Abstract
Ten mutants of Aspergillus nidulans lacking nicotinamide adenine dinucleotide-specific glutamate dehydrogenase (NAD-GDH) have been isolated, and their mutations (gdhB1 through gdhB10) have been shown to lie in the gdhB gene. In addition, a temperature-sensitive gdhB mutant (gdhB11) has been isolated. A revertant (designated R-5) of the mutant gdhB1 bears an additional lesion in the gdhB gene and has altered NAD-GDH activity with altered Km values for ammonia or ammonium ions and for alpha-ketoglutarate. These results suggest that gdhB specifies a structural component for NAD-GDH. The growth characteristics of gdhB mutants indicate the routes by which amino acids are utilized as nitrogen and carbon energy sources. The properties are described of the double mutants bearing the mutations gdhB1 and gdhA1 or tamA119, which have low NADP-GDH activity.
Full text
PDF





Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Arst H. N., Jr, MacDonald D. W. A mutant of Asperigillus nidulans lacking NADP-linked glutamate dehydrogenase. Mol Gen Genet. 1973 May 9;122(3):261–265. doi: 10.1007/BF00278601. [DOI] [PubMed] [Google Scholar]
- Berberich M. A. A glutamate-dependent phenotype in E. coli K12: the result of two mutations. Biochem Biophys Res Commun. 1972 Jun 28;47(6):1498–1503. doi: 10.1016/0006-291x(72)90242-2. [DOI] [PubMed] [Google Scholar]
- Grenson M., Hou C. Ammonia inhibition of the general amino acid permease and its suppression in NADPH-specific glutamate dehydrogenaseless mutants of saccharomyces cerevisiae. Biochem Biophys Res Commun. 1972 Aug 21;48(4):749–756. doi: 10.1016/0006-291x(72)90670-5. [DOI] [PubMed] [Google Scholar]
- Hynes M. J. The effects of carbon source on glutamate dehydrogenase activities in Aspergillus nidulans. J Gen Microbiol. 1974 Mar;81(1):165–170. doi: 10.1099/00221287-81-1-165. [DOI] [PubMed] [Google Scholar]
- Kinghorn J. R., Pateman J. A. NAD and NADP l-glutamate dehydrogenase activity and ammonium regulation in Aspergillus nidulans. J Gen Microbiol. 1973 Sep;78(1):39–46. doi: 10.1099/00221287-78-1-39. [DOI] [PubMed] [Google Scholar]
- Kinghorn J. R., Pateman J. A. The effect of the carbon source on ammonium regulation in Aspergillus nidulans. Mol Gen Genet. 1974;128(1):95–98. doi: 10.1007/BF00267298. [DOI] [PubMed] [Google Scholar]
- Kinghorn J. R., Pateman J. A. The regulation of NAD L-glutamate dehydrogenase in Aspergillus nidulans. Genet Res. 1974 Feb;23(1):119–124. doi: 10.1017/s0016672300014713. [DOI] [PubMed] [Google Scholar]
- Kinghorn J. R., Pateman J. A. The structural gene for NADP L-glutamate dehydrogenase in Aspergillus nidulans. J Gen Microbiol. 1975 Feb;86(2):294–300. doi: 10.1099/00221287-86-2-294. [DOI] [PubMed] [Google Scholar]
- McCully K. S., Forbes E. The use of p-fluorophenylalanine with 'master strains' of Aspergillus nidulans for assigning genes to linkage groups. Genet Res. 1965 Nov;6(3):352–359. doi: 10.1017/s0016672300004249. [DOI] [PubMed] [Google Scholar]
- PONTECORVO G., ROPER J. A., HEMMONS L. M., MACDONALD K. D., BUFTON A. W. J. The genetics of Aspergillus nidulans. Adv Genet. 1953;5:141–238. doi: 10.1016/s0065-2660(08)60408-3. [DOI] [PubMed] [Google Scholar]
- Pateman J. A., Kinghorn J. R., Dunn E., Forbes E. Ammonium regulation in Aspergillus nidulans. J Bacteriol. 1973 Jun;114(3):943–950. doi: 10.1128/jb.114.3.943-950.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pateman J. A. Regulation of synthesis of glutamate dehydrogenase and glutamine synthetase in micro-organisms. Biochem J. 1969 Dec;115(4):769–775. doi: 10.1042/bj1150769. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Roon R. J., Even H. L., Larimore F. Glutamate synthase: properties of the reduced nicotinamide adenine dinucleotide-dependent enzyme from Saccharomyces cerevisiae. J Bacteriol. 1974 Apr;118(1):89–95. doi: 10.1128/jb.118.1.89-95.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Savageau M. A., Kotre A. M., Sakamoto N. A possible role in the regulation of primary animation for a complex of glutamine: -ketoglutarate amidotransferase and glutamate dehydrogenase in Escherichia coli. Biochem Biophys Res Commun. 1972 Jul 11;48(1):41–47. doi: 10.1016/0006-291x(72)90341-5. [DOI] [PubMed] [Google Scholar]
- Willetts A. J. Metabolism of threonine by penicillia: growth on threonine as the sole carbon and nitrogen source. J Gen Microbiol. 1972 Nov;73(1):71–83. doi: 10.1099/00221287-73-1-71. [DOI] [PubMed] [Google Scholar]