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Gene Review

Tb09.211.1370  -  glyceraldehyde-3-phosphate dehydrogenase

Trypanosoma brucei brucei TREU927

 
 
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High impact information on Tb09.211.1370

  • The PARP mini-exon addition region abolished transient CAT expression directed by either the gGAPDH or PARP promoters in bloodstream T. brucei implying that transplicing can be a point of stage-specific gene regulation [1].
  • The gGAPDH promoter gave rise to relatively high CAT signals upon transfection into bloodstream T. brucei and relatively low signals in procyclic T. brucei, compared with levels resulting from transfection with the procyclic acidic repetitive protein (PARP) promoter [1].
  • Guided by the crystal structures of human, T. brucei, and Leishmania mexicana glyceraldehyde-3-phosphate dehydrogenase, we designed adenosine analogs as tight binding inhibitors that occupy the pocket on the enzyme that accommodates the adenosyl moiety of the NAD+ cosubstrate [2].
  • Although adenosine is a very poor inhibitor, IC50 approximately 50 mM, addition of substituents to the 2' position of ribose and the N6-position of adenosine led to disubstituted nucleosides with micromolar to submicromolar potency in glyceraldehyde-3-phosphate dehydrogenase assays, an improvement of 5 orders of magnitude over the lead [2].
  • Gel analysis of reisolated glycosomes revealed that glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) and 3-phosphoglycerate kinase (PGK) (EC 2.7.2.3) were apparently imported intact into the glycosome [3].
 

Biological context of Tb09.211.1370

  • These proteins were found to be the glycosomal enzymes aldolase (41 kDa) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH, 36 kDa) by enzyme activity, antibody cross-reaction, and N-terminal sequencing [4].
  • Synthesis and structure-activity relationships of analogs of 2'-deoxy-2'-(3-methoxybenzamido)adenosine, a selective inhibitor of trypanosomal glycosomal glyceraldehyde-3-phosphate dehydrogenase [5].
  • Crystal structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Leishmania mexicana: implications for structure-based drug design and a new position for the inorganic phosphate binding site [6].
  • The length of the combined 3' untranslated region and poly(A) tail does not control rates of glyceraldehyde-3-phosphate dehydrogenase mRNA translation in three species of parasitic protists [7].
  • This last specific metabolic arrangement and the restriction of all but the terminal steps of glycolysis to the glycosome may be the observations required to explain the presence of distinct cytosolic and glycosomal isoenzymes of glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase [8].
 

Anatomical context of Tb09.211.1370

  • By contrast, in erythrocytes more than 95% deficiencies of PGK, GAPDH, or ALD did not cause any clinical symptoms (Schuster, R. and Holzhütter, H.-G. (1995) Eur. J. Biochem. 229, 403-418) [9].
 

Associations of Tb09.211.1370 with chemical compounds

 

Analytical, diagnostic and therapeutic context of Tb09.211.1370

References

  1. Trypanosoma brucei glycosomal glyceraldehyde-3-phosphate dehydrogenase genes are stage-regulated at the transcriptional level. Bakalara, N., Kendall, G., Michels, P.A., Opperdoes, F.R. EMBO J. (1991) [Pubmed]
  2. Structure-based design of submicromolar, biologically active inhibitors of trypanosomatid glyceraldehyde-3-phosphate dehydrogenase. Aronov, A.M., Suresh, S., Buckner, F.S., Van Voorhis, W.C., Verlinde, C.L., Opperdoes, F.R., Hol, W.G., Gelb, M.H. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  3. Biogenesis of glycosomes of Trypanosoma brucei: an in vitro model of 3-phosphoglycerate kinase import. Dovey, H.F., Parsons, M., Wang, C.C. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  4. The association of glycosomal enzymes and microtubules: a physiological phenomenon or an experimental artifact? Balaban, N., Goldman, R. Exp. Cell Res. (1990) [Pubmed]
  5. Synthesis and structure-activity relationships of analogs of 2'-deoxy-2'-(3-methoxybenzamido)adenosine, a selective inhibitor of trypanosomal glycosomal glyceraldehyde-3-phosphate dehydrogenase. Van Calenbergh, S., Verlinde, C.L., Soenens, J., De Bruyn, A., Callens, M., Blaton, N.M., Peeters, O.M., Rozenski, J., Hol, W.G., Herdewijn, P. J. Med. Chem. (1995) [Pubmed]
  6. Crystal structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Leishmania mexicana: implications for structure-based drug design and a new position for the inorganic phosphate binding site. Kim, H., Feil, I.K., Verlinde, C.L., Petra, P.H., Hol, W.G. Biochemistry (1995) [Pubmed]
  7. The length of the combined 3' untranslated region and poly(A) tail does not control rates of glyceraldehyde-3-phosphate dehydrogenase mRNA translation in three species of parasitic protists. ter Kuile, B.H., Sallés, F.J. J. Bacteriol. (2000) [Pubmed]
  8. The enzymes of the classical pentose phosphate pathway display differential activities in procyclic and bloodstream forms of Trypanosoma brucei. Cronín, C.N., Nolan, D.P., Voorheis, H.P. FEBS Lett. (1989) [Pubmed]
  9. What controls glycolysis in bloodstream form Trypanosoma brucei? Bakker, B.M., Michels, P.A., Opperdoes, F.R., Westerhoff, H.V. J. Biol. Chem. (1999) [Pubmed]
  10. Inhibition of glyceraldehyde-3-phosphate dehydrogenase by phosphorylated epoxides and alpha-enones. Willson, M., Lauth, N., Perie, J., Callens, M., Opperdoes, F.R. Biochemistry (1994) [Pubmed]
 
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