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HOT5  -  alcohol dehydrogenase class-3

Arabidopsis thaliana

Synonyms: ADH2, ALCOHOL DEHYDROGENASE 2, ATGSNOR1, FALDH, GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE, ...
 
 
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High impact information on ADH2

  • The DNA sequence contains an open reading frame capable of encoding a polypeptide the same length as maize ADH1 and ADH2 (379 amino acids) and having approximately equal to 80% homology with both maize enzymes [1].
  • Computational sequence analysis indicated that a conserved local sequence motif of pyruvate formate-lyase is found in the Arabidopsis thaliana genome, and this enzyme might be the source of formate for FDH in plants [2].
  • The extent of phosphorylation of both FDH and PDH was strongly decreased by NAD+, formate, and pyruvate, indicating that reversible phosphorylation of FDH and PDHs was regulated in a similar fashion [2].
  • Modification of intracellular levels of glutathione-dependent formaldehyde dehydrogenase alters glutathione homeostasis and root development [3].
  • Glutathione (GSH)-dependent formaldehyde dehydrogenase (FALDH) is a highly conserved medium-chain dehydrogenase reductase and the main enzyme that metabolizes intracellular formaldehyde in eukaryotes [3].
 

Biological context of ADH2

  • By using combinations of matrix-assisted laser desorption/ionization mass spectrometry and electrospray ionization tandem mass spectrometry, several phosphorylation sites were identified for the first time in FDH and PDH [2].
  • Therefore, it is interesting to investigate the regulation of FALDH by mechanical wounding and plant hormones involved in signal transduction [4].
  • The maize Adh2 gene promoter is constitutively hypersensitive to DNase I, with the exception of a small region that extends to include the TATA box as the gene becomes active [5].
  • Arabidopsis thaliana mutants with modified levels of FALDH (both by over- and under-expression of the FALDH-encoding gene) show a significant reduction of root length, and this phenotype correlates with an overall decrease of intracellular GSH levels and alteration of spatial distribution of GSH in the root meristem [3].
 

Associations of ADH2 with chemical compounds

 

Analytical, diagnostic and therapeutic context of ADH2

  • Isoelectric focusing/SDS-PAGE two-dimensional gels separated FDH and PDH and resolved several different phosphorylated forms of FDH [2].
  • Effects of uptake of several C-1 compounds were evaluated by Northern blot analysis using cDNA of A. thaliana FDH prepared by cloning on the basis of known sequence [6].

References

  1. Molecular cloning and DNA sequence of the Arabidopsis thaliana alcohol dehydrogenase gene. Chang, C., Meyerowitz, E.M. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  2. Phosphorylation of formate dehydrogenase in potato tuber mitochondria. Bykova, N.V., Stensballe, A., Egsgaard, H., Jensen, O.N., Moller, I.M. J. Biol. Chem. (2003) [Pubmed]
  3. Modification of intracellular levels of glutathione-dependent formaldehyde dehydrogenase alters glutathione homeostasis and root development. Espunya, M.C., D??az, M., Moreno-Romero, J., Mart??nez, M.C. Plant Cell Environ. (2006) [Pubmed]
  4. The gene encoding glutathione-dependent formaldehyde dehydrogenase/GSNO reductase is responsive to wounding, jasmonic acid and salicylic acid. Díaz, M., Achkor, H., Titarenko, E., Martínez, M.C. FEBS Lett. (2003) [Pubmed]
  5. Permeabilized Arabidopsis protoplasts provide new insight into the chromatin structure of plant alcohol dehydrogenase genes. Paul, A.L., Ferl, R.J. Dev. Genet. (1998) [Pubmed]
  6. Formate dehydrogenase gene of Arabidopsis thaliana is induced by formaldehyde and not by formic acid. Fukusaki, E., Ikeda, T., Shiraishi, T., Nishikawa, T., Kobayashi, A. J. Biosci. Bioeng. (2000) [Pubmed]
 
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