Purification and characterization of cytochrome C dependent glyoxylate dehydrogenase as a new enzyme from tyromyces palustris

摘要

A glyoxylate dehydrogenase which catalyzes production of oxalate from glyoxylate in the presence of cytochrome c has been purificed as an elecrophoretically pure enzyme from the homogenate of a bronw-rot fungus Tyromyces palustris. The UV-visible spectra of the enyzme in oxidized ahd reduced forms indicate that it is qite similar to cytochrome b_2 type flavohemoprotein from baker's yeast. In fact, FMN was isolated form the holoenzyme by heat denaturation. reduction of cytochrmoe c was dependent on glyoxylate s ubstrate which was found to be the best substrate among the compounds tested.