Information on EC 3.2.2.4 - AMP nucleosidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.2.4
-
RECOMMENDED NAME
GeneOntology No.
AMP nucleosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
AMP + H2O = D-ribose 5-phosphate + adenine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-glycosyl bond
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
adenosine nucleotides degradation III
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purine metabolism
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Purine metabolism
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SYSTEMATIC NAME
IUBMB Comments
AMP phosphoribohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-45-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminoAMP + H2O
2-aminoadenine + D-ribose 5-phosphate
show the reaction diagram
3'-deoxy-5'-AMP
?
show the reaction diagram
-
-
-
-
?
8-azaAMP
8-azaadenine + D-ribose 5-phosphate
show the reaction diagram
AMP + H2O
?
show the reaction diagram
AMP + H2O
adenine + D-ribose 5-phosphate
show the reaction diagram
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-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
AMP + H2O
D-ribose 5-phosphate + adenine
show the reaction diagram
NMN + H2O
?
show the reaction diagram
additional information
?
-
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
AMP + H2O
?
show the reaction diagram
AMP + H2O
D-ribose 5-phosphate + adenine
show the reaction diagram
-
the enzyme is restricted to prokaryotes and is involved in purine nucleoside salvage and intracellular AMP level regulation, enzyme regulation involving the N-terminal regulatory domain of the subunits
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-
?
NMN + H2O
?
show the reaction diagram
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-aminopyrazolo(3,4-d)pyrimidine-1-ribonucleotide
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8-azido-AMP
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8-[[[(2,2,5,5-tetramethyl-1-oxy-3-pyrrolidinyl)carbamoyl]methyl]thio]AMP
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diphosphate
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flavin mononucleotide
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formycin 5'-phosphate
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conformational changes upon inhibitor binding, overview
Formycin monophosphate
N6-methyladenosine
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p-chloromercuribenzoate
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phosphate
ribose 5-phosphate
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protection of inactivation by adenine
sulfate
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transition metal-ATP complexes
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only at higher concentrations
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tubercidin 5'-phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 110
AMP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 62
AMP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.016
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wild type
0.3
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mutant enzyme
0.32
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mutant
0.6
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mutant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12);
Q8ZNS0
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
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sedimentation equilibrium analysis, monomer
52000
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4 * 52000, gel electrophoresis
60000
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gel filtration and SDS-PAGE, monomer
104000
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sedimentation equilibrium analysis, polymer
110000
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gel filtration and SDS-PAGE, dimer
120000
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gel filtration and SDS-PAGE, dimer
180000
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gel filtration, oligomer, inactive enzyme
208000
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PAGE
280000
320000
325000
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Archibald approach to equilibrium method
330000
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mutant AMP nucleosidase, gel filtration
360000
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gel filtration, polymer, active enzyme
370000
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gel filtration and sedimentation velocity experiments
520000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
octamer
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8 * 26000, gel filtration and sedimentation equilibrium analysis
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme bound to formycin 5'-phosphate or phosphate, hanging drop vapour diffusion method, 0.002 ml of 15-20 mg/ml protein in 10 mM Tris-HCl, pH 7.6, 0.15 M NaCl, 2 mM MgCl2, and 1 mM DTT, is mixed with an equal amount of reservoir solution containing 1.8-2.0 M ammonium formate, 0.1 M HEPES, pH 6.8-7.2, 0.2 M NaCl, and 1 mm DTT, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.6-3.0 A resolution
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, 2 months
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-10°C, K2SO4
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-10°C, Tris-K2SO4-buffer, 2 months
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-70°C, dry ice mixture, 1 year
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-80°C, dry ice mixture
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-80°C, Tris-NaCl-AMP buffer, 6 months
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4°C or room temperature, K2SO4
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant His6-tagged, selenomethionine-labeled enzyme from strain B834(DE3) by nickel affinity chromatography, the His-tag is cleaved off by thrombin
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mutant AMP nucleosidase
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Vmax mutant AMP nucleosidase
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; overexpression of His6-tagged, selenomethionine-labeled enzyme with an inserted thrombin cleavage site in strain B834(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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