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
3.2.2.4
-
RECOMMENDED NAME
GeneOntology No.
AMP nucleosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
AMP + H2O = D-ribose 5-phosphate + adenine
show the reaction diagram
-
-
-
-
AMP + H2O = D-ribose 5-phosphate + adenine
show the reaction diagram
SN1-type catalytic mechanism with formation of an oxocarbenium-like intermediate followed by nucleophilic attack at the anomeric carbon, overview, substrate binding site structure
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
adenosine nucleotides degradation III
-
Purine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
AMP phosphoribohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
adenosine monophosphate nucleosidase
-
-
-
-
adenylate nucleosidase
-
-
-
-
AMP ribosidase
-
-
-
-
additional information
-
the enzyme belongs to the family of nucleoside phosphorylases
CAS REGISTRY NUMBER
COMMENTARY
9025-45-0
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminoAMP
2-aminoadenine + ribose-5'phosphate
show the reaction diagram
-
-
-
?
2-aminoAMP
2-aminoadenine + ribose-5'phosphate
show the reaction diagram
-
-
-
?
3'-deoxy-5'-AMP
?
show the reaction diagram
-
-
-
-
?
8-azaAMP
8-azaadenine + ribose-5'phosphate
show the reaction diagram
-
-
-
?
8-azaAMP
8-azaadenine + ribose-5'phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
?
AMP + H2O
adenine + ribose 5-phosphate
show the reaction diagram
-
-
-
ir
AMP + H2O
adenine + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
NMN + H2O
?
show the reaction diagram
-
-
-
-
-
NMN + 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
-
-
?
additional information
?
-
Escherichia coli, Escherichia coli W3110
-
AMP nucleosidase activity leads to glucose-independent dihydroxyacetone phosphate production from adenosine phosphates in an insulated in vitro multi-step enzymatic system to carry out complex and thermodynamically unfavorable chemical conversions and biotransformations, e.g. dihydroxyacetone phosphate formation, and the gene has thus to be inhibited, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
-
-
?
NMN + H2O
?
show the reaction diagram
-
-
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4-aminopyrazolo(3,4-d)pyrimidine-1-ribonucleotide
-
-
8-[[[(2,2,5,5-tetramethyl-1-oxy-3-pyrrolidinyl)carbamoyl]methyl]thio]AMP
-
-
flavin mononucleotide
-
-
formycin 5'-phosphate
-
conformational changes upon inhibitor binding, overview
Formycin monophosphate
-
mutant AMP nucleosidase
Formycin monophosphate
-
-
N6-Methyladenosine
-
-
p-chloromercuribenzoate
-
-
phosphate
-
dissociation to inactive dimers
phosphate
-
mutant AMP nucleosidase
phosphate
-
; conformational changes upon inhibitor binding, additional phosphate binding site, overview
ribose 5-phosphate
-
protection of inactivation by adenine
transition metal-ATP complexes
-
only at higher concentrations
-
Tubercidin 5'-phosphate
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.16
-
AMP
-
mutant AMP nucleosidase
110
-
AMP
-
saturating concentration of MgATP2-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.6
-
AMP
-
mutant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.016
-
-
wild type
0.3
-
-
mutant enzyme
0.32
-
-
mutant
0.6
-
-
mutant enzyme
8
-
-
Escherichia coli-strain: DH5alpha
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
PDB
SCOP
CATH
ORGANISM
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26000
-
-
sedimentation equilibrium analysis, monomer
53850
-
-
calculation from sequence of DNA
53850
-
-
-
53850
-
-
calculation from sequence of DNA
53850
-
-
-
60000
-
-
gel filtration and SDS-PAGE, monomer
104000
-
-
sedimentation equilibrium analysis, polymer
110000
-
-
gel filtration and SDS-PAGE, dimer
120000
-
-
gel filtration and SDS-PAGE, dimer
180000
-
-
gel filtration, oligomer, inactive enzyme
208000
-
-
PAGE
280000
-
-
gel filtration, oligomer, active enzyme
320000
-
-
gel filtration
320000
-
-
hexamer
325000
-
-
Archibald approach to equilibrium method
330000
-
-
mutant AMP nucleosidase, gel filtration
360000
-
-
gel filtration, polymer, active enzyme
370000
-
-
gel filtration and sedimentation velocity experiments
520000
-
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexamer
-
6 * 54000, gel filtration
hexamer
-
; homohexamer, crystal structure, each subunit is composed of one catalytic and one regulatory domain, subunit binding site and structure analysis, intersubunit and interdomain interaction, overview
octamer
-
8 * 26000, gel filtration and sedimentation equilibrium analysis
tetramer
-
4 * 280000, chromatographic results
tetramer
-
4 * 52000, gel electrophoresis
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-10C, 2 months
-
-10C, Tris-K2SO4-buffer, 2 months
-
-70C, dry ice mixture, 1 year
-
4C or room temperature, K2SO4
-
-80C, dry ice mixture
-
-80C, Tris-NaCl-AMP buffer, 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
mutant AMP nucleosidase
-
Vmax mutant AMP nucleosidase
-
; recombinant His6-tagged, selenomethionine-labeled enzyme from strain B834(DE3) by nickel affinity chromatography, the His-tag is cleaved off by thrombin
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
; overexpression of His6-tagged, selenomethionine-labeled enzyme with an inserted thrombin cleavage site in strain B834(DE3)
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
treatment with nitrosoguanidine leads to mutants defective in degrading AMP
additional information
-
hanging drop vapor diffusion method, complexed with formycin 5'-monophosphate or inorganic phosphate
additional information
-
in enzyme knockout mutant exhibits elevated intracellular ATP levels by more than 30% across its viable temperature range. Mutant cells stored at 0C for 7 days display approximately fivefold higher cell viability than wild-type
additional information
-
AMP nucleosidase activity leads to glucose-independent dihydroxyacetone phosphate production from adenosine phosphates in an insulated in vitro multi-step enzymatic system to carry out complex and thermodynamically unfavorable chemical conversions and biotransformations, e.g. dihydroxyacetone phosphate formation, and the gene has thus to be inhibited, overview
additional information
Escherichia coli W3110
-
AMP nucleosidase activity leads to glucose-independent dihydroxyacetone phosphate production from adenosine phosphates in an insulated in vitro multi-step enzymatic system to carry out complex and thermodynamically unfavorable chemical conversions and biotransformations, e.g. dihydroxyacetone phosphate formation, and the gene has thus to be inhibited, overview
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
purine nucleotide synthesis in procaryotes; stabilization of the adenylate energy charge
synthesis
-
stabilization of the adenylate energy charge