Synthesis and enzymology of modifiedN-benzyloxycarbonyl-L-cysteinylglycyl-3,3-dimethylaminopropylamide disulphides as alternative substrates for trypanothione reductase fromTrypanosoma crud: Part 3
| Autor: | Alan H. Fairlamb, Jacqui Garforth, T. Besheya, C. T. Yuen, Kenneth T. Douglas, James H. McKie, Rabih Jaouhari |
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| Rok vydání: | 1999 |
| Předmět: |
Stereochemistry
Trypanosoma cruzi Clinical Biochemistry Trypanothione Biochemistry law.invention chemistry.chemical_compound law Animals NADH NADPH Oxidoreductases Disulfides Enzyme kinetics Amino Acids chemistry.chemical_classification biology Organic Chemistry Dipeptides Glutathione biology.organism_classification Amino acid Oxygen Kinetics Models Chemical chemistry Recombinant DNA Trypanothione reductase Cysteine |
| Zdroj: | Amino Acids. 17:175-183 |
| ISSN: | 1438-2199 0939-4451 |
| Popis: | 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 K(m) 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 K(m) values by 16.6 and 7.4 fold, respectively. These observations were consistent with the K(m) values referring primarily to binding for this series of nonspecific substrates. |
| Databáze: | OpenAIRE |
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