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Purification and properties of versiconal cyclase from Aspergillus parasiticus.

Abstract
Versiconal cyclase catalyzes the dehydration of versiconal to versicolorin B or versicolorin C [versicolorin B(C)]. The enzyme was purified from mycelia of Aspergillus parasiticus by DEAE-cellulose, hydroxylapatite, and Mono Q column chromatography. The protein contains two identical subunits of molecular weight 72,000 per molecule of native protein. The pI of the enzyme is 3.95. The pH activity curve had a broad maximum with a peak at 5.5. The Km and Vmax for versiconal at 30 degrees C and pH 6.0 are 3.1 microM and 0.15 mumol min-1mg-1, respectively. Most of the formation of versicolorin B(C) in the cell is attributed to the action of versiconal cyclase.
AuthorsB K Lin, J A Anderson
JournalArchives of biochemistry and biophysics (Arch Biochem Biophys) Vol. 293 Issue 1 Pg. 67-70 (Feb 14 1992) ISSN: 0003-9861 [Print] UNITED STATES
PMID1731640 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Aflatoxins
  • Anthraquinones
  • versiconal
  • Hydro-Lyases
  • versiconal cyclase
Topics
  • Aflatoxins (biosynthesis)
  • Anthraquinones (metabolism)
  • Aspergillus (enzymology)
  • Chromatography, High Pressure Liquid
  • Hydro-Lyases (isolation & purification)
  • Hydrogen-Ion Concentration
  • Molecular Weight

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