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Literature summary for 1.14.13.9 extracted from

  • Zheng, X.; Zhang, A.; Binnie, M.; McGuire, K.; Webster, S.P.; Hughes, J.; Howie, S.E.M.; Mole, D.J.
    Kynurenine 3-monooxygenase is a critical regulator of renal ischemia-reperfusion injury (2019), Exp. Mol. Med., 51, 1-14 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.9

Application

Application Comment Organism
medicine rationale for enzyme KMO inhibition as a therapeutic strategy to protect against acute kidney injury (AKI) during critical illness. Renal ischemia-reperfusion injury (IRI) is a leading cause of acute kidney injury (AKI) Mus musculus

Cloned(Commentary)

Cloned (Comment) Organism
gene kmo, quantitative real-time PCR enzyme expression analysis Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information generation of enzyme knockout mutant mice, which are engineered on a C57BL/6 background to lack KMO activity by insertion of a polyA transcription stop motif before exon 5 of the Kmo gene (Kmotm1a(KOMP)Wtsi). Kmonull mice are unable to form 3-hydroxykynurenine. Kmonull mice are protected against AKI after renal ischemia-reperfusion injury (IRI). KMO deletion inhibits neutrophil infiltration in the kidney following IRI. Mutant mouse phenotype, detailed overview Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial outer membrane
-
 Mus musculus 5741
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-kynurenine + NADPH + H+ + O2 Mus musculus
-
 3-hydroxy-L-kynurenine + NADP+ + H2O
-
 ?
L-kynurenine + NADPH + H+ + O2 Mus musculus C57BL/6N x C57BL/6J
-
 3-hydroxy-L-kynurenine + NADP+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q91WN4
-
-
Mus musculus C57BL/6N x C57BL/6J Q91WN4
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney high enzyme expression level Mus musculus
-
liver
-
 Mus musculus
-
renal proximal tubule epithelial cell
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-kynurenine + NADPH + H+ + O2
-
 Mus musculus 3-hydroxy-L-kynurenine + NADP+ + H2O
-
 ?
L-kynurenine + NADPH + H+ + O2
-
 Mus musculus C57BL/6N x C57BL/6J 3-hydroxy-L-kynurenine + NADP+ + H2O
-
 ?

Synonyms

Synonyms Comment Organism
KMO
-
 Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Mus musculus

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Mus musculus
NADPH
-
 Mus musculus

General Information

General Information Comment Organism
malfunction Kmonull mice are unable to form 3-hydroxykynurenine and have preserved renal function, reduced renal tubular cell injury, and fewer infiltrating neutrophils compared with wild-type (Kmowt) control mice. Tubular epithelial cell apoptosis is reduced in the kidney of Kmonull mice following IRI Mus musculus
metabolism the enzyme is involved in the kynurenine pathway of tryptophan metabolism. The conversion of tryptophan to N-formylkynurenine (KYN) is catalyzed by tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenases (IDOs). The kynurenine pathway diverges at kynurenine into two distinct branches that are regulated by kynurenine aminotransferases (KATs) and kynurenine 3-monooxygenase (KMO), respectively Mus musculus
physiological function kynurenine 3-monooxygenase is a critical regulator of renal ischemia-reperfusion injury. Flux through KMO contributes to acute kidney injury (AKI) after ischemia-reperfusion injury (IRI), and supports the rationale for KMO inhibition as a therapeutic strategy to protect against AKI during critical illness. KMO is the gate-keeper enzyme. Kynurenine pathway metabolite concentrations in plasma and kidney tissue after ischemia-reperfusion injury (IRI), overview Mus musculus