Enzymatic activities of Ura2 and Ura1 proteins (aspartate carbamoyltransferase and dihydro‐orotate dehydrogenase) are present in both isolated membranes and cytoplasm of  Saccharomyces cerevisiae | Zendy

Voříšek J. | Zendy; Techniková Z. | Zendy; Schwippel J. | Zendy; Benoist P. | Zendy

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Enzymatic activities of Ura2 and Ura1 proteins (aspartate carbamoyltransferase and dihydro‐orotate dehydrogenase) are present in both isolated membranes and cytoplasm of Saccharomyces cerevisiae

Author(s) -

Voříšek J.,

Techniková Z.,

Schwippel J.,

Benoist P.

Publication year - 2002

Publication title -

yeast

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.923

H-Index - 102

eISSN - 1097-0061

pISSN - 0749-503X

DOI - 10.1002/yea.845

Subject(s) - aspartate carbamoyltransferase , biology , biochemistry , saccharomyces cerevisiae , enzyme , cytoplasm , dehydrogenase , yeast , membrane protein , biosynthesis , differential centrifugation , uridine , pyrimidine metabolism , membrane , rna , gene , allosteric regulation , purine

Computational analysis predicted three potential hydrophobic transmembrane α‐helices within the Ura2 multidomain protein of Saccharomyces cerevisiae , the C‐terminal subdomain of which catalyses the second step of uridine‐monophosphate biosynthesis by its L ‐aspartate carbamoyltransferase activity (EC 2.1.3.2). The fourth step of pyrimidine biosynthesis is catalysed by dihydro‐orotate dehydrogenase (Ura1 protein; EC 1.3.99.11), which was similarly characterized as a peripheral membrane protein. Ex situ , the activities of the investigated enzymes were associated both with isolated yeast membranes, fractionated by differential centrifugation to remove intact nuclei, and with soluble cytoplasmic proteins. Copyright © 2002 John Wiley & Sons, Ltd.

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