Isolation and characterization of glyoxylate dehydrogenase from the fungus Sclerotium rolfsii.
Glyoxylate dehydrogenase (glyoxylate:NAD+ oxidoreductase) was purified 600-fold in three steps from crude extracts of the fungus Sclerotium rolfsii (Corticium rolfsii Curzi). Two of the purification steps involved dye-affinity chromatography. The enzyme is a tetramer of Mr 250 000, with identical subunits of Mr 57 000. Inhibition studies suggest that there is one essential thiol group per active site.
D000445:Aldehyde Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D000838:Anions / Q000494:pharmacology; D001665:Binding Sites; D002846:Chromatography, Affinity; D005658:Fungi / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing
D000838:Anions; D000445:Aldehyde Oxidoreductases; C040590:glyoxylate dehydrogenase (acylating)