RT Journal Article SR Electronic(1) A1 Nicholas, D. J. D. A1 Mabey, G. L.YR 1960 T1 Some Properties of Glutamic Dehydroǵenase from Neurospora crassa JF Microbiology, VO 22 IS 1 SP 184 OP 190 DO https://doi.org/10.1099/00221287-22-1-184 PB Microbiology Society, SN 1465-2080, AB SUMMARY: A glutamic dehydrogenase from Neurospora requiring either DPNH or TPNH for activity has a pH optimum of 8·6 and is inhibited by a number of chelating agents. The specific activity of the enzyme was high during early growth, but it fell sharply from the 2nd to the 5th day after inoculation. A deficiency of Zn decreased enzyme activity and addition of the metal in vivo to Zn-deficient mycelial felts restored the enzyme to normal values after a few days of incubation. The enzyme was unchanged when pyridoxine or riboflavin was limiting in the growth of mutants which require these vitamins. With a purified enzyme the Km values in mole/l. were as follows: α-ketoglutarate 0·75 × 107#x2212;2; TPNH, 2 × l0−4; and DPNH, 2·3 × 10−4., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-22-1-184