Does N-hydroxyglycine inhibit plant and fungal laccases?
| Autor: | Richard A. Kjonaas, William H. Flurkey, Jingming Zhang |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Laccase
chemistry.chemical_classification biology Sodium periodate Tolidine chemistry.chemical_element Plant Science General Medicine Horticulture Biochemistry Oxygen Enzyme assay chemistry.chemical_compound Enzyme chemistry Enzyme inhibitor biology.protein Organic chemistry Molecular Biology Agaricus bisporus |
| Zdroj: | Phytochemistry. 52:775-783 |
| ISSN: | 0031-9422 |
| DOI: | 10.1016/s0031-9422(99)00302-7 |
| Popis: | The effect of N -hydroxyglycine on the oxidation of substrates, syringaldazine, tolidine, 2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) and 2,6-dimethoxyphenol, by fungal and plant laccases was examined. At μM concentrations, N -hydroxyglycine decolorized solutions of substrates oxidized enzymatically by laccase or chemically by sodium periodate. This discoloration, or bleaching, could be mistaken for inhibition of laccase activity if N-hydroxyglycine was added to assays for laccase that monitored colored products. N -hydroxyglycine also affected oxygen consumption assays when some of these substrates were oxidized enzymatically or chemically. Spectral scans of the products formed during enzymatic or chemical oxidation of the substrates indicated that addition of N -hydroxyglycine caused a general decrease in absorption. Except for 2,6-dimethoxyphenol, no formation of new absorption peaks was noted. These results suggest that N -hydroxyglycine may not be a “classical” enzyme inhibitor of laccase, but that this compound interferes with both spectrophotometric and oxygen uptake enzyme assays for laccase. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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