Complete amino acid sequence of biliverdin-IX beta reductase from human liver.
The amino acid sequence of biliverdin-IX beta reductase (EC1.3.1.24) from human liver was determined by automated Edman degradation of peptides generated by enzymatic and chemical cleavages. The enzyme was a single polypeptide chain of 204 amino acid residues, and its amino acid sequence had no significant homology to that of rat liver biliverdin-IX alpha reductase. Biliverdin-IX alpha reductase from human liver had intense homology to the rat enzyme. Cysteinyl residues are essential for the enzymatic activity of biliverdin-IX alpha, but nonessential for that of biliverdin-IX beta reductase. The results strongly indicate that the two enzymes, biliverdin-IX alpha reductase and biliverdin-IX beta reductase, are distinct in enzymatic action mechanisms as well as ancient origins of gene.
Yamaguchi
T
T
Department of Biochemical Genetics, Tokyo Medical and Dental University, Japan.
Komuro
A
A
Nakano
Y
Y
Tomita
M
M
Nakajima
H
H
D000595:Amino Acid Sequence; D000818:Animals; D003488:Cyanogen Bromide; D010450:Endopeptidases; D006801:Humans; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry*; D044925:Oxidoreductases Acting on CH-CH Group Donors; D010446:Peptide Fragments / Q000302:isolation & purification; D051381:Rats; D017386:Sequence Homology, Amino Acid
D010446:Peptide Fragments; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C019789:biliverdin reductase; D010450:Endopeptidases; D003488:Cyanogen Bromide