Information on EC 3.2.2.14 - NMN nucleosidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
3.2.2.14
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RECOMMENDED NAME
GeneOntology No.
NMN nucleosidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
beta-nicotinamide D-ribonucleotide + H2O = D-ribose 5-phosphate + nicotinamide
show the reaction diagram
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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
NAD salvage pathway I (PNC VI cycle)
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pyridine nucleotide cycling (plants)
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NAD metabolism
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Nicotinate and nicotinamide metabolism
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SYSTEMATIC NAME
IUBMB Comments
nicotinamide-nucleotide phosphoribohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37237-49-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
Manually annotated by BRENDA team
bacterial meningitis, type b
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Manually annotated by BRENDA team
bacterial meningitis, type b
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-
Manually annotated by BRENDA team
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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
beta-nicotinamide D-riboside + H2O
D-ribose + nicotinamide
show the reaction diagram
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-
?
guanosine 3'-diphosphate 5'-triphosphate + H2O
?
show the reaction diagram
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-
-
?
nicotinamide mononucleotide + H2O
?
show the reaction diagram
nicotinamide mononucleotide + H2O
nicotinamide + ribose 5-phosphate
show the reaction diagram
nicotinic acid mononucleotide + H2O
nicotinic acid + ribose 5-phosphate
show the reaction diagram
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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
beta-nicotinamide D-riboside + H2O
D-ribose + nicotinamide
show the reaction diagram
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-
-
-
?
nicotinamide mononucleotide + H2O
?
show the reaction diagram
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-phosphoribose 1-diphosphate
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PRPP, inorganic polyphosphates, affinity of 5-phosphoribose 1-pyrophosphate for the enzyme is dependent on the activator concentration , inhibition mechanism with 5-phosphoribose 1-pyrophosphate is competitive with GTP
7-methylguanosine-5'-triphosphate
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adenosine
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addition of 1.4 mM, inhibition 54.7%
ADP-ribose
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addition of 1-1.4 mM, inhibition 74.4%
AMP
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addition of 1.4 mM AMP, inhibition 92.5%
D-ribose-5-phosphate
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addition of 1.4 mM, inhibition 42.3%
dCMP
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effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
desamido-NAD+
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addition of 1 mM, inhibition 66.6%
dGMP
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effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
EDTA
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1 mM inhibits NMN hydrolysis by 30%
guanosine
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addition of 1.4 mM, inhibition 44.6%
N-ethylmaleimide
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50% inhibition at 80 mM
NAD+
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greatly inhibited by intracellular levels of NAD+ and reduced NADH, addition of 1 mM NAD+, inhibition 73.2%
NADH
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addition of 1 mM, inhibition 68.6%
NADP+
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addition of 1 mM, inhibition 24%
nicotinamide hypoxanthine dinucleotide
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addition of 1 mM nicotinamide hypoxanthine dinucleotide, inhibition 61.4%
p-chloromercuribenzoate
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50% inhibition at 3 mM
pyridoxal 5'-phosphate
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addition of 1.4 mM, inhibition 8.8%
pyridoxal HCl
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addition of 1.4 mM, inhibition 5.2%
thio-NAD+
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addition of 1 mM, inhibition 63.2%
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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less effective activator than GTP
guanosine 2'-monophosphate
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guanosine 3'-diphosphate-5'-triphosphate
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guanine nucleotides, guanosinetriphosphate and polyphosphate derivatives, effective activation
guanosine 3'-monophosphate
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guanosine 5'-tetraphosphate
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most potent activator
SO42-
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10 mM relative activity 103%, 100% activity with nicotinamide as substrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0087
guanosine 3'-diphosphate 5'-triphosphate
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0.22 - 4.5
nicotinamide mononucleotide
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
80
N-ethylmaleimide
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3
p-chloromercuribenzoate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.032
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addition of 1.4 mM GTP, inhibition 93.1%
0.034
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addition of 1.4 mM AMP, inhibition 92.5%
0.049
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addition of 1.4 mM GMP, inhibition 89.4%
0.117
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addition of 1.4 mM ADP-ribose, inhibition 74.4%
0.122
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addition of 1 mM ADP-ribose, inhibition 74.4%
0.128
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addition of 1 mM NAD+, inhibition 73.2%
0.15
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addition of 1 mM NADH, inhibition 68.6%
0.16
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addition of 1 mM desamido-NAD+, inhibition 66.6%
0.176
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addition of 1 mM thio-NAD+, inhibition 63.2%
0.186
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addition of 1 mM NHD, inhibition 61.4%
0.208
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addition of 1.4 mM adenosine, inhibition 54.7%
0.254
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addition of 1.4 mM guanosine, inhibition 44.6%
0.264
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addition of 1.4 mM D-ribose-5-phosphate, inhibition 42.3%
0.363
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addition of 1 mM NADP+, inhibition 24%
0.418
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addition of 1.4 mM pyridoxal 5'-phosphate, inhibition 8.8%
0.434
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addition of 1.4 mM pyridoxal HCl, inhibition 5.2%
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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established from the roots of seedlings
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
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1 * 110000 + 1 * 110000, enzyme easily dissociates in presence of 1 mM ATP, consisting of 4 identical protomers, MW 55000, no dissociation in presence of GTP
210000
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gel filtration
213000
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gel filtration, Sephadex G-200
240000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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1 * 110000 + 1 * 110000, enzyme easily dissociates in presence of 1 mM ATP, consisting of 4 identical protomers, MW 55000, no dissociation in presence of GTP
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
remains active for 1 week at 4°C in 0.025 M Tris-HCl, pH 7.5, containing 1 mM reduced glutathione
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0 to -16°C stored for a month without significant loss of activity
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0°C, 0.025 M Tris-HCl, pH 9, containing 1 mM reduced glutathione, one-half of enzyme activity lost in 5 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially
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partially from sonic extract, purified enzyme loses over 90% of its activity after Sephadex G-200 treatment
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LINKS TO OTHER DATABASES (specific for EC-Number 3.2.2.14)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)