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Physiological concentrations of purines and pyrimidines
- T. Traut
- Chemistry, Medicine
- Molecular and Cellular Biochemistry
- 9 November 1994
Consideration of experiments on the intracellular compartmentation of nucleotides shows support for this process between the cytoplasm and mitochondria, but not between the cytoskeleton and the nucleus. Expand
A minimal gene set for cellular life derived by comparison of complete bacterial genomes
- T. Traut
The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites.
- T. Traut
- Biology, Medicine
- European journal of biochemistry
- 1 May 1994
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, finding three different sequence motifs that form the binding site for a nucleoside monophosphate (NMP). Expand
Inhibitors of orotate phosphoribosyl-transferase and orotidine-5'-phosphate decarboxylase from mouse Ehrlich ascites cells: a procedure for analyzing the inhibition of a multi-enzyme complex.
Abstract Orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase, the last two enzymes in the pathway for de novo pyrimidine biosynthesis, exist as a multi-enzyme complex in… Expand
Uracil metabolism--UMP synthesis from orotic acid or uridine and conversion of uracil to beta-alanine: enzymes and cDNAs.
The biochemical roles of carnosine and other dipeptides containing β-alanine are discussed in the chapter, and nucleotides presumably exist at very low concentrations in the extracellular environment, though no values have been published for their concentration in blood. Expand
Structure and inhibition of orotidine 5'-monophosphate decarboxylase from Plasmodium falciparum.
The structure of PfODCase was solved in the absence of ligand and displays a classic TIM-barrel fold characteristic of the enzyme, which may be associated with substrate capture and product release along the reaction pathway. Expand
Pyrimidine catabolism: individual characterization of the three sequential enzymes with a new assay.
A one-dimensional thin-layer chromatography procedure that resolves the initial substrate uracil and its catabolic derivatives dihydrouracil, N-carbamoyl-beta-alanine (NCBA) and beta-alanines and combined, these methods make it possible to assay easily and unambiguously, jointly or individually, all three enzyme activities of Uracil catabolism. Expand
Kinetic and conformational studies of the orotate phosphoribosyltransferase:orotidine-5'-phosphate decarboxylase enzyme complex from mouse Ehrlich ascites cells.
Complex U, the last two enzymes of the de nouo pathway for pyrimidine biosynthesis, can convert orotate to UMP so smoothly that OMP synthesized by the enzyme complex only partially equilibrates with a pool of exogenous OMP and is preferentially decar boxylated by the decarboxylase of complex U. Expand
Cloning and expression of a cDNA encoding uridine kinase from mouse brain.
The predicted secondary structure for uridine Kinase and the sequence comparison with three kinases having known crystal structures are consistent with uridine kinase having an alpha/beta core structure of the nucleotide-binding fold found in many kinases. Expand
Uridine kinase: altered enzyme with decreased affinities for uridine and CTP.
The characterization of an altered form of the enzyme with a single amino acid change, Q146R, within or near the uridine-binding site, which supports a model for CTP inhibition being caused by CTP binding backward at the catalytic site, as a bisubstrate analog. Expand