Abstract
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.
Original language | English |
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Pages (from-to) | 62-66 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 426 |
Issue number | 1 |
DOIs | |
Publication status | Published - Apr 10 1998 |
Keywords
- Flavin oxidase
- Hydrogen peroxide
- Polyamine oxidase
- Primary structure
- Zea mays L.
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology