Human Gene KYNU (ENST00000264170.9)
  Description: Homo sapiens kynureninase (KYNU), transcript variant 1, mRNA. (from RefSeq NM_003937)
RefSeq Summary (NM_003937): 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].
Gencode Transcript: ENST00000264170.9
Gencode Gene: ENSG00000115919.15
Transcript (Including UTRs)
   Position: hg38 chr2:142,877,664-143,055,833 Size: 178,170 Total Exon Count: 14 Strand: +
Coding Region
   Position: hg38 chr2:142,885,368-143,042,172 Size: 156,805 Coding Exon Count: 13 

Page IndexSequence and LinksUniProtKB CommentsMalaCardsCTDRNA-Seq Expression
Microarray ExpressionRNA StructureProtein StructureOther SpeciesGO AnnotationsmRNA Descriptions
PathwaysOther NamesMethods
Data last updated at UCSC: 2021-01-14 15:32:12

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr2:142,877,664-143,055,833)mRNA (may differ from genome)Protein (465 aa)
Gene SorterGenome BrowserOther Species FASTAGene interactionsTable SchemaBioGPS
CGAPEnsemblEntrez GeneExonPrimerGeneCardsHGNC
HPRDLynxMGIneXtProtOMIMPubMed
ReactomeUniProtKBWikipedia

-  Comments and Description Text from UniProtKB
  ID: KYNU_HUMAN
DESCRIPTION: RecName: Full=Kynureninase; EC=3.7.1.3; AltName: Full=L-kynurenine hydrolase;
FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.
CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L- alanine.
CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3- hydroxyanthranilate + L-alanine.
COFACTOR: Pyridoxal phosphate.
ENZYME REGULATION: Inhibited by o-methoxybenzoylalanine (OMBA).
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=493 uM for L-kynurenine (at pH 7.0); KM=28.3 uM for DL-3-hydroxykynurenine (at pH 7.0); KM=3.0 uM for DL-3-hydroxykynurenine (at pH 7.9); pH dependence: Optimum pH is 8.25 with DL-3-hydroxykynurenine as substrate;
PATHWAY: Amino-acid degradation; L-kynurenine degradation; L- alanine and anthranilate from L-kynurenine: step 1/1.
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Expressed in all tissues tested (heart, brain placenta, lung, liver, skeletal muscle, kidney and pancreas). Highest levels found in placenta, liver and lung. Expressed in all brain regions.
INDUCTION: Increased levels in several cerebral and systemic inflammatory conditions.
MASS SPECTROMETRY: Mass=52400; Method=MALDI; Range=1-465; Note=The reported mass is given to only three significant figures; Source=PubMed:11985583;
DISEASE: Note=Xanthurenic aciduria manifesting as massive urinary excretion of large amounts of kynurenine, 3-hydroxykynurenine and xanthurenic acid has been observed in an individual carrying a homozygous missense change in KYNU (PubMed:17334708). The urinary pattern in the patient suggests kynureninase deficiency and a block in the conversion of kynurenine and 3-hydroxykynurenine to anthranilate and 3-hydroxyanthranilate, respectively.
SIMILARITY: Belongs to the kynureninase family.
CAUTION: It has been reported that this enzyme possesses no measurable activity against L-kynurenine and is subject to inhibition by both L-kynurenine and D-kynurenine at pH 7.9 (PubMed:11985583).

-  MalaCards Disease Associations
  MalaCards Gene Search: KYNU
Diseases sorted by gene-association score: hydroxykynureninuria* (1639), pellagra (17), transient cerebral ischemia (13)
* = Manually curated disease association

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 18.19 RPKM in Cells - EBV-transformed lymphocytes
Total median expression: 79.08 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -25.3092-0.275 Picture PostScript Text
3' UTR -3622.8613661-0.265 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR000192 - Aminotrans_V/Cys_dSase
IPR010111 - Kynureninase
IPR015424 - PyrdxlP-dep_Trfase_major_dom
IPR015421 - PyrdxlP-dep_Trfase_major_sub1
IPR015422 - PyrdxlP-dep_Trfase_major_sub2

Pfam Domains:
PF00266 - Aminotransferase class-V

Protein Data Bank (PDB) 3-D Structure
MuPIT help

2HZP
- X-ray MuPIT

3E9K
- X-ray MuPIT


ModBase Predicted Comparative 3D Structure on Q16719
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-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
Genome BrowserGenome BrowserNo orthologNo orthologNo orthologNo ortholog
Gene Details     
Gene Sorter     
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Protein SequenceProtein Sequence    
AlignmentAlignment    

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0003824 catalytic activity
GO:0016787 hydrolase activity
GO:0030170 pyridoxal phosphate binding
GO:0030429 kynureninase activity
GO:0042803 protein homodimerization activity

Biological Process:
GO:0006569 tryptophan catabolic process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process
GO:0019441 tryptophan catabolic process to kynurenine
GO:0019442 tryptophan catabolic process to acetyl-CoA
GO:0019805 quinolinate biosynthetic process
GO:0034341 response to interferon-gamma
GO:0034516 response to vitamin B6
GO:0043420 anthranilate metabolic process
GO:0097053 L-kynurenine catabolic process

Cellular Component:
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol


-  Descriptions from all associated GenBank mRNAs
  LP747426 - Sequence 13 from Patent WO2018009939.
AK223426 - Homo sapiens mRNA for kynureninase (L-kynurenine hydrolase) variant, clone: FCC110E06.
U57721 - Human L-kynurenine hydrolase mRNA, complete cds.
AK315343 - Homo sapiens cDNA, FLJ96385, highly similar to Homo sapiens kynureninase (L-kynurenine hydrolase) (KYNU), mRNA.
AK292095 - Homo sapiens cDNA FLJ78002 complete cds, highly similar to Homo sapiens kynureninase (L-kynurenine hydrolase) (KYNU), mRNA.
AK290900 - Homo sapiens cDNA FLJ77887 complete cds, highly similar to Human L-kynurenine hydrolase mRNA.
CR457423 - Homo sapiens full open reading frame cDNA clone RZPDo834D1114D for gene KYNU, kynureninase (L-kynurenine hydrolase); complete cds, incl. stopcodon.
MB486566 - JP 2019531699-A/13: METHODS FOR DIAGNOSING AND TREATING CANCER.
BC000879 - Homo sapiens kynureninase (L-kynurenine hydrolase), mRNA (cDNA clone MGC:5080 IMAGE:3461828), complete cds.
HQ447861 - Synthetic construct Homo sapiens clone IMAGE:100071208; CCSB002729_01 kynureninase (L-kynurenine hydrolase) (KYNU) gene, encodes complete protein.
KJ892658 - Synthetic construct Homo sapiens clone ccsbBroadEn_02052 KYNU gene, encodes complete protein.
KR709639 - Synthetic construct Homo sapiens clone CCSBHm_00004634 KYNU (KYNU) mRNA, encodes complete protein.
CU674438 - Synthetic construct Homo sapiens gateway clone IMAGE:100018809 5' read KYNU mRNA.
JD168891 - Sequence 149915 from Patent EP1572962.
JD040512 - Sequence 21536 from Patent EP1572962.
JD295697 - Sequence 276721 from Patent EP1572962.
JD327755 - Sequence 308779 from Patent EP1572962.
JD432781 - Sequence 413805 from Patent EP1572962.
DQ591425 - Homo sapiens piRNA piR-58537, complete sequence.
DQ599157 - Homo sapiens piRNA piR-37223, complete sequence.
JD116176 - Sequence 97200 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  KEGG - Kyoto Encyclopedia of Genes and Genomes
hsa00380 - Tryptophan metabolism
hsa01100 - Metabolic pathways

BioCyc Knowledge Library
NADSYN-PWY - NAD de novo biosynthesis
PWY-5651 - tryptophan degradation to 2-amino-3-carboxymuconate semialdehyde
PWY-6309 - L-kynurenine degradation
PWY66-401 - superpathway of tryptophan utilization
TRYPTOPHAN-DEGRADATION-1 - tryptophan degradation

Reactome (by CSHL, EBI, and GO)

Protein Q16719 (Reactome details) participates in the following event(s):

R-HSA-71217 3-hydroxykynurenine + H2O => 3-hydroxyanthranilate + alanine
R-HSA-71240 Tryptophan catabolism
R-HSA-6788656 Histidine, lysine, phenylalanine, tyrosine, proline and tryptophan catabolism
R-HSA-71291 Metabolism of nitrogenous molecules
R-HSA-1430728 Metabolism

-  Other Names for This Gene
  Alternate Gene Symbols: B2RCZ5, D3DP79, ENST00000264170.1, ENST00000264170.2, ENST00000264170.3, ENST00000264170.4, ENST00000264170.5, ENST00000264170.6, ENST00000264170.7, ENST00000264170.8, KYNU_HUMAN, NM_003937, Q16719, Q6I9T2, Q9BVW3, uc002tvl.1, uc002tvl.2, uc002tvl.3, uc002tvl.4, uc002tvl.5
UCSC ID: ENST00000264170.9
RefSeq Accession: NM_003937
Protein: Q16719 (aka KYNU_HUMAN)
CCDS: CCDS2183.1

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.