Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
Purification and biochemical characterization of some of the properties of recombinant human kynureninase.
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Recombinant human kynureninase was purified to homogeneity; the enzyme is highly specific for 3-hydroxykynurenine and is inhibited by L-kynurenine.
"This cloned enzyme was highly specific for 3-hydroxykynurenine"
Crystal structure of Homo sapiens kynureninase.
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Crystal structure of human kynureninase as the PLP-bound holoenzyme; the human constitutive enzyme preferentially cleaves 3-hydroxy-L-kynurenine.
"preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine"
Xanthurenic aciduria due to a mutation in KYNU encoding kynureninase.
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First molecular case of hydroxykynureninuria: a homozygous KYNU T198A variant with reduced kynureninase activity and massive urinary kynurenine-pathway metabolites.
"Massive urinary excretion of xanthurenic acid, 3-hydroxykynurenine and kynurenine"
High-performance liquid chromatographic assay of human lymphocyte kynureninase activity levels.
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Human lymphocyte kynureninase activity is depressed in vitamin-B6-deficient men relative to B6-replete men, reflecting PLP cofactor dependence.
"lymphocyte kynureninase activity is depressed during a vitamin B6 deficiency"
NAD Deficiency, Congenital Malformations, and Niacin Supplementation.
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Biallelic loss-of-function KYNU (and HAAO) variants disrupt de novo NAD synthesis, causing reduced circulating NAD and a congenital malformation syndrome (VCRL2); niacin supplementation prevents defects in mice.
"The patients had reduced levels of circulating NAD."
Intracellular localization and characterization of 3-hydroxykynureninase in human liver.
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3-hydroxykynureninase in human liver was found in both cytosol and mitochondria with identical properties; active on 3-hydroxykynurenine and kynurenine (~15:1) and PLP-dependent.
"3-hydroxykynureninase in human liver was present in cytosol and mitochondria."
Isolation and expression of a cDNA clone encoding human kynureninase.
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Cloning and expression of human kynureninase, a PLP-dependent enzyme that cleaves L-kynurenine and L-3-hydroxykynurenine; Lys276 binds the cofactor.
"catalyses the cleavage of L-kynurenine and L-3-hydroxykynurenine into anthranilic and 3-hydroxyanthranilic acids"
Cloning and recombinant expression of rat and human kynureninase.
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Cloning and recombinant expression of human (and rat) kynureninase with measured Km values; kynureninase acts in NAD cofactor biosynthesis from tryptophan.
"A cDNA encoding human liver kynureninase was also isolated."
Different kynurenine pathway enzymes limit quinolinic acid formation by various human cell types.
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Kynureninase activity (with kynurenine 3-hydroxylase and 3-HAO) is a cell-type determinant of quinolinate production, and is high in interferon-gamma-stimulated cells.
"Kynurenine 3-hydroxylase and, in some cells, kynureninase and 3-hydroxyanthranilate 3,4-dioxygenase are important determinants of whether a cell can make quinolinate."
3-hydroxykynurenine + H2O => 3-hydroxyanthranilate + alanine + H+