| Autor: |
Ono, Yasufumi, Enokiya, Atsushi, Masuko, Daisuke, Shoji, Kazuo, Yamanaka, Tateo |
| Předmět: |
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| Zdroj: |
Plant & Cell Physiology; Jan1999, Vol. 40 Issue 1, p47-52, 6p |
| Abstrakt: |
From the heterotrophic nitrifier Alcaligenes faecalis IFO 13111, an enzyme was purified which oxidized pyruvic oxime to nitrite. The molecular mass of the enzyme was 115 kDa and its molecule was composed of three molecules of subunits with the same molecular mass of 40 kDa. The enzyme contained 3 atoms of nonheme iron in the molecule and was active when the iron atoms were in a ferrous state. The enzyme consumed one mol of O2 to form one mol each of nitrite and pyruvate from one mol of pyruvic oxime. Therefore, the enzyme was thought to be a pyruvic oxime dioxygenase. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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