Q16719 (KYNU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kynureninase
EC=3.7.1.3

Alternative name(s):
L-kynurenine hydrolase

Gene names

Name:

KYNU

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. HAMAP-Rule MF_03017
Catalytic activity	L-kynurenine + H2O = anthranilate + L-alanine. Ref.1 Ref.2 Ref.8 Ref.10 L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. Ref.1 Ref.2 Ref.8 Ref.10
Cofactor	Pyridoxal phosphate.
Enzyme regulation	Inhibited by o-methoxybenzoylalanine (OMBA). Ref.1 Ref.2
Pathway	Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. HAMAP-Rule MF_03017 Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. HAMAP-Rule MF_03017
Subunit structure	Homodimer. Ref.10
Subcellular location	Cytoplasm Ref.1.
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. Ref.1 Ref.2
Induction	Increased levels in several cerebral and systemic inflammatory conditions. Ref.1 Ref.2
Involvement in disease	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 (Ref.11). 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.
Sequence similarities	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 (Ref.8).
Biophysicochemical properties	Kinetic parameters: KM=493 µM for L-kynurenine (at pH 7.0) Ref.1 Ref.2 Ref.8 Ref.10 KM=28.3 µM for DL-3-hydroxykynurenine (at pH 7.0) KM=3.0 µM for DL-3-hydroxykynurenine (at pH 7.9) pH dependence: Optimum pH is 8.25 with DL-3-hydroxykynurenine as substrate.
Mass spectrometry	Molecular mass is 52400 Da from positions 1 - 465. Determined by MALDI. The reported mass is given to only three significant figures. Ref.8

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	Pyridoxal phosphate
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-kynurenine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway NAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway anthranilate metabolic process Inferred from direct assay Ref.8. Source: UniProtKB quinolinate biosynthetic process Inferred from direct assay PubMed 9291104. Source: UniProtKB response to interferon-gamma Inferred from direct assay PubMed 9291104. Source: UniProtKB response to vitamin B6 Inferred from mutant phenotype PubMed 1939450. Source: UniProtKB tryptophan catabolic process Inferred from mutant phenotype Ref.11. Source: UniProtKB tryptophan catabolic process to acetyl-CoA Inferred from electronic annotation. Source: Compara tryptophan catabolic process to kynurenine Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from direct assay PubMed 6468727. Source: UniProtKB mitochondrion Inferred from direct assay PubMed 6468727. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA
Molecular_function	kynureninase activity Inferred from direct assay Ref.8Ref.2. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.8. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q16719-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q16719-2)

The sequence of this isoform differs from the canonical sequence as follows:
     302-307: LVGWFG → RSEFFN
     308-465: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 465

465

Kynureninase HAMAP-Rule MF_03017

PRO_0000218657

Regions

Region

165 – 168

4

Pyridoxal phosphate binding HAMAP-Rule MF_03017

Sites

Binding site

137

1

Pyridoxal phosphate; via amide nitrogen By similarity

Binding site

138

1

Pyridoxal phosphate

Binding site

221

1

Pyridoxal phosphate By similarity

Binding site

250

1

Pyridoxal phosphate

Binding site

253

1

Pyridoxal phosphate

Binding site

275

1

Pyridoxal phosphate

Binding site

305

1

Pyridoxal phosphate

Binding site

333

1

Pyridoxal phosphate

Amino acid modifications

Modified residue

1

1

N-acetylmethionine By similarity

Modified residue

276

1

N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_03017

Natural variations

Alternative sequence

302 – 307

6

LVGWFG → RSEFFN in isoform 2.

VSP_042739

Alternative sequence

308 – 465

158

Missing in isoform 2.

VSP_042740

Natural variant

188

1

R → Q.
Corresponds to variant rs2304705 [ dbSNP | Ensembl ].

VAR_049724

Natural variant

198

1

T → A Detected in a boy with xanthurenic aciduria. Ref.11

VAR_054401

Natural variant

412

1

K → E. Ref.3
Corresponds to variant rs9013 [ dbSNP | Ensembl ].

VAR_022092

Secondary structure

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465

Helix Strand Turn

Details...

Helix

9 – 20

12

Helix

27 – 35

9

Helix

40 – 45

6

Helix

51 – 53

3

Helix

59 – 61

3

Turn

73 – 75

3

Helix

83 – 97

15

Helix

98 – 102

5

Beta strand

104 – 107

4

Helix

109 – 111

3

Helix

114 – 117

4

Helix

118 – 120

3

Helix

121 – 124

4

Helix

128 – 130

3

Beta strand

131 – 133

3

Helix

137 – 148

12

Beta strand

153 – 155

3

Beta strand

157 – 161

5

Helix

166 – 178

13

Helix

183 – 186

4

Beta strand

187 – 190

4

Helix

201 – 211

11

Helix

212 – 214

3

Beta strand

215 – 223

9

Turn

225 – 227

3

Helix

233 – 242

10

Beta strand

246 – 250

5

Turn

252 – 257

6

Helix

262 – 265

4

Beta strand

269 – 272

4

Beta strand

274 – 276

3

Beta strand

287 – 290

4

Helix

292 – 294

3

Turn

295 – 297

3

Helix

305 – 307

3

Helix

310 – 313

4

Helix

326 – 329

4

Helix

336 – 352

17

Helix

354 – 375

22

Beta strand

388 – 390

3

Helix

396 – 398

3

Beta strand

403 – 407

5

Helix

414 – 419

6

Turn

420 – 422

3

Beta strand

426 – 428

3

Turn

429 – 431

3

Beta strand

432 – 436

5

Turn

439 – 441

3

Helix

444 – 458

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BDD136BE18C79EBB	FASTA	465	52,352
	10 20 30 40 50 60 MEPSSLELPA DTVQRIAAEL KCHPTDERVA LHLDEEDKLR HFRECFYIPK IQDLPPVDLS 70 80 90 100 110 120 LVNKDENAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIAAY GHEVGKRPWI TGDESIVGLM 130 140 150 160 170 180 KDIVGANEKE IALMNALTVN LHLLMLSFFK PTPKRYKILL EAKAFPSDHY AIESQLQLHG 190 200 210 220 230 240 LNIEESMRMI KPREGEETLR IEDILEVIEK EGDSIAVILF SGVHFYTGQH FNIPAITKAG 250 260 270 280 290 300 QAKGCYVGFD LAHAVGNVEL YLHDWGVDFA CWCSYKYLNA GAGGIAGAFI HEKHAHTIKP 310 320 330 340 350 360 ALVGWFGHEL STRFKMDNKL QLIPGVCGFR ISNPPILLVC SLHASLEIFK QATMKALRKK 370 380 390 400 410 420 SVLLTGYLEY LIKHNYGKDK AATKKPVVNI ITPSHVEERG CQLTITFSVP NKDVFQELEK 430 440 450 460 RGVVCDKRNP NGIRVAPVPL YNSFHDVYKF TNLLTSILDS AETKN
	Isoform 2 [UniParc]. Checksum: 9219F37B19D2163E	FASTA	307	34,635
	10 20 30 40 50 60 MEPSSLELPA DTVQRIAAEL KCHPTDERVA LHLDEEDKLR HFRECFYIPK IQDLPPVDLS 70 80 90 100 110 120 LVNKDENAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIAAY GHEVGKRPWI TGDESIVGLM 130 140 150 160 170 180 KDIVGANEKE IALMNALTVN LHLLMLSFFK PTPKRYKILL EAKAFPSDHY AIESQLQLHG 190 200 210 220 230 240 LNIEESMRMI KPREGEETLR IEDILEVIEK EGDSIAVILF SGVHFYTGQH FNIPAITKAG 250 260 270 280 290 300 QAKGCYVGFD LAHAVGNVEL YLHDWGVDFA CWCSYKYLNA GAGGIAGAFI HEKHAHTIKP ARSEFFN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and expression of a cDNA clone encoding human kynureninase." Alberati-Giani D., Buchli R., Malherbe P., Broger C., Lang G., Koehler C., Lahm H.-W., Cesura A.M. Eur. J. Biochem. 239:460-468(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Hepatoma.
[2]	"Cloning and recombinant expression of rat and human kynureninase." Toma S., Nakamura M., Tone S., Okuno E., Kido R., Breton J., Avanzi N., Cozzi L., Speciale C., Mostardini M., Gatti S., Benatti L. FEBS Lett. 408:5-10(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Liver.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-412. Tissue: Synovium.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Cervix.
[8]	"Purification and biochemical characterization of some of the properties of recombinant human kynureninase." Walsh H.A., Botting N.P. Eur. J. Biochem. 269:2069-2074(2002) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Crystal structure of Homo sapiens kynureninase." Lima S., Khristoforov R., Momany C., Phillips R.S. Biochemistry 46:2735-2744(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, HOMODIMERIZATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[11]	"Xanthurenic aciduria due to a mutation in KYNU encoding kynureninase." Christensen M., Duno M., Lund A.M., Skovby F., Christensen E. J. Inherit. Metab. Dis. 30:248-255(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-198, POSSIBLE INVOLVEMENT IN XANTHURENIC ACIDURIA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U57721 mRNA. Translation: AAC50650.1.
AK315343 mRNA. Translation: BAG37742.1.
CR457423 mRNA. Translation: CAG33704.1.
AC013437 Genomic DNA. No translation available.
AC013444 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11599.1.
CH471058 Genomic DNA. Translation: EAX11600.1.
CH471058 Genomic DNA. Translation: EAX11601.1.
BC000879 mRNA. Translation: AAH00879.1.

IPI

IPI00003818.
IPI00651624.

PIR

G02652.

RefSeq

NP_001028170.1. NM_001032998.1.
NP_001186170.1. NM_001199241.1.
NP_003928.1. NM_003937.2.

UniGene

Hs.470126.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HZP	X-ray	2.00	A	1-465	[»]
3E9K	X-ray	1.70	A	1-465	[»]

ProteinModelPortal

Q16719.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q16719. 1 interaction.

STRING

9606.ENSP00000264170.

PTM databases

PhosphoSite

Q16719.

Polymorphism databases

DMDM

3913982.

Proteomic databases

PaxDb

Q16719.

PeptideAtlas

Q16719.

PRIDE

Q16719.

Protocols and materials databases

DNASU

8942.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264170; ENSP00000264170; ENSG00000115919.
ENST00000375773; ENSP00000364928; ENSG00000115919.
ENST00000409512; ENSP00000386731; ENSG00000115919.

GeneID

8942.

KEGG

hsa:8942.

UCSC

uc002tvk.3. human.
uc002tvl.3. human.

Organism-specific databases

CTD

8942.

GeneCards

GC02P143657.

HGNC

HGNC:6469. KYNU.

HPA

HPA031686.

MIM

605197. gene.

neXtProt

NX_Q16719.

Orphanet

79155. Encephalopathy due to hydroxykynureninuria.

PharmGKB

PA30258.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3844.

HOGENOM

HOG000242438.

HOVERGEN

HBG001170.

InParanoid

Q16719.

KO

K01556.

OMA

MLTHVNY.

OrthoDB

EOG490793.

PhylomeDB

Q16719.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00253; UER00329.
UPA00334; UER00455.

Gene expression databases

ArrayExpress

Q16719.

Bgee

Q16719.

CleanEx

HS_KYNU.

Genevestigator

Q16719.

GermOnline

ENSG00000115919. Homo sapiens.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

HAMAP

MF_01970. Kynureninase.

InterPro

IPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

PANTHER

PTHR14084. PTHR14084. 1 hit.

Pfam

PF00266. Aminotran_5. 1 hit.
[Graphical view]

PIRSF

PIRSF038800. KYNU. 1 hit.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

TIGRFAMs

TIGR01814. kynureninase. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q16719.

ChEMBL

CHEMBL5100.

ChiTaRS

KYNU. human.

DrugBank

DB00160. L-Alanine.
DB00114. Pyridoxal Phosphate.

EvolutionaryTrace

Q16719.

GenomeRNAi

8942.

NextBio

33630.

SOURCE

Search...

Entry information

Entry name

KYNU_HUMAN

Accession

Primary (citable) accession number: Q16719
Secondary accession number(s): B2RCZ5 , D3DP79, Q6I9T2, Q9BVW3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.