Expression of Trypanosoma congolense trypanothione reductase in Escherichia coli: overproduction, purification, and characterization.
The cloned trypanothione reductase gene from Trypanosoma congolense has been expressed in Escherichia coli to a level of 1% of the soluble protein. This has allowed facile purification and initial characterization of the reductase, and it appears by all criteria to be a representative member of the trypanothione reductase family. Most importantly, it shows the same exclusive substrate specificity for trypanothione over glutathione characteristic of other trypanothione reductases examined to date. The availability of the pure, cloned, sequenced reductase from T. congolense makes this enzyme a good target for structure/function studies and trypanocidal inhibitor design.
Sullivan
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FX
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Shames
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SL
Walsh
C T
CT
D000595:Amino Acid Sequence; D000818:Animals; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D005786:Gene Expression Regulation; D005822:Genetic Vectors; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000096:biosynthesis* / Q000302:isolation & purification; D010084:Oxidation-Reduction; D010957:Plasmids; D011994:Recombinant Proteins / Q000096:biosynthesis*; D012995:Solubility; D014348:Trypanosoma congolense / Q000201:enzymology / Q000235:genetics*
D011994:Recombinant Proteins; D009247:NADH, NADPH Oxidoreductases; C049608:trypanothione reductase