Disease relevance of BNA1

• Structure comparison with 3HAO from Ralstonia metallidurans reveals similarities at the active site and suggests the same catalytic mechanism in prokaryotic and eukaryotic 3HAO [1].

High impact information on BNA1

• Deletion of a gene in the de novo NAD(+) synthesis pathway BNA1 resulted in a significant rDNA silencing defect only on medium deficient in nicotinic acid, an NAD(+) precursor [2].
• 3-Hydroxyanthranilic acid 3,4-dioxygenase (3HAO) is a non-heme ferrous extradiol dioxygenase in the kynurenine pathway from tryptophan [1].

Biological context of BNA1

• Based on the model of the substrate HAA at the active site of Y3HAO, we propose a mechanism of catalysis for 3HAO [1].

Analytical, diagnostic and therapeutic context of BNA1

• By immunofluorescence microscopy, Myc-tagged Bna1p was localized throughout the whole cell in an asynchronously growing population [2].

References