Effects of some S-blocked glutathione derivatives on the prevalent glyoxalase II (a form) of rat liver
| Autor: | Scott J. Norton, Giovanni B. Principato, Elvio Giovannini, Vincenzo Talesa, Gabriella Rosi |
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| Rok vydání: | 1989 |
| Předmět: |
chemistry.chemical_classification
Chemistry Stereochemistry Substrate (chemistry) Glutathione Thioester Biochemistry Rats Isoenzymes chemistry.chemical_compound Cytosol Kinetics Structure-Activity Relationship Enzyme Liver Hydrolase Structure–activity relationship Animals Thiolester Hydrolases Lineweaver–Burk plot |
| Zdroj: | Enzyme. 41(3) |
| ISSN: | 0013-9432 |
| Popis: | The prevalent glyoxalase II (S-2-hydroxyacylglutathione hydrolase, EC 3.1.2.6, a form) of rat liver cytosol has been studied with a series of seven S-blocked glutathione derivatives. At pH 7.4 and 20 degrees C, only p-nitrobenzyl-S-glutathione was found completely inactive. All the other derivatives are linear competitive inhibitors of the enzyme. Ki values using S-D-lactoylglutathione as substrate are reported. Alkyl-S-glutathiones are weak inhibitors and their inhibition increases with the decrease of the length of the alkyl chain. The best inhibitors are those glutathione derivatives which contain a thioester bond (carbobenzoxy- and p-nitrocarbobenzoxy-S-glutathione) or a carbonyl group (p-chlorophenacyl-S-glutathione). Inhibition by carbobenzoxy-S-glutathione seems to be more complex since the double reciprocal plot shows deviation from linearity at low substrate concentration. |
| Databáze: | OpenAIRE |
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