ID KYNU_RAT Reviewed; 464 AA. AC P70712; Q68G25; Q7M0D0; Q9QW90; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 09-NOV-2004, sequence version 2. DT 08-APR-2008, entry version 62. DE Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase). GN Name=Kynu; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY. RC STRAIN=Wistar; TISSUE=Liver; RX MEDLINE=96049498; PubMed=7578221; DOI=10.1016/0167-4838(95)00166-R; RA Takeuchi F., Tsubouchi R., Yoshino M., Shibata Y.; RT "Amino-acid sequence of rat liver kynureninase."; RL Biochim. Biophys. Acta 1252:185-188(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RX MEDLINE=97324088; PubMed=9180257; DOI=10.1016/S0014-5793(97)00374-8; RA Toma S., Nakamura M., Tone S., Okuno E., Kido R., Breton J., RA Avanzi N., Cozzi L., Speciale C., Mostardini M., Gatti S., Benatti L.; RT "Cloning and recombinant expression of rat and human kynureninase."; RL FEBS Lett. 408:5-10(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-117, AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Kidney, and Liver; RX MEDLINE=96314506; PubMed=8706755; RA Alberati-Giani D., Buchli R., Malherbe P., Broger C., Lang G., RA Koehler C., Lahm H.-W., Cesura A.M.; RT "Isolation and expression of a cDNA clone encoding human RT kynureninase."; RL Eur. J. Biochem. 239:460-468(1996). RN [5] RP PROTEIN SEQUENCE OF 83-116 AND 273-319. RC TISSUE=Liver; RA Matsui Lee I.S., Okuno E., Kido R.; RL Submitted (JUN-1992) to the PIR data bank. CC -!- FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- CC hydroxykynurenine (L-3OHKyn) into anthranilic (AA) and 3- CC hydroxyanthranilic acids (3-OHAA), respectively. Has a preference CC for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase CC activity. CC -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L- CC alanine. CC -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3- CC hydroxyanthranilate + L-alanine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- ENZYME REGULATION: Inhibited by o-methylbenzoylalanine (OMBA). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is about 9.0 with L-Kyn as substrate, and about 8.5 CC with L-3OHKyn as substrate; CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L- CC alanine and anthranilate from L-kynurenine: step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; pyridine-2,3- CC dicarboxylate from L-kynurenine: step 2/3. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: High levels in liver and kidney. Also detected CC in heart, retina, ovary. Lung, testis and brain. CC -!- INDUCTION: Inhibited by thiol reagents and heavy metal ions. CC -!- SIMILARITY: Belongs to the kynureninase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U68168; AAC53206.1; -; mRNA. DR EMBL; BC078762; AAH78762.1; -; mRNA. DR PIR; PS0370; PS0370. DR PIR; S59898; S59898. DR PIR; T48675; T48675. DR RefSeq; NP_446354.1; -. DR UniGene; Rn.10575; -. DR SMR; P70712; 6-460. DR Ensembl; ENSRNOG00000029993; Rattus norvegicus. DR GeneID; 116682; -. DR KEGG; rno:116682; -. DR RGD; 71061; Kynu. DR ArrayExpress; P70712; -. DR GermOnline; ENSRNOG00000029993; Rattus norvegicus. DR InterPro; IPR000192; Aminotrans_V/Cys_dSase. DR InterPro; IPR010111; Kynureninase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1. DR PANTHER; PTHR14084; Kynureninase; 1. DR Pfam; PF00266; Aminotran_5; 1. DR TIGRFAMs; TIGR01814; kynureninase; 1. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; KW Pyridine nucleotide biosynthesis; Pyridoxal phosphate. FT CHAIN 1 464 Kynureninase. FT /FTId=PRO_0000218659. FT BINDING 276 276 Pyridoxal phosphate (covalent). FT MOD_RES 1 1 N-acetylmethionine. FT CONFLICT 18 18 T -> A (in Ref. 2; AAC53206). FT CONFLICT 26 26 D -> N (in Ref. 1; AA sequence). FT CONFLICT 118 118 S -> T (in Ref. 2; AAC53206). SQ SEQUENCE 464 AA; 52470 MW; 1490A74EFF7287AC CRC64; MEPSPLELPV DAVRRIATEL NCDPTDERVA LRLDEEDKLK RFKDCFYIPK MRDLPSIDLS LVNEDDNAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIGAY GHEVGKRPWI IGDESIVSLM KDIVGAHEKE IALMNALTVN LHLLLLSFFK PTPKRHKILL EAKAFPSDHY AIESQIQLHG LDVEKSMRMI KPREGEETLR MEDILEVIEK EGDSIAVVLF SGLHFYTGQL FNIPAITQAG HAKGCFVGFD LAHAVGNVEL HLHDWDVDFA CWCSYKYLNS GAGGLAGAFI HEKHAHTIKP ALVGWFGHEL STRFNMDNKL QLIPGVNGFR ISNPPILLVC SLHASLEIFQ QATMTALRRK SILLTGYLEY LLKHYHGGND TENKRPVVNI ITPSRAEERG CQLTLTFSIS KKGVFKELEK RGVVCDKREP EGIRVAPVPL YNSFHDVYKF IRLLTAILDS TERN //