mellitus. Koike, G., Van Vooren, P., Shiozawa, M., Galli, J., Li, L.S., Glaser, A., Balasubramanyam, A., Brown, L.J., Luthman, H., Szpirer, C., MacDonald, M.J., Jacob, H.J. Genomics (1996) [Pubmed]
  8. Glycerophosphate-dependent hydrogen peroxide production by brown adipose tissue mitochondria and its activation by ferricyanide. Drahota, Z., Chowdhury, S.K., Floryk, D., Mrácek, T., Wilhelm, J., Rauchová, H., Lenaz, G., Houstek, J. J. Bioenerg. Biomembr. (2002) [Pubmed]
  9. Variation in levels of enzymes related to energy metabolism in alternative developmental pathways of Blastocladiella emersonii. Ingebretsen, O.C., Sanner, T. J. Bacteriol. (1976) [Pubmed]
  10. The expression of human glycerol-3-phosphate dehydrogenase in human/rodent somatic-cell hybrids. Edwards, Y., McMillan, S.L., Kielty, C., Shaw, M.A. Biochem. Genet. (1985) [Pubmed]
  11. Multiple promoters direct the tissue-specific expression of rat mitochondrial glycerol-3-phosphate dehydrogenase. Weitzel, J.M., Grott, S., Radtke, C., Kutz, S., Seitz, H.J. Biol. Chem. (2000) [Pubmed]
  12. Reactive amino acid residues involved in glutamate-binding of human glutamate dehydrogenase isozymes. Yoon, H.Y., Cho, E.H., Yang, S.J., Lee, H.J., Huh, J.W., Choi, M.M., Cho, S.W. Biochimie (2004) [Pubmed]
  13. Cloning of glyceraldehyde-3-phosphate dehydrogenase-encoding genes in Mucor circinelloides (Syn. racemosus) and use of the gpd1 promoter for recombinant protein production. Wolff, A.M., Arnau, J. Fungal Genet. Biol. (2002) [Pubmed]
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