Structural analysis of the rat uricase gene and evidence that lysine 164 is involved in the substrate-binding site of the enzyme.
Ito
M
M
Laboratory of Biology, Saga Medical School, Japan.
Nakamura
M
M
Kato
S
S
Ogawa
H
H
Takagi
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular / Q000379:methods; D003360:Cosmids; D004926:Escherichia coli / Q000235:genetics; D015698:Genomic Library; D007700:Kinetics; D008239:Lysine; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009838:Oligodeoxyribonucleotides; D051381:Rats; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D015183:Restriction Mapping; D014503:Urate Oxidase / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D019820:Xanthine; D014970:Xanthines / Q000378:metabolism
D009838:Oligodeoxyribonucleotides; D011994:Recombinant Proteins; D014970:Xanthines; D019820:Xanthine; D014503:Urate Oxidase; D008239:Lysine