Purification and Properties of a Catechol Methyltransferase of the Yeast Candida tropicalis

Abstract

In an effort to investigate catechol methyltransferase activity in sources other than mammalian tissues and cells, a high level of enzyme activity was found in the yeast fungus C. tropicalis CBS 94. Partial purification of the enzyme (about 550-fold with a recovery of 7%) could be achieved by using ion-exchange and gel filtration techniques. The MW was estimated at 32,000 .+-. 2,000 by gel filtration on Sephadex G-100. In isoelectric focusing experiments on Sephadex G-75 the enzyme exhibited a pI-value of 5.0 .+-. 0.1. In contrast to catechol methyltransferase from various mammalian tissues, the enzyme activity was prepared from the pH 5-sediment. The substrate specificity is comparable to other catechol methyltransferases.