Purification and characterisation of NAD-glutamate dehydrogenase from Aspergillus nidulans.
NAD-Glutamate dehydrogenase has been purified from mycelia of A. nidulans. The enzyme comprises subunits of 110 kDa. It is located in the cytosol. It is completely denatured by 1.0 M guanidine hydrochloride, and is not renatured by subsequent dilution. Isophthalate is a strong competitive inhibitor and the enzyme is also inhibited by thiol reagents. The properties of the enzyme were compared to those from other fungi in terms of size, sensitivity to inhibitors, intracellular distribution and mode of regulation, and were found to resemble most closely those of Neurospora crassa.
Stevens
L
L
Department of Biological Science, University of Stirling, Scotland, U.K.
Duncan
D
D
Robertson
P
P
D001233:Aspergillus nidulans / Q000201:enzymology*; D001665:Binding Sites; D005969:Glutamate Dehydrogenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D009492:Neurospora crassa / Q000201:enzymology; D010795:Phthalic Acids / Q000494:pharmacology*; D011489:Protein Denaturation; D013045:Species Specificity; D013438:Sulfhydryl Compounds / Q000494:pharmacology
D010795:Phthalic Acids; D013438:Sulfhydryl Compounds; C059768:isophthalate; D005969:Glutamate Dehydrogenase