kynurenine 3-monooxygenase

キヌレニン-3-モノオキシゲナーゼ

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/06/19 03:29:21」(JST)

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kynurenine 3-monooxygenase
Identifiers
EC number	1.14.13.9
CAS number	9029-61-2
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, a kynurenine 3-monooxygenase (EC 1.14.13.9) is an enzyme that catalyzes the chemical reaction

L-kynurenine + NADPH + H⁺ + O₂ 3-hydroxy-L-kynurenine + NADP⁺ + H₂O

The 4 substrates of this enzyme are L-kynurenine, NADPH, H⁺, and O₂, whereas its 3 products are 3-hydroxy-L-kynurenine, NADP⁺, and H₂O.

This enzyme belongs to the family of oxidoreductases, to be specific, those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is L-kynurenine,NADPH:oxygen oxidoreductase (3-hydroxylating). Other names in common use include kynurenine 3-hydroxylase, kynurenine hydroxylase, and L-kynurenine-3-hydroxylase. This enzyme participates in tryptophan metabolism. It employs one cofactor, FAD.

References

• Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM (2006). "A proteomic analysis of arsenical drug resistance in Trypanosoma brucei". Proteomics. 6 (9): 2726–32. doi:10.1002/pmic.200500419. PMID 16526094. 
• Okamoto H, Hayaishi O (1967). "Flavin adenine dinucleotide requirement for kynurenine hydroxylase of rat liver mitochondria". Biochem. Biophys. Res. Commun. 29 (3): 394–9. doi:10.1016/0006-291X(67)90469-X. PMID 6076241. 
• SAITO Y, HAYAISHI O, ROTHBERG S (1957). "Studies on oxygenases; enzymatic formation of 3-hydroxy-L-kynurenine from L-kynurenine". J. Biol. Chem. 229 (2): 921–34. PMID 13502353. 

UpToDate Contents

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English Journal

• Kynurenine-3-monooxygenase: a review of structure, mechanism, and inhibitors.

• Smith JR1, Jamie JF2, Guillemin GJ3.
• Drug discovery today.Drug Discov Today.2015 Nov 14. pii: S1359-6446(15)00420-1. doi: 10.1016/j.drudis.2015.11.001. [Epub ahead of print]
• Kynurenine monooxygenase (KMO) is an enzyme of the kynurenine (Kyn) pathway (KP), which is the major catabolic route of tryptophan. Kyn represents a branch point of the KP, being converted into the neurotoxin 3-hydroxykynurenine via KMO, neuroprotectant kynurenic acid, and anthranilic acid. As a res
• PMID 26589832

• Pharmacological kynurenine 3-monooxygenase enzyme inhibition significantly reduces neuropathic pain in a rat model.

• Rojewska E1, Piotrowska A1, Makuch W1, Przewlocka B1, Mika J2.
• Neuropharmacology.Neuropharmacology.2015 Oct 31;102:80-91. doi: 10.1016/j.neuropharm.2015.10.040. [Epub ahead of print]
• Recent studies have highlighted the involvement of the kynurenine pathway in the pathology of neurodegenerative diseases, but the role of this system in neuropathic pain requires further extensive research. Therefore, the aim of our study was to examine the role of kynurenine 3-monooxygenase (Kmo),
• PMID 26524415

• Development of a Surface Plasmon Resonance Assay for the Characterization of Small-Molecule Binding Kinetics and Mechanism of Binding to Kynurenine 3-Monooxygenase.

• Poda SB1, Kobayashi M2, Nachane R2, Menon V1, Gandhi AS1, Budac DP1, Li G3, Campbell BM1, Tagmose L3.
• Assay and drug development technologies.Assay Drug Dev Technol.2015 Oct;13(8):466-75. doi: 10.1089/adt.2015.649. Epub 2015 Aug 20.
• Kynurenine 3-monooxygenase (KMO), a pivotal enzyme in the kynurenine pathway, was identified as a potential therapeutic target for treating neurodegenerative and psychiatric disorders. In this article, we describe a surface plasmon resonance (SPR) assay that delivers both kinetics and the mechanism
• PMID 26292018

Japanese Journal

• Dual role of the carboxyl-terminal region of pig liver L-kynurenine 3-monooxygenase : mitochondrial-targeting signal and enzymatic activity

• Hirai Kumiko,Kuroyanagi Hidehito,Tatebayashi Yoshitaka [他],HAYASHI Yoshitaka,HIRABAYASHI TAKAHASHI Kanako,SAITO Kuniaki,HAGA Seiich,UEMURA Tomihiko,IZUMI Susumu
• The journal of biochemistry 148(6), 639-650, 2010-12-01
• NAID 10027879629

• L-Kynurenine 3-Monooxygenase from Mitochondrial Outer Membrane of Pig Liver: Purification, Some Properties, and Monoclonal Antibodies Directed to the Enzyme^1

• Uemura Tomihiko,Hirai Kumiko
• The journal of biochemistry 123(2), 253-262, 1998-02-01
• NAID 10005841593

• Cloning and functional expression of human kynurenine 3-monooxygenase

• ALBERATI-GIANI D.
• FEBS Letters 410, 407-412, 1997
• NAID 80009775089

Related Links

• Cell

詳細の表示を試みましたが、サイトのオーナーによって制限されているため表示できません。

• Kynurenine 3-monooxygenase inhibition in blood ameliorates ...

1. Cell. 2011 Jun 10;145(6):863-74. doi: 10.1016/j.cell.2011.05.020. Kynurenine 3-monooxygenase inhibition in blood ameliorates neurodegeneration. Zwilling D, Huang SY, Sathyasaikumar KV, Notarangelo FM, Guidetti P, Wu HQ ...

• Structural basis of kynurenine 3-monooxygenase inhibition

Inhibition of kynurenine 3-monooxygenase (KMO), an enzyme in the eukaryotic tryptophan catabolic pathway (i.e. kynurenine pathway), leads to amelioration of Huntington’s disease-relevant phenotypes in yeast, fruit fly, and mouse ...

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★リンクテーブル★

リンク元	「KMO」「キヌレニン3-モノオキシゲナーゼ」「キヌレニン-3-モノオキシゲナーゼ」
関連記事	「monooxygenases」「monooxygenase」

「KMO」

　　[★] キヌレニン3-モノオキシゲナーゼ kynurenine 3-monooxygenase

「キヌレニン3-モノオキシゲナーゼ」

　　[★]

英

kynurenine 3-monooxygenase, KMO

関

トリプトファン

「キヌレニン-3-モノオキシゲナーゼ」

　　[★]

英

kynurenine 3-monooxygenase

「monooxygenases」

　　[★]

関

See also Cytochrome P450 system

「monooxygenase」

　　[★] モノオキシゲナーゼ