Information on EC 3.2.2.4 - AMP nucleosidase

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The expected taxonomic range for this enzyme is: Gammaproteobacteria

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
2
NMN
Azotobacter vinelandii
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-
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
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
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sedimentation equilibrium analysis, monomer
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
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gel filtration, oligomer, active enzyme
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
-10C, 2 months
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-10C, Tris-K2SO4-buffer, 2 months
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-70C, dry ice mixture, 1 year
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-80C, dry ice mixture
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-80C, Tris-NaCl-AMP buffer, 6 months
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4C 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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