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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.