Succinate Oxidase in Neurospora

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The L-amino acid oxidase of Neurospora.

In 1944 one of us described a n-amino acid oxidase in extracts of Neurospora crassa (1). Except for slight activity against L-glutamate, no oxidation of L-amino acids was observed. Recently a means for inducing the formation of a soluble L-amino acid oxidase by the mold was reported by Bender, Krebs, and Hor0wit.z (2). This is accomplished by reducing the biotin content of the basal medium (3) ...

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Mutants of Neurospora deficient in D-amino acid oxidase.

Although many investigations have been carried out on the n-amino acid oxidase since its discovery in 1935 (2)) the metabolic role of this enzyme remains somewhat obscure. It is generally believed, on the basis of indirect evidence, that in animals the enzyme functions in the inversion of exogenous n-amino acids over the pathway n-amino acid --+ Lu-keto acid -+ L-amino acid (3). The first step ...

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Proceedings: Precursors of cytochrome oxidase in cytochrome-oxidase deficient cells of Neurospora crassa.

Three different cell types of Neurospora crussa deficient in cytochrome oxidase were studied : the nuclear mutant cni-1, the cytoplasmic mutant mi-1 and copper-depleted wild-type cells. 1. The enzyme-deficient cells have retained a functioning mitochondrial protein synthesis. It accounted for 1216 % of the total protein synthesis of the cell. However, the analysis of mitochondrial translation p...

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Reconstitution of Sue&ate-Coenzyme Q Reductase (Complex II) and Succinate Oxidase Activities by a Highly Purified, Reactivated Succinate Dehydrogenase*

Succinate dehydrogenase has been isolated in a highly purified form from succinate-coenzyme Q reductase preparations. The enzyme contains 1 mole of covalently bound flavin, 8 g atoms of iron, and 8 moles of acid-labile sulfide per 150,000 g of protein. It catalyzes succinate oxidation in the presence of phenazine methosulfate as electron acceptor at a rate of 26 to 32 pmoles per min X mg of pro...

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ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 1973

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.113.2.637-644.1973