Selenium-dependent glycine reductase: differences in physicochemical properties and biological activities of selenoprotein A components isolated from Clostridium sticklandii and Clostridium purinolyticum.
The selenoprotein A component of the glycine reductase complex of Clostridium sticklandii was shown to differ in certain properties from the selenoprotein A produced by a purine-fermenting organism, Clostridium purinolyticum. Both proteins contain one selenocysteine and two cysteine residues.
Sliwkowski
M X
MX
Laboratory of Biochemistry, National Institutes of Health, Bethesda, MD 20892.
Stadtman
T C
TC
D000594:Amino Acid Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003013:Clostridium / Q000201:enzymology*; D007700:Kinetics; D009097:Multienzyme Complexes / Q000302:isolation & purification / Q000378:metabolism*; D012643:Selenium / Q000378:metabolism*; D051140:Selenoproteins; D013045:Species Specificity
D000596:Amino Acids; D001426:Bacterial Proteins; D009097:Multienzyme Complexes; D051140:Selenoproteins; C054667:selenoprotein A; D000594:Amino Acid Oxidoreductases; C020815:glycine reductase; D012643:Selenium