Enzymatic activities of Ura2 and Ura1 proteins (aspartate carbamoyltransferase and dihydro-orotate dehydrogenase) are present in both isolated membranes and cytoplasm of Saccharomyces cerevisiae
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
11921093
DOI
10.1002/yea.845
PII: 10.1002/yea.845
Knihovny.cz E-resources
- MeSH
- Aspartate Carbamoyltransferase biosynthesis metabolism MeSH
- Cell Membrane enzymology MeSH
- Cytoplasm enzymology MeSH
- Dihydroorotate Dehydrogenase MeSH
- Fluorescent Dyes chemistry MeSH
- Indoles chemistry MeSH
- Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) biosynthesis metabolism MeSH
- Molecular Sequence Data MeSH
- Multienzyme Complexes biosynthesis metabolism MeSH
- Oxidoreductases Acting on CH-CH Group Donors * MeSH
- Oxidoreductases biosynthesis metabolism MeSH
- Saccharomyces cerevisiae Proteins * MeSH
- Saccharomyces cerevisiae enzymology physiology MeSH
- Protein Structure, Secondary MeSH
- Amino Acid Sequence MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Aspartate Carbamoyltransferase MeSH
- DAPI MeSH Browser
- Dihydroorotate Dehydrogenase MeSH
- Fluorescent Dyes MeSH
- Indoles MeSH
- Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) MeSH
- Multienzyme Complexes MeSH
- Oxidoreductases Acting on CH-CH Group Donors * MeSH
- Oxidoreductases MeSH
- Saccharomyces cerevisiae Proteins * MeSH
- URA2 protein, S cerevisiae MeSH Browser
Computational analysis predicted three potential hydrophobic transmembrane alpha-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.
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