EC Number   |
General Information |
Reference |
|---|
  3.5.1.122 | evolution |
Ntaq1 and its crystal structure indicate that the active site and catalytic mechanism of NtQ-amidase are similar to those of transglutaminases |
741003 |
| 3.5.1.122 | evolution |
the catalytic triad, comprising Cys28, His81, and Asp97, is highly conserved among Ntaq proteins, transglutaminases, and cysteine proteases of diverse organisms |
741295 |
| 3.5.1.122 | malfunction |
a mutant in the Drosophila Cg8253 gene, encoding NtQ-amidase, has defective long-term memory |
741003 |
| 3.5.1.122 | malfunction |
downregulation of Ntaq1 in mouse cells results in a decrease of NtQ-amidase activity |
741003 |
| 3.5.1.122 | metabolism |
the enzyme is involved in the the N-end rule pathway, overview |
741003 |
| 3.5.1.122 | 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, overview |
741343 |
| 3.5.1.122 | more |
substrate binding structure, molecular docking studies of tripeptides with N-terminal glutamine, overview. Upon binding of a substrate with N-terminal glutamine, active site catalytic triad mediates the deamination of the N-terminal residue to glutamate by a mechanism analogous to that of cysteine proteases. Active site structure, ooverview |
741295 |
| 3.5.1.122 | more |
three-dimensional structure, mutational analysis, and mechanism of Ntaq1 NtQ-amidase, comparisons of mouse, human, and bovine enzymes, overview |
741003 |
| 3.5.1.122 | physiological function |
enzyme Ntaq is an initial component of the N-end rule pathway and converts N-terminal glutamine to glutamate |
741295 |
| 3.5.1.122 | physiological function |
the enzyme controls the expression of specific defence-response genes, activates the synthesis pathway for the phytoalexin camalexin and influences basal resistance to the hemibiotroph pathogen Pseudomonas syringae pv tomato |
754918 |
