Studies on amino acid decarboxylases in Escherichia coli.
The isolation of highly active preparations of glutamate decarboxylase, arginine decarboxylase and histidine decarboxylase from Escherichia coli is described. These preparations showed strict specificity, and were in each case resolved into apo- and co-enzyme as shown by the significant restoration of activity that took place on addition of pyridoxal 5-phosphate.
D000596:Amino Acids; D002245:Carbon Dioxide; D002262:Carboxy-Lyases; D002474:Cell-Free System; D011232:Chemical Precipitation; D003956:Dialysis; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D011732:Pyridoxal Phosphate; D013053:Spectrophotometry; D013696:Temperature
D000596:Amino Acids; D002245:Carbon Dioxide; D011732:Pyridoxal Phosphate; D002262:Carboxy-Lyases