| Autor: |
B M Austen, M.E. Haberland, Joseph F. Nyc, Emil L. Smith |
| Rok vydání: |
1977 |
| Předmět: |
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| Zdroj: |
Journal of Biological Chemistry. 252:8142-8149 |
| ISSN: |
0021-9258 |
| DOI: |
10.1016/s0021-9258(17)40950-1 |
| Popis: |
A sequence is presented for the COOH-terminal 669 residues of the NAD-specific glutamate dehydrogenase of Neurospora crassa. Comparison of this sequence with those of the vertebrate glutamate dehydrogenases of chicken and bovine liver and with the NADP-specific enzyme of Neurospora shows some similarities in sequences around residues previously identified as important for the function of these enzymes. These are: (a) the reactive lysine residue of low pK in the NADP and the vertebrate enzymes; (b) the tyrosine residue of the NADP enzyme that is readily nitrated by tetranitromethane with inactivation, a residue protected by NADP or by NMN; and (c) the arginine residue of the NADP-enzyme that is reactive with 1,2-cyclohexanedione with inactivation. Despite these similarities, comparison of the sequence of the NAD-enzyme with those of the other glutamate dehydrogenases of known sequences revealed relatively little overall homology as determined by computer analysis. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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