Literature DB >> 160694

Purification and properties of a catechol methyltransferase of the yeast Candida tropicalis.

J Veser, P Geywitz, H Thomas.   

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 Candida tropicalis CBS 94. Partial purification of the enzyme (approx. 550 fold with a recovery of 7%) could be achieved by using ion-exchange and gel filtration techniques. The molecular weight 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 specifity is comparable to other catechol methyltransferases.

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Year:  1979        PMID: 160694     DOI: 10.1515/znc-1979-9-1010

Source DB:  PubMed          Journal:  Z Naturforsch C Biosci        ISSN: 0341-0382


  2 in total

1.  Bacterial methylation of chlorinated phenols and guaiacols: formation of veratroles from guaiacols and high-molecular-weight chlorinated lignin.

Authors:  A H Neilson; A S Allard; P A Hynning; M Remberger; L Landner
Journal:  Appl Environ Microbiol       Date:  1983-03       Impact factor: 4.792

2.  Kinetics and inhibition studies of catechol O-methyltransferase from the yeast Candida tropicalis.

Authors:  J Veser
Journal:  J Bacteriol       Date:  1987-08       Impact factor: 3.490

  2 in total

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