Enzymatic activity and partial purification of solanapyrone synthase: first enzyme catalyzing Diels-Alder reaction.
Biochim Biophys Acta
; 1384(2): 387-95, 1998 May 19.
Article
em En
| MEDLINE
| ID: mdl-9659400
ABSTRACT
In cell-free extracts of Alternaria solani, an enzymatic activity converting prosolanapyrone II to solanapyrones A and D via oxidation and subsequent Diels-Alder reaction has been found. Chromatography with DEAE-Sepharose provided two active fractions, pools 1 and 2. The former fraction converted prosolanapyrone II to solanapyrones A and D in a ratio of 2.21 with optical purities of 99% and 45% ee, respectively. The latter fraction did so in a ratio of 7.61 with 99% and nearly 0% ee, respectively. The enzyme partially purified from pool 2 native molecular weight of 40-62 kD and a pl of 4.25. The high reactivity of prosolanapyrone III in aqueous solution and the chromatographic behavior of the enzyme in pool 2 suggest that a single enzyme catalyzes both the oxidation and Diels-Alder reaction.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Pironas
/
Oxirredutases Intramoleculares
/
Alternaria
/
Naftalenos
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Japão