Comparison of a nitrate reductase-inactivating enzyme from the maize root with a protease form yeast which inactivates tryptophan synthase.
A maize root fraction which inactivates nitrate reductase has been shown to have protease activity which can be measured by the hydrolysis of azocasein. This inactivating enzyme was also found to inactivate yeast tryptophan synthase. Yeast proteases A and B, which inactivate this latter enzyme, also gave a specific inactivation of the maize nitrate reductase. The maize root inactivating enzyme, like yeast protease B, degraded casein, and was inhibited by phenylmethylsulphonyl fluoride. A partially-purified yeast inhibitor prevented catalysis by the yeast proteases and maize root inactivating enzyme, but purified yeast inhibitors were without effect on the latter protein. The level of nitrate reductase-inactivating activity, and associated azocasein-degrading activity, increased with age of the maize root. Evidence was obtained for a heat stable inhibitor which maintained them in an inactive state, especially in the young root tip cells.
D007700:Kinetics; D009565:Nitrate Reductases / Q000037:antagonists & inhibitors*; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000494:pharmacology*; D010944:Plants / Q000201:enzymology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D014367:Tryptophan Synthase / Q000037:antagonists & inhibitors*; D003313:Zea mays / Q000201:enzymology
D009565:Nitrate Reductases; D010447:Peptide Hydrolases; D014367:Tryptophan Synthase