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pro vyhledávání: '"Thomas W. Traut"'
Autor:
Thomas W. Traut
Publikováno v:
eLS
Nucleosides are composed of a heterocyclic ring (defined as the base) that is attached to a ribose. Addition of a phosphate to a nucleoside, at carbon 5 of the ribose, produces a nucleotide. Nucleotides function as ubiquitous building blocks for the
Autor:
Thomas W. Traut
Publikováno v:
eLS
Cells can respond to changes in their environment by altering the flow through special, regulated metabolic steps performed by allosteric enzymes. These enzymes adopt either an active or inactive conformation in response to binding positive or negati
Autor:
Brenda Temple, Thomas W. Traut
Publikováno v:
Journal of Biological Chemistry. 275:28675-28681
Orotidine 5'-phosphate (OMP) decarboxylase has the largest rate enhancement for any known enzyme. For an average protein of 270 amino acids from more than 80 species, only 8 amino acids are invariant, and 7 of these correspond to ligand-binding resid
Publikováno v:
Bioorganic Chemistry. 26:283-288
To evaluate the effects of individual binding determinants on transition state stabilization, the binding properties of substrates and competitive inhibitors of the OMP decarboxylase activity of human UMP synthase were compared with those of fragment
Autor:
Patricia A. Ropp, Thomas W. Traut
Publikováno v:
Archives of Biochemistry and Biophysics. 336:105-112
Uridine kinase is the rate-limiting enzyme in the pyrimidine salvage pathway of all mammalian cells. A cDNA for uridine kinase from mouse brain has been isolated, sequenced, and characterized. This is the first report of a complete nucleotide sequenc
Autor:
Thomas W. Traut
Publikováno v:
European Journal of Biochemistry. 222:9-19
From an analysis of current data on 16 protein structures with defined nucleotide-binding sites consensus motifs were determined for the peptide segments that form such nucleotide-binding sites. This was done by using the actual residues shown to con
Publikováno v:
Journal of Biological Chemistry. 268:5686-5693
A cDNA for beta-alanine synthase from rat liver has been isolated, sequenced, and characterized. beta-Alanine synthase clones were isolated from rat liver cDNA libraries in lambda gt11, using affinity-purified polyclonal antibodies against beta-alani
Publikováno v:
Archives of Biochemistry and Biophysics. 293:254-263
beta-Alanine synthase has been purified greater than 1000-fold to homogeneity from rat liver. The enzyme has a subunit molecular weight of 42,000 and a native size of hexamer. The enzyme undergoes ligand-induced changes in polymerization: association
Autor:
Patricia A. Ropp, Thomas W. Traut
Publikováno v:
Archives of Biochemistry and Biophysics. 288:614-620
Purine nucleoside phosphorylase (EC 2.4.2.1) from bovine spleen is allosterically regulated. With the substrate inosine the enzyme displayed complex kinetics: positive cooperativity vs inosine when this substrate was close to physiological concentrat
Autor:
Thomas W. Traut, Hiu Chuen Lok, Maryam Shojaei, Camilla Chan, David B. Langley, Richard I. Christopherson, J. Mitchell Guss, Joel P. Mackay
Publikováno v:
Biochemistry. 47(12)
Orotidine 5'-monophosphate (OMP) decarboxylase from Plasmodium falciparum (PfODCase, EC 4.1.1.23) has been overexpressed, purified, subjected to kinetic and biochemical analysis, and crystallized. The native enzyme is a homodimer with a subunit molec