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Literature summary for 3.5.1.121 extracted from

  • Cantor, J.; Stone, E.; Georgiou, G.
    Expression and biochemical characterization of the human enzyme N-terminal asparagine amidohydrolase (2011), Biochemistry, 50, 3025-3033.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.121

Cloned(Commentary)

Cloned (Comment) Organism
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 Homo sapiens

Protein Variants

Protein Variants Comment Organism
C160A site-directed mutagenesis, the mutant show unaltered activity compared to the wild-type enzyme Homo sapiens
C75A site-directed mutagenesis, inactive mutant Homo sapiens
C75S site-directed mutagenesis, inactive mutant Homo sapiens
C75T site-directed mutagenesis, inactive mutant Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Co2+ partial inhibition at 0.050 mM Homo sapiens
Cu2+ complete inhibition at 0.050 mM Homo sapiens
Mn2+ partial inhibition at 0.050 mM Homo sapiens
additional information no inhibition by Mg2+, Ca2+, EDTA, or D-desthiobiotin Homo sapiens
Ni2+ partial inhibition at 0.050 mM Homo sapiens
Zn2+ complete inhibition at 0.050 mM Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetic modelling Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-terminal L-asparaginyl-[protein] + H2O Homo sapiens
-
 N-terminal L-aspartyl-[protein] + NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q96AB6
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by affinity cromatography and ultrafiltration, method improvement Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Homo sapiens ?
-
 ?
N-terminal L-asparaginyl-[protein] + H2O
-
 Homo sapiens N-terminal L-aspartyl-[protein] + NH3
-
 ?

Synonyms

Synonyms Comment Organism
N-terminal asparagine amidohydrolase
-
 Homo sapiens
NTAN1
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens
metabolism the enzyme is involved in the mammalian N-end rule pathway Homo sapiens
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 Homo sapiens