Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.1.121 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
Search for more literature for 3.5.1.121

Cloned(Commentary)

Cloned (Comment) Organism
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
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

Protein Variants Comment Organism
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

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
additional information the NtN-amidase is a 310-residue amidohydrolase from Mus musculus is specific for N-terminal asparagine Mus musculus ?
-
 ?
additional information the NtN-amidase is a 310-residue amidohydrolase from Mus musculus is specific for N-terminal asparagine Mus musculus BALB/c ?
-
 ?
N-terminal L-asparaginyl-[protein] + H2O
-
 Mus musculus N-terminal L-aspartyl-[protein] + NH3
-
 ?
N-terminal L-asparaginyl-[protein] + H2O
-
 Saccharomyces cerevisiae N-terminal L-aspartyl-[protein] + NH3
-
 ?
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
-
 ?
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
-
 ?
N-terminal L-asparaginyl-[protein] + H2O
-
 Mus musculus BALB/c N-terminal L-aspartyl-[protein] + NH3
-
 ?
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

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

Synonyms

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

pI Value

Organism Comment pI Value Maximum pI Value
Mus musculus sequence calculation
-
 6.1

Expression

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

General Information

General Information Comment Organism
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
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
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
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
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