3.5.1.121: protein N-terminal asparagine amidohydrolase
This is an abbreviated version!
For detailed information about protein N-terminal asparagine amidohydrolase, go to the full flat file.
Word Map on EC 3.5.1.121
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3.5.1.121
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deamidation
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asparagine-specific
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e3alpha
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outwardly
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r2r3-myb
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lashley
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glutamine-specific
- 3.5.1.121
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deamidation
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asparagine-specific
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e3alpha
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outwardly
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r2r3-myb
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lashley
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glutamine-specific
Reaction
Synonyms
amidohydrolase for N-terminal asparagine, N-terminal amidase, N-terminal asparagine amidohydrolase, Nt-amidase, NTA1, NTAN1, NTAN1 amidase, NTAN1p amidase, NtN-amidase, PNAD, protein NH2-terminal asparagine deamidase, yNta1
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General Information
General Information on EC 3.5.1.121 - protein N-terminal asparagine amidohydrolase
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malfunction
metabolism
physiological function
hNTAN1 is shown to possess a critical Cys residue that is absolutely required for catalysis, corroborated in part by abolishment of activity through the Cys75Ala point mutation
malfunction
Ntan1-/- mice lack NtN-amidase and the asparagine-specific branch of the N-end rule pathway. The phenoytpe shows altered activity, social behavior, and spatial memory in mice lacking the NTAN1p amidase and the asparagine branch of the N-end rule pathway. The Ntan1-/- mouse strains lacking the NtN-amidase activity but retaining glutamine-specific NtQ amidase, EC 3.5.1.122, show that the two enzymes are encoded by different genes. Among the normally short-lived N-end rule substrates, only those bearing N-terminal asparagine became long-lived in Ntan1-/- fibroblasts. The Ntan1-/- mice are fertile and outwardly normal but differ from their congenic wild-type counterparts in spontaneous activity, spatial memory, and a socially conditioned exploratory phenotype
malfunction
NTAN1-deficient mice are better than wild-type mice on black-white and horizontal-vertical discrimination learning. They are also better at 8-week Morris maze retention testing when a reversal trial is not included in the testing procedures. In all three tasks NTAN1-deficient mice appear to use a strong win-stay strategy. It is concluded that inactivating the asparagine-specific branch of the N-end rule pathway in mice results in impaired spatial learning with concomitant compensatory restructuring of the nervous system in favor of non-spatial (stimulus-response) learning
malfunction
recombinant mouse NtN-amidase enzyme expressed in an enzyme-mutant Saccharomyces cerevisiae strain can implement the asparagine-specific subset of the yeast N-end rule
malfunction
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NTAN1-deficient mice are better than wild-type mice on black-white and horizontal-vertical discrimination learning. They are also better at 8-week Morris maze retention testing when a reversal trial is not included in the testing procedures. In all three tasks NTAN1-deficient mice appear to use a strong win-stay strategy. It is concluded that inactivating the asparagine-specific branch of the N-end rule pathway in mice results in impaired spatial learning with concomitant compensatory restructuring of the nervous system in favor of non-spatial (stimulus-response) learning
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malfunction
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Ntan1-/- mice lack NtN-amidase and the asparagine-specific branch of the N-end rule pathway. The phenoytpe shows altered activity, social behavior, and spatial memory in mice lacking the NTAN1p amidase and the asparagine branch of the N-end rule pathway. The Ntan1-/- mouse strains lacking the NtN-amidase activity but retaining glutamine-specific NtQ amidase, EC 3.5.1.122, show that the two enzymes are encoded by different genes. Among the normally short-lived N-end rule substrates, only those bearing N-terminal asparagine became long-lived in Ntan1-/- fibroblasts. The Ntan1-/- mice are fertile and outwardly normal but differ from their congenic wild-type counterparts in spontaneous activity, spatial memory, and a socially conditioned exploratory phenotype
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metabolism
the enzyme is involved in the mammalian N-end rule pathway, comparison of enzymatic reactions that underlie the activity of N-dt and N-ds residues in the N-end rule pathways of different organisms, overview
metabolism
the enzyme is involved in the mammalian N-end rule pathway, comparison of enzymatic reactions that underlie the activity of N-dt and N-ds residues in the N-end rule pathways of different organisms, overview
metabolism
the enzyme is involved in the mammalian N-end rule pathway, overview
metabolism
the enzyme is involved in the mammalian N-end rule pathway. The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. N-terminal asparagine and glutamine are tertiary destabilizing residues, in that they are enzymatically deamidated to yield secondary destabilizing residues aspartate and glutamate, which are conjugated to arginine, a primary destabilizing residue
metabolism
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the enzyme is involved in the N-end rule-mediated degradation in eukaryotic cells, pathway overview
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
metabolism
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the enzyme is involved in the mammalian N-end rule pathway, overview
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metabolism
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the enzyme is involved in the mammalian N-end rule pathway, comparison of enzymatic reactions that underlie the activity of N-dt and N-ds residues in the N-end rule pathways of different organisms, overview
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metabolism
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the enzyme is involved in the mammalian N-end rule pathway. The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. N-terminal asparagine and glutamine are tertiary destabilizing residues, in that they are enzymatically deamidated to yield secondary destabilizing residues aspartate and glutamate, which are conjugated to arginine, a primary destabilizing residue
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conversion of the resulting NH2-terminal asparagine to aspartic acid by enzyme PNAD renders the protein susceptible to arginylation, polyubiquitinylation and degradation as specified by the N-end rule. Proteins beginning with Met-Asp, Met-Glu, and Met-Asn sequences are Nalpha-acetylated, while those beginning with Met-Gln sequences are not. The enzyme protein NH2-terminal asparagine deamidase (PNAD) catalyzes the specific deamidation of peptide-bound NH2-terminal asparagine residues
physiological function
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Ntan1 (amidohydrolase for N-terminal asparagine) is a magnetism responsive gene in rat brain. Ntan1 is an essential component of a protein degradation signal, which is a destabilizing N-terminal residue of a protein, in the N-end rule. Overexpression of gene Ntan1 results in a marked decrease in the MAP2 protein expression in hippocampal neurons. Brief magnetism leads to the induction of Ntan1 responsible for MAP2 protein degradation through ubiquitin-proteasome pathway in rat hippocampal neurons
physiological function
the enzymatic deamidation of N-terminal L-Asn by N-terminal asparagine amidohydrolase (NTAN1) is a feature of the ubiquitin-dependent N-end rule pathway of protein degradation, which relates the in vivo half-life of a protein to the identity of its N-terminal residue. hNTAN1 is shown to possess a critical Cys residue that is absolutely required for catalysis, corroborated in part by abolishment of activity through the Cys75Ala point mutation. The exposure of a conserved L-Pro at the N-terminus of hNTAN1 following removal of the initiating L-Met is important for the function of the enzyme
physiological function
the N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. In mammals, the tertiary destabilizing N-terminal residues asparagine and glutamine function through their conversion, by enzymatic deamidation, into the secondary destabilizing residues aspartate and glutamate, whose destabilizing activity requires their enzymatic conjugation to arginine, one of the primary destabilizing residues. The NtN-amidase is a 310-residue amidohydrolase specific for N-terminal asparagine. Recombinant NtN-amidase retains its asparagine selectivity in vivo and can implement the asparagine-specific subset of the N-end rule
physiological function
the N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. In mammals, the tertiary destabilizing N-terminal residues asparagine and glutamine function through their conversion, by enzymatic deamidation, into the secondary destabilizing residues aspartate and glutamate, whose destabilizing activity requires their enzymatic conjugation to arginine, one of the primary destabilizing residues. The NtN-amidase is a 310-residue amidohydrolase specific for N-terminal asparagine. Recombinant NtN-amidase retains its asparagine selectivity in vivo and can implement the asparagine-specific subset of the N-end rule
physiological function
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the N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. In mammals, the tertiary destabilizing N-terminal residues asparagine and glutamine function through their conversion, by enzymatic deamidation, into the secondary destabilizing residues aspartate and glutamate, whose destabilizing activity requires their enzymatic conjugation to arginine, one of the primary destabilizing residues. The NtN-amidase is a 310-residue amidohydrolase specific for N-terminal asparagine. Recombinant NtN-amidase retains its asparagine selectivity in vivo and can implement the asparagine-specific subset of the N-end rule
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