Information on EC 2.7.1.22 - ribosylnicotinamide kinase

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

EC NUMBER
COMMENTARY hide
2.7.1.22
-
RECOMMENDED NAME
GeneOntology No.
ribosylnicotinamide kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 1-(beta-D-ribofuranosyl)-nicotinamide = ADP + beta-nicotinamide D-ribonucleotide
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
NAD salvage pathway IV
-
-
Nicotinate and nicotinamide metabolism
-
-
NAD metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:N-ribosylnicotinamide 5'-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9030-61-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + N-ribosylnicotinamide
ADP + nicotinamide ribonucleotide
show the reaction diagram
ATP + nicotinamide mononucleotide
NAD+ + diphosphate
show the reaction diagram
phosphate + inosine
?
show the reaction diagram
-
-
-
-
?
phosphate + nicotinamide riboside
nicotinamide + ribose-1-phosphate
show the reaction diagram
-
-
-
r
additional information
?
-
-
the enzymes' C-terminal domain has nicotinamide ribose kinase activity, the central domain performes adenylyltransferase reaction, EC 2.7.7.1, overview, the purified enzyme binds nadB promotor sequence in absence of ATP with or without NAD+, DNA binding activity of the enzyme is regulated by ATP binding to the adenylyltransferase domain
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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
ATP + N-ribosylnicotinamide
ADP + nicotinamide ribonucleotide
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
69% inhibition at 1.2 mM, complete inhibition at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2
ATP
-
recombinant enzyme, pH 7.6, 37C
0.08
N-ribosylnicotinamide
-
recombinant enzyme, pH 7.6, 37C
0.14
nicotinamide mononucleotide
pH 7.5, 37C, nicotinamide mononucleotide adenylyltransferase activity
1.1
nicotinamide riboside
-
pH 7.4
0.28
phosphate
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pH 7.4
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.92
nicotinamide mononucleotide
Haemophilus influenzae
Q57425
pH 7.5, 37C, nicotinamide mononucleotide adenylyltransferase activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.9
pH 7.5, 37C, nicotinamide mononucleotide adenylyltransferase activity
1
-
pH 7.5, 37C, ribosylnicotinamide kinase activity
1.4
-
purified recombinant enzyme
4.25
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
assay at
8
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nicotinamide riboside phosphorolysis
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
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approx. 25% of maximal activity at pH 6.0, approx. 55% of maximal activity at pH 10, nicotinamide riboside phosphorolysis
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
and liver, highest eypression
Manually annotated by BRENDA team
additional information
-
presence of quinolinate phosphoribosyltransferase and nicotinamide riboside kinase in all examined tissues/cell lines
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
-
at 0.4 mg/ml protein, analytical ultracentrifugation
170000
-
at 1.2 mg/ml protein, analytical ultracentrifugation
180000
-
deduced from nucleotide sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion, 10 mg/ml protein in 100 mM Hepes, pH 7.2, 300 mM NaCl, 1 mM dithiothreitol are incubated with 3 mM NAD and 3 mM ATP and mixed with an equal volume of the reservoir solution consisting of 100 mM MES, pH 6.0, 1 M ammonium sulfate, crystal structure of enzyme complexed with NAD
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sitting-drop vapor-diffusion method at 22C, crystal structures of NRK1 in a binary complex with the reaction product nicotinamide mononucleotide at 1.5 A resolution and in a ternary complex with ADP and tiazofurin at 2.7 A resolution. The active site is located in a groove between the central parallel beta sheet core and the LID and NMP-binding domains
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, several weeks, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, calcium phosphate gel, alumina gel
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recombinant enzyme
recombinant enzyme, Ni2+-nitrilotriacetic acid-agarose, Superdex 200
recombinant N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene nadR, expression of N-terminally His6-tagged enzyme in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D138A
mutation has minor effects on catalysis
D36A
mutation abolishes activity
D56A
mutation abolishes activity
K16A
mutation abolishes activity
additional information
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analysis of mutant strains for activities/functions of enzyme domains, reduced activity of class I mutants, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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simple, fast and sensitive coupled fluorometric assay that enables simultaneous determination of nicotinamide phosphoribosyltransferase EC 2.4.2.12, quinolinate phosphoribosyltransferase EC 2.4.2.19, nicotinate phosphoribosyltransferase EC 6.3.4.21 and nicotinamide riboside kinase in whole-cell extracts and biological fluids yielding an overall picture of the tissue/cell-specific distribution of the activities of the various enzymes
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