Search

Research has been conducted on S-adenosylmethionine decarboxylase from Trypanosoma cruzi. The role of putrescine in polypeptide processing reaction activation and enzyme activity in S-adenosylmethionine decarboxylase has been investigated and the details are presented.

Research has been conducted on the S-adenosylmethionine decarboxylase from Trypanosoma cruzi. The catalysis of the pyruvoyl-dependent S-adenosylmethionine decarboxylation has been carried out.

Analysis of the formation kinetics of ornithine decarboxylase (ODC) from mice and two parasitic protozoa, Leishmania donovani and Trypanosoma brucei, reveals the spontaneous formation of cross-species heterodimers in mice and T. brucei. The dimer interface of ODC has a highly conserved amino acid composition in T. brucei and mice and the substrate binding characteristics of the heterodimers resemble those of the wild-type enzyme. No cross-species heterodimers form between ODC of mouse or T. brucei and L. donovani and the ODC subunits in L. donovani do not exhibit rapid equilibrium as those of the other two species.

Structure-based docking and functional analyses of REDD1, a conserved stress-response protein that regulates mTORC1, a critical regulator of cell growth and proliferation that is implicated in cancer is described. The results from the sequence conservation mapping to the surface of the structure and mutagenesis studies distinguished a region likely to interact with effector proteins that is essential for REDD1-mediated mTORC1 inhibition.