ID KYNU_RAT STANDARD; PRT; 464 AA. AC P70712; Q68G25; Q7M0D0; Q9QW90; DT 15-DEC-1998 (Rel. 37, Created) DT 25-JAN-2005 (Rel. 46, Last sequence update) DT 25-JAN-2005 (Rel. 46, Last annotation update) 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; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP 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 SEQUENCE FROM N.A., AND PARTIAL 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 SEQUENCE FROM N.A. RC TISSUE=Kidney; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 19-117 FROM N.A., AND PARTIAL 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 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. Optimum activity is around pH 9.0 for L- CC kyn and around 8.5 for L-3OHKYN. Also has cysteine-conjugate-beta- CC lyase 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 -!- PATHWAY: NAD biosynthesis; kynurenine pathway; tryptophan to NaMN; CC fourth step. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. 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; -. DR EMBL; BC078762; AAH78762.1; -. DR PIR; PS0370; PS0370. DR PIR; S59898; S59898. DR PIR; T48675; T48675. DR RGD; 71061; Kynu. DR InterPro; IPR010111; Kynureninase. DR TIGRFAMs; TIGR01814; kynureninase; 1. KW Acetylation; Direct protein sequencing; Hydrolase; KW Pyridine nucleotide biosynthesis; Pyridoxal phosphate. FT MOD_RES 1 1 N-acetylmethionine. FT BINDING 276 276 Pyridoxal phosphate. FT CONFLICT 18 18 T -> A (in Ref. 2). FT CONFLICT 26 26 D -> N (in Ref. 1). FT CONFLICT 118 118 S -> T (in Ref. 2). SQ SEQUENCE 464 AA; 52469 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 //