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Literature summary extracted from

  • 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 (1996), J. Biol. Chem., 271, 28521-28532.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.121 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 Saccharomyces cerevisiae
3.5.1.121 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 Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.121 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 Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.1.121 cytosol NtN-amidase is located in both the cytosol and the nucleus Mus musculus 5829
-
3.5.1.121 nucleus NtN-amidase is located in both the cytosol and the nucleus Mus musculus 5634
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.121 35000
-
-
 Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.121 N-terminal L-asparaginyl-[protein] + H2O Mus musculus
-
 N-terminal L-aspartyl-[protein] + NH3
-
 ?
3.5.1.121 N-terminal L-asparaginyl-[protein] + H2O Saccharomyces cerevisiae
-
 N-terminal L-aspartyl-[protein] + NH3
-
 ?
3.5.1.121 N-terminal L-asparaginyl-[protein] + H2O Mus musculus BALB/c
-
 N-terminal L-aspartyl-[protein] + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.121 Mus musculus Q64311
-
-
3.5.1.121 Mus musculus BALB/c Q64311
-
-
3.5.1.121 Saccharomyces cerevisiae P40354
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.121 kidney
-
 Mus musculus
-
3.5.1.121 liver
-
 Mus musculus
-
3.5.1.121 lymphoma cell
-
 Mus musculus
-
3.5.1.121 MEL-C19 cell
-
 Mus musculus
-
3.5.1.121 additional information ubiquitous enzyme expression in mouse tissues Saccharomyces cerevisiae
-
3.5.1.121 additional information ubiquitous enzyme expression in mouse tissues, expression profile and analysis Mus musculus
-
3.5.1.121 myoblast
-
 Mus musculus
-
3.5.1.121 myoblast
-
 Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.121 additional information the NTA1-encoded Nt-amidase of Saccharomyces cerevisiae can deamidate N-terminal Asn or Gln, cf. EC 3.5.1.122 Saccharomyces cerevisiae ?
-
 ?
3.5.1.121 additional information the NtN-amidase is a 310-residue amidohydrolase from Mus musculus is specific for N-terminal asparagine Mus musculus ?
-
 ?
3.5.1.121 additional information the NtN-amidase is a 310-residue amidohydrolase from Mus musculus is specific for N-terminal asparagine Mus musculus BALB/c ?
-
 ?
3.5.1.121 N-terminal L-asparaginyl-[protein] + H2O
-
 Mus musculus N-terminal L-aspartyl-[protein] + NH3
-
 ?
3.5.1.121 N-terminal L-asparaginyl-[protein] + H2O
-
 Saccharomyces cerevisiae N-terminal L-aspartyl-[protein] + NH3
-
 ?
3.5.1.121 N-terminal L-asparaginyl-[protein] + H2O purified, 35S-labeled X DHFR protein bearing Asn at its N-terminus is used as substrate Mus musculus N-terminal L-aspartyl-[protein] + NH3
-
 ?
3.5.1.121 N-terminal L-asparaginyl-[protein] + H2O purified, 35S-labeled X DHFR test proteins bearing either Asn, Gln, or Asp at their N termini are used as substrates Saccharomyces cerevisiae N-terminal L-aspartyl-[protein] + NH3
-
 ?
3.5.1.121 N-terminal L-asparaginyl-[protein] + H2O
-
 Mus musculus BALB/c N-terminal L-aspartyl-[protein] + NH3
-
 ?
3.5.1.121 N-terminal L-asparaginyl-[protein] + H2O purified, 35S-labeled X DHFR protein bearing Asn at its N-terminus is used as substrate Mus musculus BALB/c N-terminal L-aspartyl-[protein] + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.121 ? x * 35000, about, sequence calculation Mus musculus

Synonyms

EC Number Synonyms Comment Organism
3.5.1.121 NTA1
-
 Saccharomyces cerevisiae
3.5.1.121 NTAN1
-
 Mus musculus
3.5.1.121 NtN-amidase
-
 Mus musculus
3.5.1.121 NtN-amidase
-
 Saccharomyces cerevisiae

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.5.1.121 Mus musculus sequence calculation
-
 6.1

Expression

EC Number Organism Comment Expression
3.5.1.121 Mus musculus the enzyme expression is downregulated upon the conversion of myoblasts into myotubes down
3.5.1.121 Saccharomyces cerevisiae the enzyme expression is downregulated upon the conversion of myoblasts into myotubes down

General Information

EC Number General Information Comment Organism
3.5.1.121 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 Saccharomyces cerevisiae
3.5.1.121 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 Mus musculus
3.5.1.121 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 Saccharomyces cerevisiae
3.5.1.121 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 Mus musculus
3.5.1.121 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 Saccharomyces cerevisiae