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Information on EC 3.5.1.121 - protein N-terminal asparagine amidohydrolase
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EC Tree
3.5.1.121 protein N-terminal asparagine amidohydrolaseIUBMB Comments
This enzyme participates in the eukaryotic ubiquitin-dependent Arg/N-end rule pathway of protein degradation, promoting the turnover of intracellular proteins that initiate with Met-Asn. Following the acetylation and removal of the initiator methionine, the exposed N-terminal asparagine is deaminated, resulting in its conversion to L-aspartate. The latter serves as a substrate for EC 2.3.2.8, arginyltransferase, making the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule.
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Word Map
- 3.5.1.121
-
deamidation
-
asparagine-specific
-
e3alpha
-
outwardly
-
r2r3-myb
-
lashley
-
glutamine-specific
The enzyme appears in viruses and cellular organisms
Reaction Schemes
N-terminal L-asparaginyl-[protein]
+
=
N-terminal L-aspartyl-[protein]
+
Synonyms
ntan1, n-terminal amidase, nt-amidase, n-terminal asparagine amidohydrolase, ntn-amidase, ynta1, ntan1 amidase, protein nh2-terminal asparagine deamidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NTAN1
NTAN1 amidase
NTAN1p amidase
NtN-amidase
NTAN1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-terminal L-asparaginyl-[protein] + H2O = N-terminal L-aspartyl-[protein] + NH3
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
protein N-terminal asparagine amidohydrolase
This enzyme participates in the eukaryotic ubiquitin-dependent Arg/N-end rule pathway of protein degradation, promoting the turnover of intracellular proteins that initiate with Met-Asn. Following the acetylation and removal of the initiator methionine, the exposed N-terminal asparagine is deaminated, resulting in its conversion to L-aspartate. The latter serves as a substrate for EC 2.3.2.8, arginyltransferase, making the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
Asp-DHFR protein bearing Asn at its N-terminus is used as substrate
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
purified, 35S-labeled X DHFR protein bearing Asn at its N-terminus is used as substrate
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
purified, 35S-labeled X DHFR protein bearing Asn at its N-terminus is used as substrate
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
Asp-DHFR protein bearing Asn at its N-terminus is used as substrate
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
purified, 35S-labeled X DHFR test proteins bearing either Asn, Gln, or Asp at their N termini are used as substrates
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
the enzyme specifically converts NH2-terminal asparagine residues of peptide and protein substrate to aspartic acid
-
-
?
additional information
?
-
hNTAN1 is highly selective for the hydrolysis of N-terminal peptidyl L-Asn but fails to deamidate free L-Asn or L-Gln, N-terminal peptidyl L-Gln, or acetylated N-terminal peptidyl L-Asn
-
-
?
additional information
?
-
-
hNTAN1 is highly selective for the hydrolysis of N-terminal peptidyl L-Asn but fails to deamidate free L-Asn or L-Gln, N-terminal peptidyl L-Gln, or acetylated N-terminal peptidyl L-Asn
-
-
?
additional information
?
-
the NtN-amidase is a 310-residue amidohydrolase from Mus musculus is specific for N-terminal asparagine
-
-
?
additional information
?
-
-
the NtN-amidase is a 310-residue amidohydrolase from Mus musculus is specific for N-terminal asparagine
-
-
?
additional information
?
-
the NtN-amidase is a 310-residue amidohydrolase from Mus musculus is specific for N-terminal asparagine
-
-
?
additional information
?
-
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 asparagine-specific enzyme activity with dipeptides An-Val and Asn-Gly, Michaelis-Menten kinetics
-
-
?
additional information
?
-
-
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 asparagine-specific enzyme activity with dipeptides An-Val and Asn-Gly, Michaelis-Menten kinetics
-
-
?
additional information
?
-
the NTA1-encoded Nt-amidase of Saccharomyces cerevisiae can deamidate N-terminal Asn or Gln, cf. EC 3.5.1.122
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-
?
additional information
?
-
-
the NTA1-encoded Nt-amidase of Saccharomyces cerevisiae can deamidate N-terminal Asn or Gln, cf. EC 3.5.1.122
-
-
?
additional information
?
-
-
intracellular eukaryotic proteins with N-terminal methionine-asparagin sequences as potential substrates in vivo, overveiw
-
-
?
additional information
?
-
-
enzyme PNAD does not act on internal asparagine residues and requires a free Nalpha-amino groups. It has reduced or no activity on NH2-terminal asparagine dipeptides and no activity toward free asparagine or asparagine amide. It does not act on any NH2-terminal glutamine substrates
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
intracellular eukaryotic proteins with N-terminal methionine-asparagin sequences as potential substrates in vivo, overveiw
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
-
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition by Mg2+, Ca2+, EDTA, or D-desthiobiotin
-
additional information
-
no inhibition by Mg2+, Ca2+, EDTA, or D-desthiobiotin
-
additional information
-
no inhibition by DTT, PMSF, Na2SO4, Mg2+, Ca2+, Na+, and EDTA
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hypertension
Genetic predictors of glucocorticoid-induced hypertension in children with acute lymphoblastic leukemia.
Infections
microRNA-125a-3p is regulated by MyD88 in Legionella pneumophila infection and targets NTAN1.
Legionnaires' Disease
microRNA-125a-3p is regulated by MyD88 in Legionella pneumophila infection and targets NTAN1.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
asparagine-specific enzyme activity with dipeptides Gln-Val and Gln-Gly, Michaelis-Menten kinetics, overview
-
additional information
additional information
-
asparagine-specific enzyme activity with dipeptides Gln-Val and Gln-Gly, Michaelis-Menten kinetics, overview
-
additional information
additional information
Michaelis-Menten kinetic modelling
-
additional information
additional information
-
Michaelis-Menten kinetic modelling
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
in wild-type embryos, Ntan1 is strongly expressed in the branchial arches and in the tail and limb buds
brenda
-
in wild-type embryos, Ntan1 is strongly expressed in the branchial arches and in the tail and limb buds
-
brenda
additional information
ubiquitous enzyme expression in mouse tissues, expression profile and analysis
brenda
additional information
-
ubiquitous enzyme expression in mouse tissues, expression profile and analysis
brenda
additional information
-
ubiquitous enzyme expression in mouse tissues, expression profile and analysis
-
brenda
additional information
ubiquitous enzyme expression in mouse tissues
brenda
additional information
-
ubiquitous enzyme expression in mouse tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme PNAD does not contain disulfide bridges and exists as a soluble enzyme in monomeric form
-
brenda
NtN-amidase is located in both the cytosol and the nucleus
brenda
-
NtN-amidase is located in both the cytosol and the nucleus
-
brenda
NtN-amidase is located in both the cytosol and the nucleus
brenda
-
NtN-amidase is located in both the cytosol and the nucleus
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
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
-
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
-
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
-
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
-
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
-
the enzyme is involved in the mammalian N-end rule pathway, 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. 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
-
physiological function
-
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
-
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
-
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NTAN1_HUMAN
310
0
34677
Swiss-Prot
Mitochondrion (Reliability: 4)
NTAN1_MOUSE
310
0
34595
Swiss-Prot
Mitochondrion (Reliability: 4)
NTAN1_PIG
311
0
34890
Swiss-Prot
Mitochondrion (Reliability: 4)
NTAN1_ARATH
347
0
39174
Swiss-Prot
Chloroplast (Reliability: 5)
B1H1G1_XENTR
310
0
34539
TrEMBL
other Location (Reliability: 3)
A0A7R8CWQ1_LEPSM
251
0
28799
TrEMBL
other Location (Reliability: 2)
A0A7R8CRQ7_LEPSM
265
0
30567
TrEMBL
other Location (Reliability: 2)
A0A1Z5JGJ5_FISSO
380
0
42004
TrEMBL
other Location (Reliability: 2)
A0A7R8CFX5_LEPSM
132
0
15019
TrEMBL
other Location (Reliability: 2)
A0A812DES9_SEPPH
316
0
35569
TrEMBL
other Location (Reliability: 2)
A0A6J8BK56_MYTCO
307
0
34279
TrEMBL
other Location (Reliability: 1)
A0A1Z5J5M7_FISSO
380
0
42042
TrEMBL
other Location (Reliability: 2)
A0A7R8GYU7_LEPSM
395
0
44791
TrEMBL
other Location (Reliability: 4)
E3TDR9_ICTPU
306
0
34058
TrEMBL
other Location (Reliability: 3)
A0A812DI13_SEPPH
341
0
38315
TrEMBL
other Location (Reliability: 2)
NTA1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
457
0
51897
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
in solution, yNta1 is a monomer containing 14 beta-strands, 11 alpha-helices, and three 310-helices. The core region of the enzyme shows antiparallel and parallel mixed beta-sheets surrounded by helices, and these sixstranded beta-sheets face each other
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C160A
site-directed mutagenesis, the mutant show unaltered activity compared to the wild-type enzyme
additional information
additional information
construction and analysis of mouse strains lacking the asparagine-specific N-terminal amidase (NtN-amidase), encoded by the Ntan1 gene, by deletion-disruption of the mouse Ntan1 gene
additional information
-
construction and analysis of mouse strains lacking the asparagine-specific N-terminal amidase (NtN-amidase), encoded by the Ntan1 gene, by deletion-disruption of the mouse Ntan1 gene
additional information
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
additional information
-
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
additional information
-
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
-
additional information
-
construction and analysis of mouse strains lacking the asparagine-specific N-terminal amidase (NtN-amidase), encoded by the Ntan1 gene, by deletion-disruption of the mouse Ntan1 gene
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 11515fold to homogeneity from liver by anion exchange chromatography, ammonium sulfate fractionation, gel filtration, and another step of anion exchange chromatgraphy, follwed by chromatofocusing and again gel filtration
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recombinant tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by affinity cromatography and ultrafiltration, method improvement
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Ntan1 gene is located in the proximal region of mouse chromosome 16 and contains 10 exons ranging from 54 to 177 base pairs in length, recombinant expression of mouse NtN-amidase in Saccharomyces cerevisiae nta1DELTA enzyme-deficient strain
gene Ntan1, chromosomal localization and expression analysis, recombinant expression of N-terminally GFP-tagged 65-kDa in NTAN1pmouse 3T3 cells
gene Ntan1, DNA and amino acid sequence determination and analysis, Ntan1 promoter identification, chromosome mapping of gene Ntan1 reveals that Ntan1 is located in the proximal region of mouse chromosome 16, the gene is located in the proximal region of mouse chromosome 16 and contains 10 exons ranging from 54 to 177 base pairs in length, recombinant expression of full-length mouse NtN-amidase in Saccharomyces cerevisiae nta1DELTA enzyme-deficient strain
gene NTAN1, phylogenetic analysis, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes with a C-terminal strepII-tag or a FLAG-strepII tandem affinity tag in Escherichia coli strain BL21(DE3), method improvement
gene Ntan1, rat Ntan1 promoter (-1361 to +99) is prepared from rat genomic DNA by PCR, sequence comparisons, overexpression of Ntan1 using recombinant Ntan1 adenovirus vector resulting in a marked decrease in the MAP2 protein expression in hippocampal neurons
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene Ntan1 mRNA is increased about 3fold after 3 h in response to brief magnetism. Brief magnetism also increases the transcriptional activity of Ntan1 promoter by luciferase reporter assay
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the enzyme expression is downregulated upon the conversion of myoblasts into myotubes
the enzyme expression is downregulated upon the conversion of myoblasts into myotubes
the enzyme expression is downregulated upon the conversion of myoblasts into myotubes
the enzyme expression is downregulated upon the conversion of myoblasts into myotubes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cantor, J.; Stone, E.; Georgiou, G.
Expression and biochemical characterization of the human enzyme N-terminal asparagine amidohydrolase
Biochemistry
50
3025-3033
2011
Homo sapiens (Q96AB6), Homo sapiens
brenda
Balogh, S.; McDowell, C.; Tae Kwon, Y.; Denenberg, V.
Facilitated stimulus-response associative learning and long-term memory in mice lacking the NTAN1 amidase of the N-end rule pathway
Brain Res.
892
336-343
2001
Mus musculus (Q64311), Mus musculus 129 (Q64311)
brenda
Stewart, A.; Arfin, S.; Bradshaw, R.
Protein NH2-terminal asparagine deamidase: isolation and characterization of a new enzyme
J. Biol. Chem.
269
23509-23517
1994
Sus scrofa
brenda
Grigoryev, S.; Stewart, A.E.; Kwon, Y.T.; Arfin, S.M.; Bradshaw, R.A.; Jenkins, N.A.; Copeland, N.G.; Varshavsky, A.
A mouse amidase specific for N-terminal asparagine. The gene, the enzyme, and their function in the N-end rule pathway
J. Biol. Chem.
271
28521-28532
1996
Saccharomyces cerevisiae (P40354), Saccharomyces cerevisiae, Mus musculus (Q64311), Mus musculus, Mus musculus BALB/c (Q64311)
brenda
Hirai, T.; Taniura, H.; Goto, Y.; Ogura, M.; Sng, J.; Yoneda, Y.
Stimulation of ubiquitin-proteasome pathway through the expression of amidohydrolase for N-terminal asparagine (Ntan1) in cultured rat hippocampal neurons exposed to static magnetism
J. Neurochem.
96
1519-1530
2006
Rattus norvegicus
brenda
Kwon, Y.; Balogh, S.; Davydov, I.; Kashina, A.; Yoon, J.; Xie, Y.; Gaur, A.; Hyde, L.; Denenberg, V.; Varshavsky, A.
Altered activity, social behavior, and spatial memory in mice lacking the NTAN1p amidase and the asparagine branch of the N-end rule pathway
Mol. Cell. Biol.
20
4135-4148
2000
Mus musculus (Q64311), Mus musculus, Mus musculus C129 (Q64311)
brenda
Kim, M.K.; Oh, S.J.; Lee, B.G.; Song, H.K.
Structural basis for dual specificity of yeast N-terminal amidase in the N-end rule pathway
Proc. Natl. Acad. Sci. USA
113
12438-12443
2016
Saccharomyces cerevisiae (P40354), Saccharomyces cerevisiae
brenda
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Release 2023.1 (January 2023)
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