Open AccessPurification and characterisation of NAD‐glutamate dehydrogenase from Aspergillus nidulans
Author(s) -
Stevens Lewis,
Duncan Doris,
Robertson Patricia
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03294.x
Subject(s) - aspergillus nidulans , neurospora crassa , glutamate dehydrogenase , nad+ kinase , biochemistry , guanidine , enzyme , neurospora , dehydrogenase , biology , chemistry , glutamate receptor , receptor , gene , mutant
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 .