Date published: 2026-6-3

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kynureninase Substrates

Santa Cruz Biotechnology now offers a broad range of kynureninase Substrates for use in various applications. Kynureninase is a key enzyme in the kynurenine pathway, which is the primary route for the catabolism of the amino acid tryptophan. This pathway leads to the production of several important metabolites, including nicotinamide adenine dinucleotide (NAD+), which is crucial for cellular energy production and various other cellular processes. Kynureninase specifically catalyzes the hydrolysis of kynurenine into anthranilic acid or 3-hydroxykynurenine into 3-hydroxyanthranilic acid, both of which are important intermediates in the pathway. Kynureninase Substrates are essential tools in scientific research, allowing researchers to study the enzyme's activity and its role in regulating the balance of metabolites within this pathway. By utilizing these substrates, scientists can explore how alterations in kynureninase activity impact the production of neuroactive and immune-regulating compounds, which have been implicated in various neurological disorders, immune responses, and even cancer. These substrates are widely used in biochemical assays to measure kynureninase activity, in studies aiming to understand the physiological and pathological roles of the kynurenine pathway, and in the development of potential scientific strategies targeting this metabolic route. The availability of these substrates has significantly advanced research in neurobiology, immunology, and metabolic studies, providing crucial insights into the complex interactions and regulatory mechanisms within the kynurenine pathway. View detailed information on our available kynureninase Substrates by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

L-Kynurenine

2922-83-0sc-202688
50 mg
$57.00
2
(1)

L-Kynurenine acts as a substrate for kynureninase, facilitating the conversion of kynurenine to kynurenic acid. Its unique structure allows for specific enzyme-substrate interactions, influencing the reaction kinetics and pathway dynamics. The compound exhibits distinct conformational flexibility, which may enhance its binding affinity to the active site of kynureninase. Additionally, L-Kynurenine's polar and non-polar regions contribute to its solubility profile, impacting its behavior in biological systems.