EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
  3.5.1.122 | more |
dual specificity of yeast Nta1 (yNta1), importance of second-position residues in Asn/Gln-bearing N-terminal degradation signals (N-degrons), also cf. EC 3.5.1.121. Specific hydrogen bonds stabilize interactions between N-degron peptides and hydrophobic peripheral regions of the active site pocket, interactions between Nta1 and N-degron peptides, detailed overview. The enzyme shows glutamine-specific enzyme activity with dipeptides Gln-Val and Gln-Gly, Michaelis-Menten kinetics |
Saccharomyces cerevisiae |
? |
- |
? |
| 3.5.1.122 | more |
the amidohydrolase activity of the native enzyme and of proteolytic fragments is analyzed using either L-glutamine or gamma-L-glutamic 4-nitroanilide as substrates |
Escherichia coli |
? |
- |
? |
| 3.5.1.122 | N-terminal L-glutaminyl-[DHFRbt] + H2O |
substrate is Escherichia coli dihydrofolate reductase (DHFR) moiety fused to a C-terminal peptide (denoted as bt) that is biotinylated in vivo |
Mus musculus |
N-terminal L-glutamyl-[DHFRbt] + NH3 |
- |
? |
| 3.5.1.122 | N-terminal L-glutaminyl-[protein] + H2O |
- |
Saccharomyces cerevisiae |
N-terminal L-glutamyl-[protein] + NH3 |
- |
? |
| 3.5.1.122 | N-terminal L-glutaminyl-[protein] + H2O |
- |
Homo sapiens |
N-terminal L-glutamyl-[protein] + NH3 |
- |
? |
| 3.5.1.122 | N-terminal L-glutaminyl-[protein] + H2O |
- |
Drosophila melanogaster |
N-terminal L-glutamyl-[protein] + NH3 |
- |
? |
| 3.5.1.122 | N-terminal L-glutaminyl-[protein] + H2O |
- |
Mus musculus |
N-terminal L-glutamyl-[protein] + NH3 |
- |
? |
| 3.5.1.122 | N-terminal L-glutaminyl-[protein] + H2O |
- |
Bos taurus |
N-terminal L-glutamyl-[protein] + NH3 |
- |
? |
| 3.5.1.122 | QKGSGAW + H2O |
- |
Arabidopsis thaliana |
EKGSGAW + NH3 |
- |
? |
| 3.5.1.122 | QLGSGAW + H2O |
about 80% of the activity compared to QKGSGAW |
Arabidopsis thaliana |
ELGSGAW + NH3 |
- |
? |
