Atypical biosynthetic properties of a Delta 12/nu+3 desaturase from the model basidiomycete Phanerochaete chrysosporium.

ABSTRACT: The model white-rot basidiomycete Phanerochaete chrysosporium contains a single integral membrane Delta(12)-desaturase FAD2 related to the endoplasmic reticular plant FAD2 enzymes. The fungal fad2-like gene was cloned and distinguished itself from plant homologs by the presence of four introns and a significantly larger coding region. The coding sequence exhibits ca. 35% sequence identity to plant homologs, with the highest sequence conservation found in the putative catalytic and major structural domains. In vivo activity of the heterologously expressed enzyme favors C(18) substrates with nu+3 regioselectivity, where the site of desaturation is three carbons carboxy-distal to the reference position of a preexisting double bond (nu). Linoleate accumulated to levels in excess of 12% of the

SUBMITTER: Minto RE 

PROVIDER: S-EPMC2643574 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature