Abstract
The production of oxalic acid is an important attacking mechanism utilized by Whetzelinia sclerotiorum ( = Sclerotinia sclerotiorum) during pathogenesis. An understanding of oxalate biosynthesis would provide the basis for studies on regulation of its production. Extracts prepared from hyphae of W. sclerotiorum contained an enzyme which catalyzed the formation of [ 14C]oxalate and [ 14C]acetate from [U- 14C]oxaloacetate. [ 14C]Oxaloacetate was formed in the reaction mixture by the action of a transaminase on l-[ 14C]aspartate in the presence of α-ketoglutarate. When l-[1- 14C]aspartate was used [ 14C]oxalate was formed but not [ 14C]acetate. When l-[4- 14C]aspartate was used, [ 14C]acetate was formed but not [ 14C]oxalate. These data are consistent with the involvement of oxaloacetate acetylhydrolase in oxalate biosynthesis by this pathogen. Extracts of W. sclerotiorum did not catalyze the reduction of nicotinamide adenine dinucleotide with the concomitant oxidation of glyoxylate to oxalate, as did extracts from Sclerotium rolfsii. The failure to detect oxaloacetate acetylhydrolase in extracts of diseased tissues was probably because it was inactivated during extraction.
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