EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.1.122 | gene C8orf32 | Homo sapiens |
3.5.1.122 | gene Cg8253 | Drosophila melanogaster |
3.5.1.122 | gene Cg8253 | Bos taurus |
3.5.1.122 | gene Ntaq1, DNA and amino acid sequence determination and analysis, mouse Hebp2 cDNA and Wdyhv1 cDNA are subcloned into the plasmid p425Met25, the FLAG-tagged mouse Hebp2f and Wdyhv1f are expressed in an nta1DELTA mutant of Saccharomyces cerevisiae that lacks the endogenous Nta1 NtN,Q-amidase activity. Recombinant transient expression of a mouse Ntaq1-EGFP fusion from the PCMV promoter transfected into NIH-3T3 cells. Recombinant expression of C-terminally His6-tagged mouse Ntaq1 in Pichia pastoris | Mus musculus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.5.1.122 | crystal structure analysis of C8orf32/Ntaq1 | Homo sapiens |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.5.1.122 | 26000 | - |
- |
Bos taurus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.122 | Bos taurus | Q3T0D3 | - |
- |
3.5.1.122 | Drosophila melanogaster | Q7K2Y9 | - |
- |
3.5.1.122 | Homo sapiens | Q96HA8 | - |
- |
3.5.1.122 | Mus musculus | Q80WB5 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.5.1.122 | native enzyme from a brain extract by ion exchange, hydrophobic chromatography, and gel filtration | Bos taurus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.5.1.122 | brain | - |
Bos taurus | - |
3.5.1.122 | additional information | varying levels of NtQ-amidase activity in all mouse tissues examined | Mus musculus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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 | - |
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 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.1.122 | ? | x * 26000, native enzyme, SDS-PAGE | Bos taurus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.122 | C8orf32 | - |
Homo sapiens |
3.5.1.122 | Cg8253 | - |
Drosophila melanogaster |
3.5.1.122 | FLJ10204 | - |
Homo sapiens |
3.5.1.122 | glutamine-specific N-terminal amidase | - |
Homo sapiens |
3.5.1.122 | glutamine-specific N-terminal amidase | - |
Drosophila melanogaster |
3.5.1.122 | glutamine-specific N-terminal amidase | - |
Mus musculus |
3.5.1.122 | glutamine-specific N-terminal amidase | - |
Bos taurus |
3.5.1.122 | NTAQ1 | - |
Homo sapiens |
3.5.1.122 | NTAQ1 | - |
Drosophila melanogaster |
3.5.1.122 | NTAQ1 | - |
Bos taurus |
3.5.1.122 | NTAQ1 | - |
Mus musculus |
3.5.1.122 | NtQ-amidase | - |
Homo sapiens |
3.5.1.122 | NtQ-amidase | - |
Drosophila melanogaster |
3.5.1.122 | NtQ-amidase | - |
Mus musculus |
3.5.1.122 | NtQ-amidase | - |
Bos taurus |
3.5.1.122 | Wdyhv1 | - |
Mus musculus |
3.5.1.122 | Wdyhv1 | - |
Bos taurus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
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 | Homo sapiens |
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 | Drosophila melanogaster |
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 | Mus musculus |
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 | Bos taurus |
3.5.1.122 | malfunction | a mutant in the Drosophila Cg8253 gene, encoding NtQ-amidase, has defective long-term memory | Drosophila melanogaster |
3.5.1.122 | malfunction | downregulation of Ntaq1 in mouse cells results in a decrease of NtQ-amidase activity | Mus musculus |
3.5.1.122 | metabolism | the enzyme is involved in the the N-end rule pathway, overview | Homo sapiens |
3.5.1.122 | metabolism | the enzyme is involved in the the N-end rule pathway, overview | Drosophila melanogaster |
3.5.1.122 | metabolism | the enzyme is involved in the the N-end rule pathway, overview | Mus musculus |
3.5.1.122 | metabolism | the enzyme is involved in the the N-end rule pathway, overview | Bos taurus |
3.5.1.122 | additional information | three-dimensional structure, mutational analysis, and mechanism of Ntaq1 NtQ-amidase, comparisons of mouse, human, and bovine enzymes, overview | Homo sapiens |
3.5.1.122 | additional information | three-dimensional structure, mutational analysis, and mechanism of Ntaq1 NtQ-amidase, comparisons of mouse, human, and bovine enzymes, overview | Mus musculus |
3.5.1.122 | additional information | three-dimensional structure, mutational analysis, and mechanism of Ntaq1 NtQ-amidase, comparisons of mouse, human, and bovine enzymes, overview | Bos taurus |