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
ECTree
3.5.1.121 protein N-terminal asparagine amidohydrolaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.5.1.121 - protein N-terminal asparagine amidohydrolase
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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
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?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
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-
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?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
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-
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?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
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-
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?
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
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-
?
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
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-
?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
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?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
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-
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?
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
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?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
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-
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?
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
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?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
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?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
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-
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?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
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?
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
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?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
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?
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
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the enzyme specifically converts NH2-terminal asparagine residues of peptide and protein substrate to aspartic acid
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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the NtN-amidase is a 310-residue amidohydrolase from Mus musculus is specific for N-terminal asparagine
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?
additional information
?
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the NtN-amidase is a 310-residue amidohydrolase from Mus musculus is specific for N-terminal asparagine
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?
additional information
?
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the NtN-amidase is a 310-residue amidohydrolase from Mus musculus is specific for N-terminal asparagine
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
?
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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
?
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intracellular eukaryotic proteins with N-terminal methionine-asparagin sequences as potential substrates in vivo, overveiw
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?
additional information
?
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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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?
