Synthesis and enzymology of modified N-benzyloxycarbonyl-L-cysteinylglycyl-3,3-dimethylaminopropylamide disulphides as alternative substrates for trypanothione reductase from Trypanosoma cruzi: Part 3

C. T. Yuen, J. Garforth, T. Besheya, R. Jaouhari, J. H. McKie, A. H. Fairlamb, K. T. Douglas

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    6 Citations (Scopus)

    Abstract

    Kinetic data for alternative substrates of recombinant trypanothione reductase from Trypanosoma cruzi were measured for a series of N-substituted-L-cysteinylglycyl-3-dimethylaminopropylamides, in which the cysteine N-substituent was either a variant of the benzyloxycarbonyl group or was L-phenylalanine or L-tryptophan. Replacing the benzylic ether oxygen atom by CH2 or NH had relatively minor effects on kcat, but raised the value of Km 4.5- and 10-fold, respectively. Similarly, relative to the carbobenzoxy group, an N-L-phenylalanyl or N-L-tryptophanyl replacement on the cysteine hardly altered kcat, but increased Km values by 16.6 and 7.4 fold, respectively. These observations were consistent with the Km values referring primarily to binding for this series of nonspecific substrates.

    Original languageEnglish
    Pages (from-to)175-183
    Number of pages9
    JournalAmino Acids
    Volume17
    Issue number2
    DOIs
    Publication statusPublished - Jun 1999

    Keywords

    • Amino acids
    • Benzyloxycarbonyl-reductase
    • Glutathione
    • Hydrocinnamoyl
    • Trypanothione

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