Kynurenine-3-Monooxygenase (KMO)

Kynurenine 3-Hydroxylase

SPN	O989
HGNC	6381
MGI	2138151
PubMed	23575632
RGD	620610
UniProt	O15229
Wiki	KMO

Kynurenine 3-monooxygenase (KMO; EC 1.14.13.9) is an NADPH-dependent flavin monooxygenase that catalyzes the hydroxylation of the L-tryptophan metabolite L-kynurenine to form L-3-hydroxykynurenine.

The predicted 486-amino acid human protein shares 47% sequence identity with Drosophila KMO. When expressed in mammalian cells, recombinant human KMO exhibited kinetic properties similar to those of the native human protein. Northern blot analysis revealed that human KMO is expressed as an approximately 2-kb mRNA in liver and placenta, and at lower levels in kidney.Expression of a mutant huntingtin (HTT) fragment in yeast, as in neurons, results in the formation of inclusion bodies and confers cellular toxicity.

Reference

"Cloning and functional expression of human kynurenine 3-monooxygenase."
FEBS Lett. 410:407-412(1997) [PubMed] [Europe PMC] [Abstract].

"Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase."
Eur. J. Biochem. 267:1092-1099(2000) [PubMed] [Europe PMC] [Abstract]

Ref.2"Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase."
Eur. J. Biochem. 267:1092-1099(2000) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and biological annotation of human chromosome 1."
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]

"Endogenous kynurenines as targets for drug discovery and development."
Nat. Rev. Drug Discov. 1:609-620(2002) [PubMed] [Europe PMC] [Abstract]