Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase
نویسندگان
چکیده
منابع مشابه
Spectroscopic and Thermodynamic Characterization of Human 3-Hydroxyanthranilate-3,4-Dioxygenase
3-Hydroxyanthranilate-3,4-dioxygenase (HAO) is a non-heme iron dependent enzyme that catalyzes the oxidative ring opening of 3-hydroxyanthranilate (HAA) which is an intermediate in the kynurenine pathway and its ring opening is the final enzymatic step from tryptophan to quinolinic acid (QUIN). QUIN functions as an N-methyl-D-aspartate (NMDA) receptor agonist and elevated brain levels of QUIN h...
متن کاملCrystal structures of human 3-hydroxyanthranilate 3,4-dioxygenase with native and non-native metals bound in the active site.
3-Hydroxyanthranilate 3,4-dioxygenase (3HAO) is an enzyme in the microglial branch of the kynurenine pathway of tryptophan degradation. 3HAO is a non-heme iron-containing, ring-cleaving extradiol dioxygenase that catalyzes the addition of both atoms of O2 to the kynurenine pathway metabolite 3-hydroxyanthranilic acid (3-HANA) to form quinolinic acid (QUIN). QUIN is a highly potent excitotoxin t...
متن کاملPurification and properties of 3-hydroxyanthranilate oxygenase from beef kidney.
1. Beef kidney 3-hydroxyanthranilate oxygenase was purified in the inactive form, free of bound ferrous ion. Its properties are very similar to those of the liver enzyme. 2. The enzyme in the early stages of purification could be activated by acidification to about pH 4 in the presence of ferrous salts. For the most purified preparations, a sulfhydryl compound, as well as acid and iron, was req...
متن کامل3 , 4 = Dioxygenase III
In the early stage of the reaction of protocatechuate 3,4dioxygenase, a new spectral species of the enzyme having a broad absorption band with a maximum between 500 and 520 nm was observed by using a stopped flow technique. The observed spectrum was distinct from those of the enzyme or the enzyme-protoacatechuic acid complex and its formation was absolutely dependent on the simultaneous presenc...
متن کاملStructural and functional studies of ferredoxin and oxygenase components of 3-nitrotoluene dioxygenase from Diaphorobacter sp. strain DS2
3-nitrotoluene dioxygenase (3NTDO) from Diaphorobacter sp. strain DS2 catalyses the conversion of 3-nitrotoluene (3NT) into a mixture of 3- and 4-methylcatechols with release of nitrite. We report here, X-ray crystal structures of oxygenase and ferredoxin components of 3NTDO at 2.9 Å and 2.4 Å, respectively. The residues responsible for nitrite release in 3NTDO were further probed by four singl...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 2005
ISSN: 0108-7673
DOI: 10.1107/s0108767305091282