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3-Hydroxybenzoate:Coenzyme A Ligase from Cell Cultures of Centaurium erythraea: Isolation and Characterization
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Wagner Barillas
Published/Copyright:
June 1, 2005
Abstract
In xanthone biosynthesis, 3-hydroxybenzoate:coenzyme A ligase (3HBL) supplies the starter substrate for the formation of an intermediate benzophenone. 3HBL from cell cultures of the medicinal plant Centaurium erythraea was purified to apparent homogeneity using a sevenstepprocedure. The enzyme was an AMPforming CoA ligase with a K = 14.7 for 3-hydroxybenzoic acid, 8.5 for coenzyme A and 229 for ATP. The pH and temperature optima were 7.5 and 35C, respectively. In SDSPAGE, two polypeptides of M 41500 and 40500 were detected. Both proteins were structurally related to each other as shown by tryptic digestion. Their Ntermini were blocked. The difference in their apparent molecular masses could not be attributed to glycosylation. 3HBL had a native M of approx. 50000 and is thus active as a monomer.
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Published Online: 2005-06-01
Published in Print: 2000-02-15
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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- Responses to Peroxynitrite in Yeast: Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) as a Sensitive Intracellular Target for Nitration and Enhancement of Chaperone Expression and Ubiquitination
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