Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase.
نویسندگان
چکیده
منابع مشابه
3-hydroxyanthranilic Acid Metabolism
The participation of 3-hydroxyanthranilic acid as an intermediate in the biosynthesis of nicotinic acid from tryptophan was first demonstrated in certain mutant strains of Neurospora in 1948 by Bonner (1) and by Mitchell and Nyc (2). In addition, Mitchell et al. (3) found that 3-hydroxyanthranilic acid can replace nicotinic acid in the nutrition of the rat. In 1946 Singal et al. (4) noted a sub...
متن کاملEnzymatic conversion of 3-hydroxyanthranilic acid to nicotinic acid.
The apparent conversion of tryptophan to nicotinic acid has been observed for several animal species (cf. (1)). Other studies demonstrated that at least some of the nicotinic acid (or amide) was synthesized within the tissues of the animal (2, 3). It was of interest to extend these studies and the ability of liver slices to synthesize nicotinic acid from its biologically active intermediate, 3-...
متن کاملStudies on purified 3-hydroxyanthranilic acid oxidase.
3-Hydroxyanthranilic acid oxidase is known to cat,alyze the oxidation of 3-hydroxyanthranilic acid to a very unstable aliphatic compound, which may either be spontaneously transformed into quinolinic acid or undergo enzymic conversion to picolinic or nicotinic acid, or both (l-3). According to Mason (4), this enzyme has been classified as an “oxygen transferase,” since the oxygen consumed, 1 mo...
متن کاملBeef liver 3-hydroxyanthranilic acid oxidase.
The oxidation of 3-hydroxyanthranilic acid, an intermediate in the conversion of tryptophan to niacin (l-3), is catalyzed by a liver oxidase (4). The first recognized product, termed Compound I (5), yields quinolinic acid spontaneously or picolinic acid under the influence of a liver carboxylase (6). The intermediate is detectable by its absorption maximum at 360 rnp (4). Wiss and Bettendorf (7...
متن کاملBeef Kidney 3-Hydroxyanthranilic Acid Oxygenase
Beef kidney 3-hydroxyanthranilic acid oxygenase has been purified to homogeneity. It is a single subunit protein of M, = 34,000 * 2,000 with a frictional coefficient (f/iO) of about 1.1. The enzyme readily aggregates to form, apparently inactive, higher molecular weight oligomers. The very rapid loss of enzyme activity during the assay was analyzed extensively. It was found to be due to inactiv...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1994
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)36717-0