A tobacco soluble protoporphyrinogen-oxidizing enzyme similar to plant peroxidases in their amino acid sequences and immunochemical reactivity.
Partial amino acid sequences of a soluble protoporphyrinogen-oxidizing enzyme (PPO) purified from tobacco cultured cells were identified. The sequences of two regions of the soluble PPO corresponded to the acid/base catalysis and heme binding regions of plant peroxidases. Anti-soluble PPO IgG cross-reacted with these plant peroxidases. Thus, the soluble PPO seems to be a kind of peroxidase.
Yamato
S
S
Graduate School of Science and Technology, Kobe University, Japan.
Ida
T
T
Katagiri
M
M
Ohkawa
H
H
D000595:Amino Acid Sequence; D000818:Animals; D000918:Antibody Specificity; D015153:Blotting, Western; D002478:Cells, Cultured; D003488:Cyanogen Bromide; D005260:Female; D007120:Immunochemistry; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D044925:Oxidoreductases Acting on CH-CH Group Donors; D010544:Peroxidases / Q000378:metabolism*; D010947:Plants, Toxic; D050768:Protoporphyrinogen Oxidase; D011817:Rabbits; D014026:Nicotiana / Q000737:chemistry / Q000201:enzymology*
D010088:Oxidoreductases; D010544:Peroxidases; D044925:Oxidoreductases Acting on CH-CH Group Donors; D050768:Protoporphyrinogen Oxidase; D003488:Cyanogen Bromide