Maleylacetate reductase from Trichosporon cutaneum.
The enzyme catalysing the reduction of maleylacetate to 3-oxoadipate was purified 150-fold from Trichosporon cutaneum, induced for aromatic metabolisms by growth with resorcinol as a major carbon source. The enzyme separated upon electrofocusing into three species with PI values 4.6, 5.1 and 5.6. They had similar catalytic properties and the same molecular weight.
D055598:Chemical Phenomena; D002621:Chemistry; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000302:isolation & purification; D010088:Oxidoreductases / Q000302:isolation & purification*; D044925:Oxidoreductases Acting on CH-CH Group Donors; D015003:Yeasts / Q000201:enzymology*
D007527:Isoenzymes; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C021530:maleylacetate reductase