Amino-acid sequence of rat liver kynureninase.
Amino-acid sequence of kynureninase purified from rat liver cytosol was determined by an amino-acid sequencer. The enzyme was degraded to small peptides with cyanogen bromide, TPCK-trypsin, endoproteinase Glu-C, lysyl endoprotease and alpha-chymotrypsin. The enzyme subunit consisted of 464 amino acids, and the molecular weight of subunit was determined to be 52,510. The coenzyme pyridoxal phosphate-binding residue was lysine of which position was 276, and the N-terminal residue was N-acetylmethionine. The homology search between this enzyme and the other pyridoxal phosphate-dependent enzymes showed that kynureninase was similar to mitochondrial aspartate aminotransferase, and also to cystathionine gamma-synthase and gamma-lyase to a lesser extent.
Takeuchi
F
F
Department of Biochemistry Aichi Medical University Nagakute-cho, Japan.
Tsubouchi
R
R
Yoshino
M
M
Shibata
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003488:Cyanogen Bromide; D003600:Cytosol / Q000201:enzymology; D006867:Hydrolases / Q000737:chemistry / Q000302:isolation & purification*; D008099:Liver / Q000201:enzymology*; D008297:Male; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D051381:Rats; D017208:Rats, Wistar; D016415:Sequence Alignment
D010446:Peptide Fragments; D006867:Hydrolases; C021480:kynureninase; D003488:Cyanogen Bromide