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Kynurenin-3-Monooxygenase: the pathway in the body

Kynurenin-3-Monooxygenase is part of the pathway “Kynurenine pathway”. This page shows the whole pathway; the station of Kynurenin-3-Monooxygenase is highlighted.

Where this laboratory value sits: Kynurenine — first intermediate. The enzymes IDO and TDO open the ring of tryptophan; kynurenine forms via a short-lived intermediate. The kynurenine-to-tryptophan ratio describes how active this step currently is. Source 1, 2

In brief

The kynurenine pathway is the main breakdown route of the amino acid tryptophan and includes kynurenine, kynurenic acid, 3-hydroxykynurenine and quinolinic acid. It opens the ring of tryptophan and ultimately yields NAD⁺.

9 stations · 5 sources
ORYMain routeSide routesIDO, TDOHaem (iron)OxygenKMOFADNADPHKynureninaseVitamin B6 (PLP)3-HAOIronQPRTPRPPvia KAT, with vitamin B6via KAT, with vitamin B6via ACMS and ACMSDInterferon-γTryptophanamino acid from foodKynureninefirst intermediate3-Hydroxykynureninehydroxylated form3-OH-anthranilic acidnext stageQuinolinic acidalso called quinolinateNAD⁺coenzyme of metabolismKynurenic acidside productXanthurenic acidfrom 3-hydroxykynureninePicolinic acidbranch via ACMS

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The pathway step by step

  1. Tryptophan → Kynurenine IDO, TDO · Haem (iron), Oxygen The enzymes IDO and TDO open the ring of tryptophan; kynurenine forms via a short-lived intermediate. The kynurenine-to-tryptophan ratio describes how active this step currently is. Source 1, 2
  2. Kynurenine → 3-Hydroxykynurenine KMO · FAD, NADPH Kynurenine 3-monooxygenase (KMO) attaches an OH group to kynurenine. The enzyme sits in the outer membrane of the mitochondria and works with FAD and NADPH. Source 3, 1
  3. 3-Hydroxykynurenine → 3-OH-anthranilic acid Kynureninase · Vitamin B6 (PLP) Kynureninase cleaves the side chain from 3-hydroxykynurenine, forming 3-hydroxyanthranilic acid. This enzyme also works with pyridoxal phosphate, the active form of vitamin B6. Source 1
  4. 3-OH-anthranilic acid → Quinolinic acid 3-HAO · Iron An iron-containing enzyme opens the ring; the intermediate ACMS rearranges spontaneously into quinolinic acid. In the nervous system, quinolinic acid binds to NMDA receptors. Source 1
  5. Quinolinic acid → NAD⁺ QPRT · PRPP The enzyme QPRT converts quinolinic acid further; NAD⁺ forms over two steps. This route from tryptophan provides NAD⁺ in addition to the route that starts from niacin (vitamin B3). Source 4, 1

Cofactors in this pathway

What acts on this pathway

Sources

  1. Badawy AA. Kynurenine Pathway of Tryptophan Metabolism: Regulatory and Functional Aspects. Int J Tryptophan Res 2017 · PubMed 28469468
  2. King NJ, Thomas SR. Molecules in focus: indoleamine 2,3-dioxygenase. Int J Biochem Cell Biol 2007 · PubMed 17320464
  3. Smith JR, Jamie JF, Guillemin GJ. Kynurenine-3-monooxygenase: a review of structure, mechanism, and inhibitors. Drug Discov Today 2016 · PubMed 26589832
  4. Magni G, Amici A, Emanuelli M et al. Enzymology of NAD+ synthesis. Adv Enzymol Relat Areas Mol Biol 1999 · PubMed 10218108
  5. Rossi F, Miggiano R, Ferraris DM et al. The Synthesis of Kynurenic Acid in Mammals: An Updated Kynurenine Aminotransferase Structural KATalogue. Front Mol Biosci 2019 · PubMed 30873412

Whole pathway: Kynurenine pathway

Related pathways

As of 2026-09-16. Draft written by Claude to schema v2; sources checked in PubMed; expert review pending
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