EC Number   |
General Information |
Reference |
|---|
   3.5.1.121 | malfunction |
hNTAN1 is shown to possess a critical Cys residue that is absolutely required for catalysis, corroborated in part by abolishment of activity through the Cys75Ala point mutation |
740050 |
| 3.5.1.121 | malfunction |
Ntan1-/- mice lack NtN-amidase and the asparagine-specific branch of the N-end rule pathway. The phenoytpe shows altered activity, social behavior, and spatial memory in mice lacking the NTAN1p amidase and the asparagine branch of the N-end rule pathway. The Ntan1-/- mouse strains lacking the NtN-amidase activity but retaining glutamine-specific NtQ amidase, EC 3.5.1.122, show that the two enzymes are encoded by different genes. Among the normally short-lived N-end rule substrates, only those bearing N-terminal asparagine became long-lived in Ntan1-/- fibroblasts. The Ntan1-/- mice are fertile and outwardly normal but differ from their congenic wild-type counterparts in spontaneous activity, spatial memory, and a socially conditioned exploratory phenotype |
-, 740991 |
| 3.5.1.121 | malfunction |
NTAN1-deficient mice are better than wild-type mice on black-white and horizontal-vertical discrimination learning. They are also better at 8-week Morris maze retention testing when a reversal trial is not included in the testing procedures. In all three tasks NTAN1-deficient mice appear to use a strong win-stay strategy. It is concluded that inactivating the asparagine-specific branch of the N-end rule pathway in mice results in impaired spatial learning with concomitant compensatory restructuring of the nervous system in favor of non-spatial (stimulus-response) learning |
-, 740246 |
| 3.5.1.121 | malfunction |
recombinant mouse NtN-amidase enzyme expressed in an enzyme-mutant Saccharomyces cerevisiae strain can implement the asparagine-specific subset of the yeast N-end rule |
740657 |
| 3.5.1.121 | metabolism |
the enzyme is involved in the mammalian N-end rule pathway |
740050, 740888 |
| 3.5.1.121 | metabolism |
the enzyme is involved in the mammalian N-end rule pathway, comparison of enzymatic reactions that underlie the activity of N-dt and N-ds residues in the N-end rule pathways of different organisms, overview |
-, 740657 |
| 3.5.1.121 | metabolism |
the enzyme is involved in the mammalian N-end rule pathway, overview |
-, 740246 |
| 3.5.1.121 | metabolism |
the enzyme is involved in the mammalian N-end rule pathway. The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. N-terminal asparagine and glutamine are tertiary destabilizing residues, in that they are enzymatically deamidated to yield secondary destabilizing residues aspartate and glutamate, which are conjugated to arginine, a primary destabilizing residue |
-, 740991 |
| 3.5.1.121 | metabolism |
the enzyme is involved in the N-end rule-mediated degradation in eukaryotic cells, pathway overview |
740655 |
| 3.5.1.121 | metabolism |
the first step of the hierarchically organized Arg/N-end rule pathway of protein degradation is deamidation of the N-terminal glutamine and asparagine residues of substrate proteins to glutamate and aspartate, respectively. These reactions are catalyzed by the N-terminal amidase (Nt-amidase) Nta1 in fungi such as Saccharomyces cerevisiae, and by the glutamine-specific Ntaq1 and asparagine-specific Ntan1 Nt-amidases in mammals. Specific deamidation mechanisms in the first step of the N-end rule pathway |
741343 |
