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Literature summary extracted from

  • Wang, H.; Piatkov, K.I.; Brower, C.S.; Varshavsky, A.
    Glutamine-specific N-terminal amidase, a component of the N-end rule pathway (2009), Mol. Cell, 34, 686-695.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.122 crystal structure analysis of C8orf32/Ntaq1 Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.122 26000
-
-
Bos taurus

Natural Substrates/ Products (Substrates)

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
-
?

Organism

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
-
-

Purification (Commentary)

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

Source Tissue

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
-

Substrates and Products (Substrate)

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
-
?

Subunits

EC Number Subunits Comment Organism
3.5.1.122 ? x * 26000, native enzyme, SDS-PAGE Bos taurus

Synonyms

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

General Information

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