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

Bioscience, Biotechnology, and Biochemistry

Online ISSN : 1347-6947
Print ISSN : 0916-8451

Organic Chemistry Notes

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

2008 Volume 72 Issue 2 Pages 604-607

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

View "Advance Publication" version (February 7, 2008).

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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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