Journal Article

Pyruvic Oxime Dioxygenase from the Heterotrophic Nitrifier <i>Alcaligenes faecalis</i>: Purification, and Molecular and Enzymatic Properties

Yasufumi Ono, Atsushi Enokiya, Daisuke Masuko, Kazuo Shoji and Tateo Yamanaka

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 40, issue 1, pages 47-52
Published in print January 1999 | ISSN: 0032-0781
Published online January 1999 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a029473
Pyruvic Oxime Dioxygenase from the Heterotrophic Nitrifier Alcaligenes faecalis: Purification, and Molecular and Enzymatic Properties

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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.

Keywords: Alcaligenes faecalis; Dioxygenase; Heterotrophic nitrifier; Nonheme iron; Pyruvic oxime

Journal Article.  0 words. 

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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