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Literature summary for 3.5.1.122 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)

Cloned (Comment) Organism
gene C8orf32 Homo sapiens
gene Cg8253 Drosophila melanogaster
gene Cg8253 Bos taurus
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)

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-terminal L-glutaminyl-[protein] + H2O Homo sapiens
-
N-terminal L-glutamyl-[protein] + NH3
-
?
N-terminal L-glutaminyl-[protein] + H2O Drosophila melanogaster
-
N-terminal L-glutamyl-[protein] + NH3
-
?
N-terminal L-glutaminyl-[protein] + H2O Mus musculus
-
N-terminal L-glutamyl-[protein] + NH3
-
?
N-terminal L-glutaminyl-[protein] + H2O Bos taurus
-
N-terminal L-glutamyl-[protein] + NH3
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus Q3T0D3
-
-
Drosophila melanogaster Q7K2Y9
-
-
Homo sapiens Q96HA8
-
-
Mus musculus Q80WB5
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from a brain extract by ion exchange, hydrophobic chromatography, and gel filtration Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Bos taurus
-
additional information varying levels of NtQ-amidase activity in all mouse tissues examined Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
N-terminal L-glutaminyl-[protein] + H2O
-
Homo sapiens N-terminal L-glutamyl-[protein] + NH3
-
?
N-terminal L-glutaminyl-[protein] + H2O
-
Drosophila melanogaster N-terminal L-glutamyl-[protein] + NH3
-
?
N-terminal L-glutaminyl-[protein] + H2O
-
Mus musculus N-terminal L-glutamyl-[protein] + NH3
-
?
N-terminal L-glutaminyl-[protein] + H2O
-
Bos taurus N-terminal L-glutamyl-[protein] + NH3
-
?

Subunits

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

Synonyms

Synonyms Comment Organism
C8orf32
-
Homo sapiens
Cg8253
-
Drosophila melanogaster
FLJ10204
-
Homo sapiens
glutamine-specific N-terminal amidase
-
Homo sapiens
glutamine-specific N-terminal amidase
-
Drosophila melanogaster
glutamine-specific N-terminal amidase
-
Mus musculus
glutamine-specific N-terminal amidase
-
Bos taurus
NTAQ1
-
Homo sapiens
NTAQ1
-
Drosophila melanogaster
NTAQ1
-
Bos taurus
NTAQ1
-
Mus musculus
NtQ-amidase
-
Homo sapiens
NtQ-amidase
-
Drosophila melanogaster
NtQ-amidase
-
Mus musculus
NtQ-amidase
-
Bos taurus
Wdyhv1
-
Mus musculus
Wdyhv1
-
Bos taurus

General Information

General Information Comment Organism
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
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
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
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
malfunction a mutant in the Drosophila Cg8253 gene, encoding NtQ-amidase, has defective long-term memory Drosophila melanogaster
malfunction downregulation of Ntaq1 in mouse cells results in a decrease of NtQ-amidase activity Mus musculus
metabolism the enzyme is involved in the the N-end rule pathway, overview Homo sapiens
metabolism the enzyme is involved in the the N-end rule pathway, overview Drosophila melanogaster
metabolism the enzyme is involved in the the N-end rule pathway, overview Mus musculus
metabolism the enzyme is involved in the the N-end rule pathway, overview Bos taurus
additional information three-dimensional structure, mutational analysis, and mechanism of Ntaq1 NtQ-amidase, comparisons of mouse, human, and bovine enzymes, overview Homo sapiens
additional information three-dimensional structure, mutational analysis, and mechanism of Ntaq1 NtQ-amidase, comparisons of mouse, human, and bovine enzymes, overview Mus musculus
additional information three-dimensional structure, mutational analysis, and mechanism of Ntaq1 NtQ-amidase, comparisons of mouse, human, and bovine enzymes, overview Bos taurus