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Gene Review

Sodh-1  -  Sorbitol dehydrogenase 1

Drosophila melanogaster

Synonyms: BG:DS00464.2, CG1982, DM_7298873, Dmel\CG1982, Sdh-1, ...
 
 
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High impact information on Sodh-1

  • Comparisons based on peptides from segments of sorbitol dehydrogenase reveal that homologous regions with 38% identity include two ligands to the active site zinc atom in liver alcohol dehydrogenase, as well as further important residues [1].
  • Sdh-1 and Sdh-2 genes were located at positions 84E-F and 86D in polytene chromosomes [2].
  • In liver alcohol dehydrogenase no Tyr residue is appreciably labelled, while in the homologous sorbitol dehydrogenase Tyr-109 is specifically labelled; the difference corresponds to a segment correlating with subunit interactions and the different quaternary structures of the proteins [3].
  • These include (1) a soluble NAD-dependent sorbitol dehydrogenase (NAD-SoDHS), (2) a mitochondrial NAD-dependent sorbitol dehydrogenase (NAD-SoDHm), and (3) a soluble NADP-dependent sorbitol dehydrogenase (NADP-SoDH) [4].
 

Biological context of Sodh-1

  • At the genomic level, two genes, Sdh-1 and Sdh-2, have a single transcriptional start site and no functional TATA box [2].

References

  1. Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. Jörnvall, H., Persson, M., Jeffery, J. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  2. Sorbitol dehydrogenase of Drosophila. Gene, protein, and expression data show a two-gene system. Luque, T., Hjelmqvist, L., Marfany, G., Danielsson, O., El-Ahmad, M., Persson, B., Jörnvall, H., González-Duarte, R. J. Biol. Chem. (1998) [Pubmed]
  3. Identification of reactive tyrosine residues in cysteine-reactive dehydrogenases. Differences between liver sorbitol, liver alcohol and Drosophila alcohol dehydrogenases. Prozorovski, V., Krook, M., Atrian, S., Gonzàlez-Duarte, R., Jörnvall, H. FEBS Lett. (1992) [Pubmed]
  4. Genetic control of soluble NAD-dependent sorbitol dehydrogenase in Drosophila melanogaster. Bischoff, W.L. Biochem. Genet. (1976) [Pubmed]
 
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