Neuro Phosphates

Proprietary Name. It is an ingredient of Neuro Phosphates. Strychnidin-10-one... 

Both isomers of both serine and threonine are deaminated by Neuro-spora extracts 225-228). The enzymes involved have been purified by Yanofsky and his associates 225-228). A specific D-serine and D-threonine dehydrase has been purified thirty-five- to fortyfold from this mold 2f ). An absolute requirement for pyridoxal phosphate was demonstrated. No requirement for AMP or glutathione could be demonstrated. Some indication of a metal requirement was observed. The preparation was not active with the li-isomers of serine and threonine or DL-homoserine and DL-homo-cysteine. The rate of deamination of D-threonine is very slow compared to that with L-serine. Activity was observed with D-glutamic acid and D-as-partic acid. Since other D-amino acids were not deaminated by the preparation, these results could not be due to a contamination with D-amino acid oxidase. Furthermore, when either of these amino acids was incubated in the presence of D-serine, the keto acid production was a summation of that for each substrate alone. Pyridoxal phosphate had no effect on keto acid formation from the dicarboxylic amino acids. It is of interest that D-amino acid oxidase of Neurospora does not attack D-serine or D-threonine (77). 

The enzyme that catalyzes the conversion of 0-homoserine phosphate to threonine, threonine synthetase, has been purified 500-fold from Neuro-apora by Flavin and Slaughter (107). The purification procedure utilized acetone and ammonium sulfate precipitation tmd chromatography on a DEAE-cellulose column. 

---