Purification and N-Terminal Amino Acid Sequence of Solanapyrone Synthase, A Natural Diels-Alderase from Alternaria solani

Kinya KATAYAMA; Tomonori KOBAYASHI; Masao CHIJIMATSU; Akitami ICHIHARA; Hideaki OIKAWA

doi:10.1271/bbb.70600

This article has now been updated. Please use the final version.

Purification and N-Terminal Amino Acid Sequence of Solanapyrone Synthase, A Natural Diels-Alderase from Alternaria solani

Kinya KATAYAMA, Tomonori KOBAYASHI, Masao CHIJIMATSU, Akitami ICHIHARA, Hideaki OIKAWA

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Keywords: Diels-Alderase, solanapyrone synthase, Alternaria solani

JOURNAL FREE ACCESS Advance online publication

Article ID: 70600

DOI https://doi.org/10.1271/bbb.70600

The final version of this article is now available: Vol. 72 (2008) , No. 2 p.604

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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.

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