ID KYNU_RAT STANDARD; PRT; 464 AA. AC P70712; Q9QW90; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase). GN 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; 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; 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 OF 19-117 FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Liver, and Kidney; 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). 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- CC BETA-LYASE ACTIVITY. CC -!- CATALYTIC ACTIVITY: L-KYNURENINE + H(2)O = ANTHRANILATE + CC L-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: INVOLVED IN THE BIOSYNTHESIS OF NAD COFACTORS FROM CC TRYPTOPHAN THROUGH THE KYNURENINE PATHWAY. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: HIGH LEVELS IN LIVER AND KIDNEY. ALSO CC DETECTED 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. SLIGHTLY RELATED CC TO CLASS-V OF PYRIDOXAL-PHOSPHATE-DEPENDENT AMINOTRANSFERASES. 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; -. KW Hydrolase; Pyridoxal phosphate; Acetylation. FT MOD_RES 1 1 ACETYLATION. FT BINDING 276 276 PYRIDOXAL PHOSPHATE. FT CONFLICT 18 18 A -> T (IN REF. 1). FT CONFLICT 26 26 D -> N (IN REF. 1). FT CONFLICT 118 118 T -> S (IN REF. 1). SQ SEQUENCE 464 AA; 52453 MW; FF1CC95E3202ECEC CRC64; MEPSPLELPV DAVRRIAAEL NCDPTDERVA LRLDEEDKLK RFKDCFYIPK MRDLPSIDLS LVNEDDNAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIGAY GHEVGKRPWI IGDESIVTLM 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 //