Purification and N-terminal amino acid sequence of solanapyrone synthase, a natural Diels-Alderase from Alternaria solani

Biosci Biotechnol Biochem. 2008 Feb;72(2):604-7. doi: 10.1271/bbb.70600. Epub 2008 Feb 7.

Abstract

The first natural Diels-Alderase, solanapyrone synthase, was purified 1,630-fold from a crude extract. The 41-kDa protein on SDS-polyacrylamide gel electrophoresis was identified as truncated solanapyrone synthase, and its N-terminal amino acid sequence was found to be QETQNLNNFLESNAINP.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternaria / enzymology*
  • Amino Acid Sequence
  • Electrophoresis, Polyacrylamide Gel
  • Ligases / chemistry
  • Ligases / isolation & purification*
  • Molecular Sequence Data

Substances

  • Ligases