BRENDA - Enzyme Database show
show all sequences of 2.7.1.22

The phosphorolysis of nicotinamide riboside

Rowen, J.W.; Kornberg, A.; J. Biol. Chem. 193, 497-507 (1951)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.28
-
phosphate
pH 7.4
Sus scrofa
1.1
-
nicotinamide riboside
pH 7.4
Sus scrofa
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sus scrofa
-
-
-
Purification (Commentary)
Commentary
Organism
ammonium sulfate, calcium phosphate gel, alumina gel
Sus scrofa
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Sus scrofa
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.25
-
-
Sus scrofa
Storage Stability
Storage Stability
Organism
-10°C, several weeks, no loss of activity
Sus scrofa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + N-ribosylnicotinamide
-
641173
Sus scrofa
ADP + nicotinamide ribonucleotide
-
641173
Sus scrofa
?
phosphate + inosine
-
641173
Sus scrofa
?
-
-
-
?
phosphate + nicotinamide riboside
-
641173
Sus scrofa
nicotinamide + ribose-1-phosphate
-
641173
Sus scrofa
r
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
nicotinamide riboside phosphorolysis
Sus scrofa
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
10
approx. 25% of maximal activity at pH 6.0, approx. 55% of maximal activity at pH 10, nicotinamide riboside phosphorolysis
Sus scrofa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.28
-
phosphate
pH 7.4
Sus scrofa
1.1
-
nicotinamide riboside
pH 7.4
Sus scrofa
Purification (Commentary) (protein specific)
Commentary
Organism
ammonium sulfate, calcium phosphate gel, alumina gel
Sus scrofa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Sus scrofa
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.25
-
-
Sus scrofa
Storage Stability (protein specific)
Storage Stability
Organism
-10°C, several weeks, no loss of activity
Sus scrofa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + N-ribosylnicotinamide
-
641173
Sus scrofa
ADP + nicotinamide ribonucleotide
-
641173
Sus scrofa
?
phosphate + inosine
-
641173
Sus scrofa
?
-
-
-
?
phosphate + nicotinamide riboside
-
641173
Sus scrofa
nicotinamide + ribose-1-phosphate
-
641173
Sus scrofa
r
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
nicotinamide riboside phosphorolysis
Sus scrofa
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
10
approx. 25% of maximal activity at pH 6.0, approx. 55% of maximal activity at pH 10, nicotinamide riboside phosphorolysis
Sus scrofa
Other publictions for EC 2.7.1.22
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738213
Zamporlini
Novel assay for simultaneous m ...
Homo sapiens
FEBS J.
281
5104-5119
2014
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
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-
4
-
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-
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-
-
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1
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-
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-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
679077
Belenky
Nicotinamide riboside promotes ...
Saccharomyces cerevisiae
Cell
129
473-484
2007
-
-
-
-
-
-
-
-
-
-
-
1
-
1
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1
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1
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1
-
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-
682879
Khan
Crystal structure of human nic ...
Homo sapiens
Structure
15
1005-1013
2007
-
-
1
1
4
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
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-
-
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1
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1
4
-
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-
1
-
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-
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-
-
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-
-
-
-
-
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-
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-
-
-
659066
Grose
Regulation of NAD synthesis by ...
Salmonella enterica
J. Bacteriol.
187
2774-2782
2005
-
-
1
-
1
-
1
2
-
1
-
1
-
2
-
-
1
1
-
-
1
-
3
-
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
1
-
-
1
-
2
-
1
-
1
-
-
-
1
-
-
1
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
680451
Merdanovic
Coupling of NAD+ biosynthesis ...
Haemophilus influenzae
J. Bacteriol.
187
4410-4420
2005
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
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-
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-
1
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-
1
-
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-
-
-
-
-
-
-
-
-
-
-
641174
Singh
Crystal structure of Haemophil ...
Haemophilus influenzae
J. Biol. Chem.
277
33291-33299
2002
-
-
1
1
-
-
-
-
-
-
3
-
-
3
-
-
1
-
-
-
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-
1
1
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1
-
1
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3
-
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-
1
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-
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-
1
1
-
-
-
-
-
-
-
-
-
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-
-
-
-
641175
Kurnasov
Ribosylnicotinamide kinase dom ...
Escherichia coli, Haemophilus influenzae, Salmonella enterica
J. Bacteriol.
184
6906-6917
2002
-
-
2
-
-
-
-
1
-
-
-
3
-
6
-
-
3
3
-
-
4
-
9
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
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-
-
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-
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1
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3
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3
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-
4
-
9
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
641173
Rowen
The phosphorolysis of nicotina ...
Sus scrofa
J. Biol. Chem.
193
497-507
1951
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
1
-
-
1
1
1
3
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
1
-
1
1
1
3
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-