| Autor: |
Nishimura, Atsuo, Yoshizako, Fumiki, Chubachi, Mitsuo |
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry; January 1997, Vol. 61 Issue: 9 p1527-1530, 4p |
| Abstrakt: |
The aspergillic acid degrading enzyme (ADE) that catalyzes the cleavage of the pyrazine ring in aspergillic acid (AA, l-hydroxy-3-isobutyl-6-sec-butyl-2-pyrazinone) was purified to electrophoretic homogeneity from extracts of Trichoderma koningiiATCC 76666. ADE was a homodimeric protein with a molecular mass of 112kDa, contained lmol of FAD per mol of subunit, and required NAD(P)H and molecular oxygen for its activity. ADE had an isoelectric point of around 5.3, and an optimum pH of 7.0–8.0. p-Chloromercuribenzoate and HgCl2completely inhibited ADE activity, while metal chelating reagents, α, α′-dipyridyl and o-phenanthroline, were not inhibitors. The substrate specificity among AA-related compounds was that hydroxyaspergillic acid was a poor substrate (16% of the activity for AA) and deoxyaspergillic acid did not serve as a substrate. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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