PAPS-reductase from Escherichia coli: characterization of the enzyme as probe for thioredoxins.
PAPS-reductase from Escherichia coli was employed to detect thioredoxins from pro- and eukaryotic organisms. A simple method for the isolation of this enzyme and properties of the enzymatic assay were described. A comparison between thioredoxins detected by the PAPS-reductase and the Fructose-bisphosphatase or NADP malate dehydrogenase was used to assess the validity of the test. The high cross-reactivity of the bacterial enzyme was useful in the purification of heterologous thioredoxins from spinach, Synechococcus, and Saccharomyces cerevisiae.
D001426:Bacterial Proteins / Q000032:analysis*; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D010944:Plants / Q000032:analysis; D013879:Thioredoxins / Q000032:analysis* / Q000378:metabolism
D001426:Bacterial Proteins; D013879:Thioredoxins; D010088:Oxidoreductases; C052449:3'-phosphoadenylyl-5'-phosphosulfate reductase