BRENDA - Enzyme Database show
show all sequences of 2.4.99.20

Channelling of substrate promiscuity of the skeletal-muscle ADP-ribosyl cyclase isoform

Bacher, I.; Zidar, A.; Kratzel, M.; Hohenegger, M.; Biochem. J. 381, 147-154 (2004)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Oryctolagus cuniculus
additional information
the cyclization reaction is insensitive to free Ca2+ concentration in the range 20 nM–100 microM. Mg2+ is not inhibitory
Oryctolagus cuniculus
NAD+
-
Oryctolagus cuniculus
NADP+
-
Oryctolagus cuniculus
nicotinamide
inhibition of the cyclization reaction and is 30fold more potent at suppressing the base-exchange reaction. Inhibition is not via a competition with the nicotinic acid-binding site
Oryctolagus cuniculus
Zn2+
-
Oryctolagus cuniculus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0334
-
NGDP+
pH 7.4, temperature not specified in the publication
Oryctolagus cuniculus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
of heavy sarcoplasmic reticulum
Oryctolagus cuniculus
16020
-
sarcoplasmic reticulum
membrane of heavy sarcoplasmic reticulum
Oryctolagus cuniculus
16529
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Oryctolagus cuniculus
-
skeletal muscle isoform
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2'-phospho-cyclic ADP-ribose + nicotinate
-
726898
Oryctolagus cuniculus
nicotinate-adenine dinucleotide phosphate
-
-
-
?
additional information
the cyclization reaction to form cADPr and cGDPr as well as the base-exchange reaction to form nicotinic acid adenine dinucleotide phosphate are strictly dependent on pH. Although the formation of cyclic GDP-ribose is optimized at pH 6, the synthesis of nicotinic acid adenine dinucleotide phosphate is most pronounced at a pH below 5. Nicotinic acid has virtually no influence on the cyclization reaction, but increases the affinity of NADP at an acidic pH and has the opposite effect at alkaline pH
726898
Oryctolagus cuniculus
?
-
-
-
-
NADP+
-
726898
Oryctolagus cuniculus
2'-phospho-cyclic ADP-ribose + nicotinamide
-
-
-
?
NGDP+
-
726898
Oryctolagus cuniculus
2'-phospho-cyclic GDP-ribose + nicotinamide
-
-
-
?
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.00027
-
formation of cGDPr, pH 7.4, temperature not specified in the publication
Oryctolagus cuniculus
Cu2+
0.0013
-
formation of cGDPr, pH 7.4, temperature not specified in the publication
Oryctolagus cuniculus
NADP+
0.0023
-
formation of cGDPr, pH 7.4, temperature not specified in the publication
Oryctolagus cuniculus
Zn2+
0.0054
-
formation of cGDPr, pH 7.4, temperature not specified in the publication
Oryctolagus cuniculus
NAD+
0.7
-
cyclization reaction, pH 7.4, temperature not specified in the publication
Oryctolagus cuniculus
nicotinamide
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.00027
-
formation of cGDPr, pH 7.4, temperature not specified in the publication
Oryctolagus cuniculus
Cu2+
0.0013
-
formation of cGDPr, pH 7.4, temperature not specified in the publication
Oryctolagus cuniculus
NADP+
0.0023
-
formation of cGDPr, pH 7.4, temperature not specified in the publication
Oryctolagus cuniculus
Zn2+
0.0054
-
formation of cGDPr, pH 7.4, temperature not specified in the publication
Oryctolagus cuniculus
NAD+
0.7
-
cyclization reaction, pH 7.4, temperature not specified in the publication
Oryctolagus cuniculus
nicotinamide
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Oryctolagus cuniculus
additional information
the cyclization reaction is insensitive to free Ca2+ concentration in the range 20 nM–100 microM. Mg2+ is not inhibitory
Oryctolagus cuniculus
NAD+
-
Oryctolagus cuniculus
NADP+
-
Oryctolagus cuniculus
nicotinamide
inhibition of the cyclization reaction and is 30fold more potent at suppressing the base-exchange reaction. Inhibition is not via a competition with the nicotinic acid-binding site
Oryctolagus cuniculus
Zn2+
-
Oryctolagus cuniculus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0334
-
NGDP+
pH 7.4, temperature not specified in the publication
Oryctolagus cuniculus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
of heavy sarcoplasmic reticulum
Oryctolagus cuniculus
16020
-
sarcoplasmic reticulum
membrane of heavy sarcoplasmic reticulum
Oryctolagus cuniculus
16529
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2'-phospho-cyclic ADP-ribose + nicotinate
-
726898
Oryctolagus cuniculus
nicotinate-adenine dinucleotide phosphate
-
-
-
?
additional information
the cyclization reaction to form cADPr and cGDPr as well as the base-exchange reaction to form nicotinic acid adenine dinucleotide phosphate are strictly dependent on pH. Although the formation of cyclic GDP-ribose is optimized at pH 6, the synthesis of nicotinic acid adenine dinucleotide phosphate is most pronounced at a pH below 5. Nicotinic acid has virtually no influence on the cyclization reaction, but increases the affinity of NADP at an acidic pH and has the opposite effect at alkaline pH
726898
Oryctolagus cuniculus
?
-
-
-
-
NADP+
-
726898
Oryctolagus cuniculus
2'-phospho-cyclic ADP-ribose + nicotinamide
-
-
-
?
NGDP+
-
726898
Oryctolagus cuniculus
2'-phospho-cyclic GDP-ribose + nicotinamide
-
-
-
?
Other publictions for EC 2.4.99.20
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)
727515
Schmid
CD38: a NAADP degrading enzyme ...
Homo sapiens, Mus musculus
FEBS Lett.
585
3544-3548
2011
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2
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2
2
-
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-
727868
Rah
Generation of cyclic ADP-ribos ...
Mus musculus
J. Biol. Chem.
285
21877-21887
2010
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1
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1
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1
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1
1
-
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-
726853
Moreschi
NAADP+ synthesis from cADPRP a ...
Aplysia californica, Axinella polypoides, Homo sapiens
Biochem. Biophys. Res. Commun.
345
573-580
2006
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3
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9
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9
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727857
Graeff
Acidic residues at the active ...
Homo sapiens
J. Biol. Chem.
281
28951-28957
2006
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-
1
1
5
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1
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1
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1
5
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726898
Bacher
Channelling of substrate promi ...
Oryctolagus cuniculus
Biochem. J.
381
147-154
2004
-
-
-
-
-
-
6
1
2
-
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1
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4
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5
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5
6
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1
2
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4
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724210
Chini
CD38 is the major enzyme respo ...
Mus musculus, Rattus norvegicus
Biochem. J.
362
125-130
2002
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4
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2
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2
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3
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7
4
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6
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1
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1
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4
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2
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7
4
-
6
-
1
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-
1
-
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-
3
3
-
-
-
726647
Lee
ADP-ribosyl cyclase and CD38. ...
Aplysia californica, Homo sapiens
Adv. Exp. Med. Biol.
419
411-419
1997
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1
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2
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8
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1
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8
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727816
Aarhus
ADP-ribosyl cyclase and CD38 c ...
Aplysia californica, Homo sapiens
J. Biol. Chem.
270
30327-30333
1995
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2
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2
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6
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2
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6
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