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Identification
HMDB Protein ID HMDBP02606
Secondary Accession Numbers
  • 8105
Name Kynurenine 3-monooxygenase
Synonyms
  1. Kynurenine 3-hydroxylase
Gene Name KMO
Protein Type Unknown
Biological Properties
General Function Involved in monooxygenase activity
Specific Function Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract.
Pathways
  • NAD(+) biosynthesis
  • Tryptophan Metabolism
  • Tryptophan metabolism
Reactions
L-Kynurenine + NADPH + Oxygen → L-3-Hydroxykynurenine + NADP + Water details
L-Kynurenine + Oxygen + NADPH + Hydrogen Ion → L-3-Hydroxykynurenine + NADP + Water details
GO Classification
Biological Process
NAD biosynthetic process
tryptophan catabolic process
kynurenine metabolic process
response to salt stress
tryptophan catabolic process to kynurenine
Cellular Component
cytosol
mitochondrial outer membrane
integral to membrane
mitochondrial inner membrane
Function
catalytic activity
monooxygenase activity
oxidoreductase activity
Molecular Function
kynurenine 3-monooxygenase activity
NAD(P)H oxidase activity
flavin adenine dinucleotide binding
Process
metabolic process
oxidation reduction
Cellular Location
  1. Multi-pass membrane protein
  2. Mitochondrion outer membrane
Gene Properties
Chromosome Location 1
Locus 1q42-q44
SNPs KMO
Gene Sequence
>1461 bp
ATGGACTCATCTGTCATTCAAAGGAAAAAAGTAGCTGTCATTGGTGGTGGCTTGGTTGGC
TCATTACAAGCATGCTTTCTTGCAAAGAGGAATTTCCAGATTGATGTATATGAAGCTAGG
GAAGATACTCGAGTGGCTACCTTCACACGTGGAAGAAGCATTAACTTAGCCCTTTCTCAT
AGAGGACGACAAGCCTTGAAAGCTGTTGGCCTGGAAGATCAGATTGTATCCCAAGGTATT
CCCATGAGAGCAAGAATGATCCACTCTCTTTCAGGAAAAAAGTCTGCAATTCCCTATGGG
ACAAAGTCTCAGTATATTCTTTCTGTAAGCAGAGAAAATCTAAACAAGGATCTATTGACT
GCTGCTGAGAAATACCCCAATGTGAAAATGCACTTTAACCACAGGCTGTTGAAATGTAAT
CCAGAGGAAGGAATGATCACAGTGCTTGGATCTGACAAAGTTCCCAAAGATGTCACTTGT
GACCTCATTGTAGGATGTGATGGAGCCTATTCAACTGTCAGATCTCACCTGATGAAGAAA
CCTCGCTTTGATTACAGTCAGCAGTACATTCCTCATGGGTACATGGAGTTGACTATTCCA
CCTAAGAACGGAGATTATGCCATGGAACCTAATTATCTGCATATTTGGCCTAGAAATACC
TTTATGATGATTGCACTTCCTAACATGAACAAATCATTCACATGTACTTTGTTCATGCCC
TTTGAAGAGTTTGAAAAACTTCTAACCAGTAATGATGTGGTAGATTTCTTCCAGAAATAC
TTTCCGGATGCCATCCCTCTAATTGGAGAGAAACTCCTAGTGCAAGATTTCTTCCTGTTG
CCTGCCCAGCCCATGATATCTGTAAAGTGCTCTTCATTTCACTTTAAATCTCACTGTGTA
CTGCTGGGAGATGCAGCTCATGCTATAGTGCCGTTTTTTGGGCAAGGAATGAATGCGGGC
TTTGAAGACTGCTTGGTATTTGATGAGTTAATGGATAAATTCAGTAACGACCTTAGTTTG
TGTCTTCCTGTGTTCTCAAGATTGAGAATCCCAGATGATCACGCGATTTCAGACCTATCC
ATGTACAATTACATAGAGATGCGAGCACATGTCAACTCAAGCTGGTTCATTTTTCAGAAG
AACATGGAGAGATTTCTTCATGCGATTATGCCATCGACCTTTATCCCTCTCTATACAATG
GTCACTTTTTCCAGAATAAGATACCATGAGGCTGTGCAGCGTTGGCATTGGCAAAAAAAG
GTGATAAACAAAGGACTCTTTTTCTTGGGATCACTGATAGCCATCAGCAGTACCTACCTA
CTTATACACTACATGTCACCACGATCTTTCCTCTGCTTGAGAAGACCATGGAACTGGATA
GCTCACTTCCGGAATACAACATGTTTCCCCGCAAAGGCCGTGGACTCCCTAGAACAAATT
TCCAATCTCATTAGCAGGTGA
Protein Properties
Number of Residues 486
Molecular Weight 55809.445
Theoretical pI 9.032
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Kynurenine 3-monooxygenase
MDSSVIQRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATFTRGRSINLALSH
RGRQALKAVGLEDQIVSQGIPMRARMIHSLSGKKSAIPYGTKSQYILSVSRENLNKDLLT
AAEKYPNVKMHFNHRLLKCNPEEGMITVLGSDKVPKDVTCDLIVGCDGAYSTVRSHLMKK
PRFDYSQQYIPHGYMELTIPPKNGDYAMEPNYLHIWPRNTFMMIALPNMNKSFTCTLFMP
FEEFEKLLTSNDVVDFFQKYFPDAIPLIGEKLLVQDFFLLPAQPMISVKCSSFHFKSHCV
LLGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFSNDLSLCLPVFSRLRIPDDHAISDLS
MYNYIEMRAHVNSSWFIFQKNMERFLHAIMPSTFIPLYTMVTFSRIRYHEAVQRWHWQKK
VINKGLFFLGSLIAISSTYLLIHYMSPRSFLRLRRPWNWIAHFRNTTCFPAKAVDSLEQI
SNLISR
GenBank ID Protein 2239124
UniProtKB/Swiss-Prot ID O15229
UniProtKB/Swiss-Prot Entry Name KMO_HUMAN
PDB IDs Not Available
GenBank Gene ID Y13153
GeneCard ID KMO
GenAtlas ID KMO
HGNC ID HGNC:6381
References
General References
  1. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  2. Alberati-Giani D, Cesura AM, Broger C, Warren WD, Rover S, Malherbe P: Cloning and functional expression of human kynurenine 3-monooxygenase. FEBS Lett. 1997 Jun 30;410(2-3):407-12. [PubMed:9237672 ]
  3. Breton J, Avanzi N, Magagnin S, Covini N, Magistrelli G, Cozzi L, Isacchi A: Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase. Eur J Biochem. 2000 Feb;267(4):1092-9. [PubMed:10672018 ]
  4. Stone TW, Darlington LG: Endogenous kynurenines as targets for drug discovery and development. Nat Rev Drug Discov. 2002 Aug;1(8):609-20. [PubMed:12402501 ]