Purification and Properties of a New Enzyme from Evernia prunastri, which Reduces ʟ-Usnic Acid
Open Access
- 1 February 1981
- journal article
- Published by Walter de Gruyter GmbH in Zeitschrift für Naturforschung C
- Vol. 36 (1-2) , 35-39
- https://doi.org/10.1515/znc-1981-1-208
Abstract
New enzyme, usnic acid dehydrogenase, which catalyzes the reduction of ʟ-usnic acid, has been isolated from cell-free extract of Evernia prunastri thallus. Purification of the enzyme (approx. 150-fold with a recovery of 42%) can be achieved by using gel adsorption and gel filtration techniques. The apparent molecular weight of the enzyme is 450000. Cofactor requirement is restricted to NADH. Kinetics of the enzyme show an allosteric behaviour for both ʟ-usnic acid and NADH. Structure of the reaction product is described.Keywords
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