Ontology highlight
ABSTRACT:
SUBMITTER: Jones DC
PROVIDER: S-EPMC2789240 | biostudies-literature | 2010 Jan
REPOSITORIES: biostudies-literature
Jones Deuan C DC Ariza Antonio A Chow Wing-Huen A WH Oza Sandra L SL Fairlamb Alan H AH
Molecular and biochemical parasitology 20090910 1
As part of a drug discovery programme to discover new treatments for human African trypanosomiasis, recombinant trypanothione reductase from Trypanosoma brucei has been expressed, purified and characterized. The crystal structure was solved by molecular replacement to a resolution of 2.3A and found to be nearly identical to the T. cruzi enzyme (root mean square deviation 0.6A over 482 Calpha atoms). Kinetically, the K(m) for trypanothione disulphide for the T. brucei enzyme was 4.4-fold lower th ...[more]