Information on EC 3.5.1.122 - protein N-terminal glutamine amidohydrolase

for references in articles please use BRENDA:EC3.5.1.122
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.5.1.122
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RECOMMENDED NAME
GeneOntology No.
protein N-terminal glutamine amidohydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-terminal L-glutaminyl-[protein] + H2O = N-terminal L-glutamyl-[protein] + NH3
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arg/N-end rule pathway (eukaryotic)
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SYSTEMATIC NAME
IUBMB Comments
protein N-terminal glutamine 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-Gln. Following the acetylation and removal of the initiator methionine, the exposed N-terminal glutamine is deaminated, resulting in its conversion to L-glutamate. 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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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
GENERAL INFORMATION
ORGANISM
UNIPROT
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LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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-glutaminyl-[DHFRbt] + H2O
N-terminal L-glutamyl-[DHFRbt] + NH3
show the reaction diagram
substrate is Escherichia coli dihydrofolate reductase (DHFR) moiety fused to a C-terminal peptide (denoted as bt) that is biotinylated in vivo
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N-terminal L-glutaminyl-[protein] + H2O
N-terminal L-glutamyl-[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-glutaminyl-[protein] + H2O
N-terminal L-glutamyl-[protein] + NH3
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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LITERATURE
IMAGE
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
7.2
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
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LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
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LITERATURE
SUBUNITS
ORGANISM
UNIPROT
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LITERATURE
monomer
in solution, yNta1 is a monomer containing 14 beta-strands, 11 alpha-helices, and three 310-helices. The core region of the enzyme shows antiparallel and parallel mixed beta-sheets surrounded by helices, and these sixstranded beta-sheets face each other
additional information
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the enzyme structure reveals a monomeric globular protein with alpha-beta-alpha three-layer sandwich architecture. The catalytic triad located in the active site, Cys-His-Asp, is highly conserved among Ntaq family and transglutaminases from diverse organisms. Substrate binding mode of hNtaq1 with the N-terminus of a symmetry-related Ntaq1 molecule bound in the substrate binding cleft
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of C8orf32/Ntaq1
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purified enzyme Ntaq1 bound with the N-terminus of a symmetry-related Ntaq1 molecule, hanging drop vapor diffusion method, mixing of 10 mg/ml protein in 50 mM sodium chloride, 3 mM sodium azide, 0.3 mM TCEP, and 100 mM Bis-Tris, pH 7.0, with well solution containing 1% ethylene glycol, 1.8 M ammonium sulfate, 100 mM MES, pH 6.0, in 1:1 ratio, at 18°C, X-ray diffraction structure determination and analysis at 1.5 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from a brain extract by ion exchange, hydrophobic chromatography, and gel filtration
recombinant N-terminally His6-MBP-tagged enzyme from Escherichia coli strain B834 as Se-Met labeled protein by nickel affinity chromatography, tag cleavage by TEV protease, gel filtration,and another step of nickel affinity chromatography, followed by desalting gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene C8orf32
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gene C8orf32, the enzyme is expressed as recombinant fusion enzyme containing N-terminally fused His6-maltose binding protein (MBP) and a linker region with the TEV protease site for cleavage of target proteins, expression in Escherichia coli strain B834 as Se-Met labeled protein
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gene Cg8253
gene Ntaq1, DNA and amino acid sequence determination and analysis, mouse Hebp2 cDNA and Wdyhv1 cDNA are subcloned into the plasmid p425Met25, the FLAG-tagged mouse Hebp2f and Wdyhv1f are expressed in an nta1DELTA mutant of Saccharomyces cerevisiae that lacks the endogenous Nta1 NtN,Q-amidase activity. Recombinant transient expression of a mouse Ntaq1-EGFP fusion from the PCMV promoter transfected into NIH-3T3 cells. Recombinant expression of C-terminally His6-tagged mouse Ntaq1 in Pichia pastoris