Palladium--a new inhibitor of cellulase activities
| Autor: | B.R. Evans, M.G. Gooch, J. Woodward, J.P. Lassig, Michael Shultz |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
inorganic chemicals
Glycoside Hydrolases Stereochemistry Biophysics Cystine chemistry.chemical_element Cellulase Biochemistry Catalysis chemistry.chemical_compound Cellulose 1 4-beta-Cellobiosidase Organic chemistry Molecular Biology Histidine Trichoderma reesei Chromatography High Pressure Liquid chemistry.chemical_classification Trichoderma Binding Sites biology beta-Glucosidase Cell Biology biology.organism_classification Kinetics Enzyme chemistry biology.protein Palladium Cysteine |
| Zdroj: | Biochemical and biophysical research communications. 209(3) |
| ISSN: | 0006-291X |
| Popis: | Palladium complexes have been shown to strongly inhibit cellobiohydrolase I (CBH I) and endoglucanase II (EG II), two cellulases produced by Trichoderma reesei. Also inhibited were total cellulase (Avicelase) and β-glucosidase (cellobiase) activities. The catalytic domain of CBH II, the second most abundant component of this cellulase, appeared less susceptible to inhibition by palladium. The inhibition was irreversible and could be prevented if histidine, cysteine or cystine was added to the enzyme reaction mixture simultaneously with the inhibitor. The binding of CBH I to microcrystalline cellulose (Avicel) was unaffected by palladium. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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