Open AccessPartial amino-acid sequence of NAD-specific glutamate dehydrogenase of Neurospora crassa.
Author(s) -
Brian Austen,
Joseph F. Nyc,
Yair Degani,
Emil L. Smith
Publication year - 1975
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.72.12.4891
Subject(s) - neurospora crassa , glutamate dehydrogenase , neurospora , nad+ kinase , biochemistry , oxidoreductase , biology , enzyme , glutamate synthase , protein subunit , amino acid , peptide sequence , glutamate receptor , gene , mutant , receptor
Parts of the primary structure of the NAD-specific glutamate dehydrogenase [L-glutamate:NAD oxidoreductase (deaminating), EC 1.4.1.2] from Neurospora crassa are presented. Segments of the sequence representing 886 unique amino-acid residues have been determined; the largest contains 267 residues. There are only short regions of possible homology between this enzyme and the glutamate dehydrogenases of bovine liver or the NADP-specific enzyme of Neurospora. The large size of the subunit (116,000 molecular weight) of the NAD-specific glutamate dehydrogenase is unusual when compared to other known dehydrogenases.