Interactions of platinum complexes, peptides, methionine and dehydrogenases
| Autor: | C. A. Mcauliffe, I. Photaki, M. Sakarellou-Daitsiotou, Paul Melius |
|---|---|
| Rok vydání: | 1977 |
| Předmět: |
chemistry.chemical_classification
Binding Sites Dipeptide Methionine L-Lactate Dehydrogenase Ligand Stereochemistry chemistry.chemical_element Alcohol General Medicine Ethylenediamines Biochemistry Alcohol Oxidoreductases chemistry.chemical_compound Enzyme chemistry Halogen Organic chemistry Histidine Cisplatin Platinum Oligopeptides |
| Zdroj: | Bioinorganic Chemistry. 7:203-210 |
| ISSN: | 0006-3061 |
| DOI: | 10.1016/s0006-3061(00)80094-0 |
| Popis: | Eight platinum-methionine complexes have been investigated as inhibitors of the alcohol (EC 1.1.1.1) and lactate (EC 1.1.1.27) dehydroganse systems. While only one complex, Pt(Met)Cl 2 , had two halogen ligands on the platinum, all the complexes were able to inhibit both enzyme systems. Of the various methionine and histidine containing peptides evaluated, the dipeptide Met-Met gave the best protection against inhibition by N-alkyl-substituted ethylenediamine-platinum complexes. The histidine containing peptides gave a slight protection against the inhibition by β-[Pt(Met)(NH 3 )Cl]Cl. Thus it appears that in the enzyme systems studied, the methionine acts as a strong ligand for platinum. |
| Databáze: | OpenAIRE |
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