Maize polyamine oxidase: primary structure from protein and cDNA sequencing.
The first complete amino acid sequence of a flavin-containing polyamine oxidase was solved by a combined approach of nucleotide and peptide sequence analysis. A cDNA of 1737 bp, isolated from maize seedlings by reverse transcription-polymerase chain reaction and rapid amplification of cDNA ends strategies, was cloned and its sequence determined. This cDNA contains information for a polypeptide chain of 500 amino acids. Its amino-terminal sequence shows the typical features of secretion signal peptides. The primary structure of the mature protein was independently confirmed by extensive amino acid sequencing. Structural relationships with flavin-containing monoamine oxidases are also discussed.
Tavladoraki
P
P
Dipartimento di Biologia, Università Roma Tre, Rome, Italy.
Schininà
M E
ME
Cecconi
F
F
Di Agostino
S
S
Manera
F
F
Rea
G
G
Mariottini
P
P
Federico
R
R
Angelini
R
R
D000595:Amino Acid Sequence; D001483:Base Sequence; D018076:DNA, Complementary / Q000235:genetics; D008969:Molecular Sequence Data; D008995:Monoamine Oxidase / Q000737:chemistry; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry* / Q000235:genetics; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D003313:Zea mays / Q000201:enzymology* / Q000235:genetics; D000097667:Polyamine Oxidase
D018076:DNA, Complementary; D008995:Monoamine Oxidase; D000587:Oxidoreductases Acting on CH-NH Group Donors; D010940:Plant Proteins; D000097667:Polyamine Oxidase