Information on EC 3.2.2.14 - NMN nucleosidase

for references in articles please use BRENDA:EC3.2.2.14
Word Map on EC 3.2.2.14
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


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

top print hide
EC NUMBER
COMMENTARY hide
3.2.2.14
-
top print hide
RECOMMENDED NAME
GeneOntology No.
NMN nucleosidase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
beta-nicotinamide D-ribonucleotide + H2O = D-ribose 5-phosphate + nicotinamide
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NAD salvage pathway I
-
-
pyridine nucleotide cycling (plants)
-
-
NAD metabolism
-
-
Nicotinate and nicotinamide metabolism
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
nicotinamide-nucleotide phosphoribohydrolase
-
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
37237-49-3
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
bacterial meningitis, type b
-
-
Manually annotated by BRENDA team
bacterial meningitis, type b
-
-
Manually annotated by BRENDA team
top print hide
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
-
-
-
-
?
guanosine 3'-diphosphate 5'-triphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
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
top print hide
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
-
-
-
-
?
nicotinamide mononucleotide + H2O
?
show the reaction diagram
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-phosphoribose 1-diphosphate
-
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
-
-
adenosine
-
addition of 1.4 mM, inhibition 54.7%
ADP-ribose
-
addition of 1-1.4 mM, inhibition 74.4%
AMP
-
addition of 1.4 mM AMP, inhibition 92.5%
D-ribose-5-phosphate
-
addition of 1.4 mM, inhibition 42.3%
dCMP
-
effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
desamido-NAD+
-
addition of 1 mM, inhibition 66.6%
dGMP
-
effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
EDTA
-
1 mM inhibits NMN hydrolysis by 30%
guanosine
-
addition of 1.4 mM, inhibition 44.6%
N-ethylmaleimide
-
50% inhibition at 80 mM
NAD+
-
greatly inhibited by intracellular levels of NAD+ and reduced NADH, addition of 1 mM NAD+, inhibition 73.2%
NADH
-
addition of 1 mM, inhibition 68.6%
NADP+
-
addition of 1 mM, inhibition 24%
nicotinamide hypoxanthine dinucleotide
-
addition of 1 mM nicotinamide hypoxanthine dinucleotide, inhibition 61.4%
p-chloromercuribenzoate
-
50% inhibition at 3 mM
pyridoxal 5'-phosphate
-
addition of 1.4 mM, inhibition 8.8%
pyridoxal HCl
-
addition of 1.4 mM, inhibition 5.2%
thio-NAD+
-
addition of 1 mM, inhibition 63.2%
top print hide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
less effective activator than GTP
guanosine 2'-monophosphate
-
-
guanosine 3'-diphosphate-5'-triphosphate
-
guanine nucleotides, guanosinetriphosphate and polyphosphate derivatives, effective activation
guanosine 3'-monophosphate
-
-
guanosine 5'-tetraphosphate
-
most potent activator
SO42-
-
10 mM relative activity 103%, 100% activity with nicotinamide as substrate
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0087
guanosine 3'-diphosphate 5'-triphosphate
-
-
0.22 - 4.5
nicotinamide mononucleotide
top print hide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
80
N-ethylmaleimide
-
-
3
p-chloromercuribenzoate
-
-
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.032
-
addition of 1.4 mM GTP, inhibition 93.1%
0.034
-
addition of 1.4 mM AMP, inhibition 92.5%
0.049
-
addition of 1.4 mM GMP, inhibition 89.4%
0.117
-
addition of 1.4 mM ADP-ribose, inhibition 74.4%
0.122
-
addition of 1 mM ADP-ribose, inhibition 74.4%
0.128
-
addition of 1 mM NAD+, inhibition 73.2%
0.15
-
addition of 1 mM NADH, inhibition 68.6%
0.16
-
addition of 1 mM desamido-NAD+, inhibition 66.6%
0.176
-
addition of 1 mM thio-NAD+, inhibition 63.2%
0.186
-
addition of 1 mM NHD, inhibition 61.4%
0.208
-
addition of 1.4 mM adenosine, inhibition 54.7%
0.254
-
addition of 1.4 mM guanosine, inhibition 44.6%
0.264
-
addition of 1.4 mM D-ribose-5-phosphate, inhibition 42.3%
0.363
-
addition of 1 mM NADP+, inhibition 24%
0.418
-
addition of 1.4 mM pyridoxal 5'-phosphate, inhibition 8.8%
0.434
-
addition of 1.4 mM pyridoxal HCl, inhibition 5.2%
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
established from the roots of seedlings
Manually annotated by BRENDA team
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
-
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
-
gel filtration
213000
-
gel filtration, Sephadex G-200
240000
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
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
top print hide
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
-
top print hide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0 to -16°C stored for a month without significant loss of activity
-
0°C, 0.025 M Tris-HCl, pH 9, containing 1 mM reduced glutathione, one-half of enzyme activity lost in 5 days
-
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially
-
partially from sonic extract, purified enzyme loses over 90% of its activity after Sephadex G-200 treatment
-
top
top
top
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)