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LmjF27.0730  -  reductase

Leishmania major strain Friedlin

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Disease relevance of LMJ_0329

  • Only 2 of 22 plasma samples from patients with visceral leishmaniasis were found to have detectable anti-reductase antibodies and peripheral blood mononuclear cells (PBMC) from one of three individuals previously infected with visceral leishmaniasis proliferated in the presence of recombinant reductase protein [1].

High impact information on LMJ_0329


Biological context of LMJ_0329

  • The DNA sequence of the P100/11E cDNA predicts an acidic polypeptide of Mr = 32,000 which shows 40-46% similarity to the superfamily of reductase proteins including 2,5-diketo-D-gluconic acid reductase, aldose reductase, aldehyde reductase, and rho-crystallin [5].

Anatomical context of LMJ_0329

  • The present study suggests that this reactivity is partly caused by T-cells recognising L. donovani reductase [1].

Associations of LMJ_0329 with chemical compounds


  1. Cloning, expression and antigenicity of the L. donovani reductase. Jensen, A.T., Kemp, K., Theander, T.G., Handman, E. APMIS (2001) [Pubmed]
  2. PTR1: a reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major. Bello, A.R., Nare, B., Freedman, D., Hardy, L., Beverley, S.M. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  3. Kinetic characterization of bifunctional thymidylate synthase-dihydrofolate reductase (TS-DHFR) from Cryptosporidium hominis: a paradigm shift for ts activity and channeling behavior. Atreya, C.E., Anderson, K.S. J. Biol. Chem. (2004) [Pubmed]
  4. Leishmania major LmACR2 is a pentavalent antimony reductase that confers sensitivity to the drug pentostam. Zhou, Y., Messier, N., Ouellette, M., Rosen, B.P., Mukhopadhyay, R. J. Biol. Chem. (2004) [Pubmed]
  5. The developmentally regulated P100/11E gene of Leishmania major shows homology to a superfamily of reductase genes. Samaras, N., Spithill, T.W. J. Biol. Chem. (1989) [Pubmed]
  6. Probing electrostatic channeling in protozoal bifunctional thymidylate synthase-dihydrofolate reductase using site-directed mutagenesis. Atreya, C.E., Johnson, E.F., Williamson, J., Chang, S.Y., Liang, P.H., Anderson, K.S. J. Biol. Chem. (2003) [Pubmed]
  7. A molecular docking strategy identifies Eosin B as a non-active site inhibitor of protozoal bifunctional thymidylate synthase-dihydrofolate reductase. Atreya, C.E., Johnson, E.F., Irwin, J.J., Dow, A., Massimine, K.M., Coppens, I., Stempliuk, V., Beverley, S., Joiner, K.A., Shoichet, B.K., Anderson, K.S. J. Biol. Chem. (2003) [Pubmed]
  8. Structures of Leishmania major pteridine reductase complexes reveal the active site features important for ligand binding and to guide inhibitor design. Schüttelkopf, A.W., Hardy, L.W., Beverley, S.M., Hunter, W.N. J. Mol. Biol. (2005) [Pubmed]
  9. Characterization and regulation of Leishmania major 3-hydroxy-3-methylglutaryl-CoA reductase. Montalvetti, A., Peña-Díaz, J., Hurtado, R., Ruiz-Pérez, L.M., González-Pacanowska, D. Biochem. J. (2000) [Pubmed]
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