Disease relevance of Kynu

• RESULTS: Levels of mRNA for IDO (indoleamine 2,3-dioxygenase) and kynureninase, enzymes constituting the tryptophan degradation pathway, were found to be upregulated in the skin lesions as compared to the uninvolved skin of patients with AD or psoriasis [1].

High impact information on Kynu

• In liver homogenates, however, this compound caused unexpected accumulation of 3-hydroxyanthranilic acid, the product of kynureninase activity and the precursor of quinolinic acid [2].
• The use of o-methoxybenzoylalanine, a selective kynureninase inhibitor, has been proposed with the aim of reducing brain synthesis of quinolinic acid, an excitotoxic tryptophan metabolite [2].
• It was notable that basal kynureninase activity was much higher in MT2 macrophages than in N11 microglial cells [3].
• Kynurenine disposition in blood and brain of mice: effects of selective inhibitors of kynurenine hydroxylase and of kynureninase [4].
• This pathway is sensitive to reductions in vitamin B-6 availability because two key enzymes, kynurenine aminotransferase (KAT) and kynureninase (KYNase), require pyridoxal 5'-phosphate [5].

Associations of Kynu with chemical compounds

• After intraperitoneal injection of [14C]tryptophan, vitamin B6-deficient mice showed lower liberation of 14CO2 from [methylene-14C]tryptophan and [U-14C]tryptophan than did controls, indicating impairment of kynureninase (EC 3.7.1.3) activity [6].
• o-Methoxybenzoylalanine, a selective kynureninase inhibitor, caused unexpected accumulation of 3-hydroxyanthranilic acid (3OH-ANA), the product of kynureninase activity and the precursor of quinolinic acid (QUIN) in liver homogenates incubated with 3OH-kynurenine (3OH-KYN) [7].

Other interactions of Kynu

• Under these conditions the enzymatic activity of the kynureninase is decreased and the activity of the kynurenine aminotransferase as well as of the tryptophan pyrrolase is not altered [8].

References