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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Kynureninase

kynureninase, L-kynurenine hydrolase
Kynureninase is a pyridoxal-5'-phosphate (pyridoxal-P) dependent enzyme that catalyzes the cleavage of L-kynurenine and L-3-hydroxykynurenine into anthranilic and 3-hydroxyanthranilic acids, respectively. Kynureninase is involved in the biosynthesis of NAD cofactors from tryptophan through the kynurenine pathway. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2010] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, Indo, tryptophan 2,3-dioxygenase
Papers on kynureninase
Chemical inhibition of kynureninase reduces Pseudomonas aeruginosa quorum sensing and virulence factor expression.
New
Cady et al., In Acs Chem Biol, Feb 2016
Finally, it was shown that S-phenyl-L-cysteine sulfoxide competitively inhibits P. aeruginosa kynureninase (KynU) activity in vitro and reduces PQS production in vivo.
Elevation of Kynurenine Metabolites in Rat Liver and Serum: A Potential Additional Mechanism of the Alcohol Aversive and Anti-cancer Effects of Disulfiram?
New
Bano et al., Karāchi, Pakistan. In Alcohol Alcohol, Jan 2016
RESULTS: DS increased liver and serum [3-HK] and [3-HAA] possibly by increasing the flux of tryptophan down the hepatic kynurenine pathway and activation of kynurenine hydroxylase and kynureninase.
The tryptophan metabolism enzyme L-kynureninase is a novel inflammatory factor in psoriasis and other inflammatory diseases.
New
Lowes et al., New York City, United States. In J Allergy Clin Immunol, Jan 2016
However, in patients with chronic inflammatory skin disease, such as psoriasis and atopic dermatitis (AD), another tryptophan metabolism enzyme downstream of IDO, L-kynureninase (KYNU), is heavily upregulated.
The kynurenine pathway is activated in human obesity and shifted toward kynurenine monooxygenase activation.
New
Poulain-Godefroy et al., Lille, France. In Obesity (silver Spring), Oct 2015
The expression of several KP enzyme genes (indoleamine 2,3-dioxygenase 1 [IDO1], kynureninase [KYNU], kynurenine 3-monooxygenase [KMO], and kynurenine aminotransferase III [CCBL2]) was increased in the omental adipose tissue of women with obesity compared to lean (P < 0.05), and their expression was induced by proinflammatory cytokines in human primary adipocytes (P < 0.05), except for KMO that is not expressed in these cells.
Chemistry and diversity of pyridoxal-5'-phosphate dependent enzymes.
Review
New
Phillips, Athens, United States. In Biochim Biophys Acta, Sep 2015
The reaction mechanisms of two PLP-dependent enzymes are discussed, kynureninase and tyrosine phenol-lyase (TPL).
Effects of persistent organochlorine exposure on the liver transcriptome of the common minke whale (Balaenoptera acutorostrata) from the North Pacific.
Iwata et al., Japan. In Ecotoxicol Environ Saf, 2014
In addition, a negative correlation between kynureninase and PCB169 levels was also observed, which suggest an enhanced accumulation of an endogenous aryl hydrocarbon receptor agonist, kynurenine in the minke whale population.
Enhanced antibody responses to an HIV-1 membrane-proximal external region antigen in mice reconstituted with cultured lymphocytes.
Kelsoe et al., Durham, United States. In J Immunol, 2014
We have shown that the protective HIV-1 Ab, 2F5, avidly reacts with a conserved mammalian self-Ag, kynureninase, and that the development of B cells specific for the 2F5 epitope is constrained by immunological tolerance.
Structure and mechanism of kynureninase.
Review
Phillips, Athens, United States. In Arch Biochem Biophys, 2014
In this pathway, kynureninase catalyzes the hydrolysis of l-kynurenine (in bacteria) or 3-hydroxy-l-kynurenine (in eukaryotes) to give anthranilic acid or 3-hydroxyanthranilic acid, respectively, and l-alanine.
The phosphate of pyridoxal-5'-phosphate is an acid/base catalyst in the mechanism of Pseudomonas fluorescens kynureninase.
Barron et al., Athens, United States. In Febs J, 2014
Kynureninase (L-kynurenine hydrolase, EC 3.7.1.3)
Involvement of the kynurenine pathway in human glioma pathophysiology.
Guillemin et al., Sydney, Australia. In Plos One, 2013
Our data revealed that interferon-gamma (IFN-γ) stimulation significantly potentiated the expression of the KP enzymes, IDO-1 IDO-2, kynureninase (KYNU), kynurenine hydroxylase (KMO) and significantly down-regulated 2-amino-3-carboxymuconate semialdehyde decarboxylase (ACMSD) and kynurenine aminotransferase-I (KAT-I) expression in cultured human glioma cells.
The urinary ratio of 3-hydroxykynurenine/3-hydroxyanthranilic acid is an index to predicting the adverse effects of D-tryptophan in rats.
Fukuwatari et al., Japan. In J Nutr Sci Vitaminol (tokyo), 2013
The reaction 3-hydroxykynurenine→3-hydroxyanthranilic acid is catalyzed by the pyridoxal phosphate-dependent enzyme kynureninase.
Urine 3-hydroxykynurenine is higher during the postovulatory phase than in the preovulatory phase indicating a higher vitamin B6 requirement.
Shibata, Japan. In Biosci Biotechnol Biochem, 2013
This increase in 3-hydroxykynurenine suggests a decreased reaction of 3-hydroxykynurenine → 3-hydroxyanthranilic acid catalyzed by kynureninase, a vitamin B6 enzyme.
A rare variant at the KYNU gene is associated with kynureninase activity and essential hypertension in the Han Chinese population.
GeneRIF
Zhu et al., Shanghai, China. In Circ Cardiovasc Genet, 2011
A rare variant at the KYNU gene is associated with essential hypertension in the Han Chinese population.
Structure, mechanism, and substrate specificity of kynureninase.
Review
Phillips, Athens, United States. In Biochim Biophys Acta, 2011
The kynurenine pathway is the major route for tryptophan catabolism in animals and some fungi and bacteria.
[A polymorphism of kynureninase gene in a hypertensive candidate chromosomal region is associated with essential hypertension].
GeneRIF
Zhu et al., Shanghai, China. In Zhonghua Xin Xue Guan Bing Za Zhi, 2005
The Lys412Glu polymorphism of the KYNU gene in a hypertensive candidate chromosomal region is associated with essential hypertension in Han Chinese.
Gene expression of enzymes for tryptophan degradation pathway is upregulated in the skin lesions of patients with atopic dermatitis or psoriasis.
GeneRIF
Ra et al., Ibaraki, Japan. In J Dermatol Sci, 2004
Levels of mRNA for IDO (indoleamine 2,3-dioxygenase) and kynureninase, enzymes constituting the tryptophan degradation pathway, were found to be upregulated in the skin lesions of atopic dermatitis or psoriasis
Expression of kynurenine aminotransferase in the subplate of the rat and its possible role in the regulation of programmed cell death.
GeneRIF
Vécsei et al., Szeged, Hungary. In Cereb Cortex, 2002
Kynurenine aminotransferase is expressed in the neurons of the transient subplate zone during prenatal development of the cerebral cortex and may play a role in regulating programmed neuronal cell death.
A missense mutation in kynurenine aminotransferase-1 in spontaneously hypertensive rats.
GeneRIF
Kapoor et al., Sydney, Australia. In J Biol Chem, 2002
Spontaneously hypertensive rats have a missense mutation in KAT-1
[Enzymes of the kynurenine pathway].
Review
Buczko et al., In Postepy Hig Med Dosw, 2000
In this review, the role of kynurenine pathway enzymes (tryptophan 2,3-dioxygenase, indoleamine 2,3-dioxygenase, formamidase, kynurenine aminotransferase, kynurenine 3-hydroxylase, kynureninase, 3-hydroxyanthranilic acid oxygenase, picolinic carboxylase, quinolinic acid phosphoribosyltransferase) in the synthesis of tryptophan products degradation was described.
Regulation of quinolinic acid synthesis by mitochondria and o-methoxybenzoylalanine.
Review
Moroni et al., Florence, Italy. In Adv Exp Med Biol, 1998
o-Methoxybenzoylalanine, a selective kynureninase inhibitor, caused unexpected accumulation of 3-hydroxyanthranilic acid (3OH-ANA), the product of kynureninase activity and the precursor of quinolinic acid (QUIN) in liver homogenates incubated with 3OH-kynurenine (3OH-KYN).
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