Information on EC 3.5.1.121 - protein N-terminal asparagine amidohydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.121
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RECOMMENDED NAME
GeneOntology No.
protein N-terminal asparagine amidohydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-terminal L-asparaginyl-[protein] + H2O = N-terminal L-aspartyl-[protein] + NH3
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arg/N-end rule pathway (eukaryotic)
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-terminal L-asparaginyl-[protein] + H2O
N-terminal L-aspartyl-[protein] + NH3
show the reaction diagram
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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fe2+
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complete irreversible inhibition at 0.2 mM
iodoacetic acid
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55% inhibition at 0.25 mM
Li+
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complete inhibition at 0.2 mM
N-ethylmaleimide
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50% inhibition at 0.25 mM
Ni2+
partial inhibition at 0.050 mM
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
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sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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hippocampal neurons
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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the enzyme PNAD does not contain disulfide bridges and exists as a soluble enzyme in monomeric form
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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1 * 33000, SDS-PAGE
34000
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native enzyme, gel filtration
35000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
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enzyme amino acid composition, overview
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
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
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gene Ntan1, chromosomal localization and expression analysis, recombinant expression of N-terminally GFP-tagged 65-kDa in NTAN1pmouse 3T3 cells
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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
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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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C160A
site-directed mutagenesis, the mutant show unaltered activity compared to the wild-type enzyme
C75A
site-directed mutagenesis, inactive mutant
C75S
site-directed mutagenesis, inactive mutant
C75T
site-directed mutagenesis, inactive mutant
additional information