Abstract
A new glyoxylate dehydrogenase which catalyzes dehydrogenation of glyoxylate to oxalate in the presence of cytochrome c has been purified as an electrophoretically homogeneous protein from the cell-free extracts of a wood-destroying basidiomycete Tyromyces palustris. The enzymatic reduction of cytochrome c was dependent on glyoxylate which was found to be the best substrate among the compounds tested. The K m value for glyoxylate was determined to be 2.7 mM at the optimal pH (8.0). The UV-visible spectra of the enzyme in oxidized and reduced forms indicate that the enzyme belongs to a family of flavohemoproteins. The flavin nucleotide isolated from the native enzyme by heat denaturation was identified as FMN. The enzyme ( M r 331 000) consists of six identical homopolymers ( M r of subunit 59 000), which were found to constitute a symmetric octahedral shape by electron-microscopic observation with a negative staining method.
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