Maize polyamine oxidase: primary structure from protein and cDNA sequencing

FEBS Lett. 1998 Apr 10;426(1):62-6. doi: 10.1016/s0014-5793(98)00311-1.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • DNA, Complementary / genetics
  • Molecular Sequence Data
  • Monoamine Oxidase / chemistry
  • Oxidoreductases Acting on CH-NH Group Donors / chemistry*
  • Oxidoreductases Acting on CH-NH Group Donors / genetics
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Zea mays / enzymology*
  • Zea mays / genetics

Substances

  • DNA, Complementary
  • Plant Proteins
  • Monoamine Oxidase
  • Oxidoreductases Acting on CH-NH Group Donors
  • polyamine oxidase

Associated data

  • GENBANK/AJ002204