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

Autor:	Yasufumi Ono, Atsushi Enokiya, Kazuo Shoji, Tateo Yamanaka, Daisuke Masuko
Rok vydání:	1999
Předmět:	chemistry.chemical_classification Alcaligenes faecalis Molecular mass biology Physiology Stereochemistry Cell Biology Plant Science General Medicine biology.organism_classification Ferrous chemistry.chemical_compound Enzyme Biochemistry chemistry Dioxygenase Mole Molecule Nitrite
Zdroj:	Plant and Cell Physiology. 40:47-52
ISSN:	1471-9053 0032-0781
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::1c7e460d95df8e25de38f62419a4a8a2 https://doi.org/10.1093/oxfordjournals.pcp.a029473 Zobrazit plný text záznamu Plný text ve formátu PDF