Information on EC 2.7.7.35 - ADP ribose phosphorylase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
2.7.7.35
-
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RECOMMENDED NAME
GeneOntology No.
ADP ribose phosphorylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ADP + D-ribose 5-phosphate = phosphate + ADP-D-ribose
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ADP:D-ribose-5-phosphate adenylyltransferase
The enzyme, characterized from the single-celled alga Euglena gracilis, catalyses an irreversible reaction in the direction of ADP formation. cf. EC 2.7.7.96, ADP-D-ribose pyrophosphorylase.
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CAS REGISTRY NUMBER
COMMENTARY hide
9054-55-1
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Chlorella pyrenoidosa
-
-
-
Manually annotated by BRENDA team
no activity in Chlorella sp.
-
-
-
Manually annotated by BRENDA team
no activity in Gloeocapsa sp.
-
-
-
Manually annotated by BRENDA team
no activity in Pisum sativum
-
-
-
Manually annotated by BRENDA team
no activity in Spinacia oleracea
-
-
-
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
phosphate + ADP
ADP + phosphate
show the reaction diagram
phosphate + ADP-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
phosphate + deamino-NAD+
?
show the reaction diagram
additional information
?
-
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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
phosphate + ADP-ribose
ADP + D-ribose 5-phosphate
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
weak, ADP-ribose phosphorolysis
ADP-ribose
-
competitive to phosphate
arsenate
D-ribose 5-phosphate
deoxyribose 5-phosphate
-
ADP/phosphate-exchange
IDP
-
weak, ADPribose phosphorolysis
additional information
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no activation by EDTA
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
ADP
0.04 - 0.05
ADP-ribose
0.4 - 0.5
phosphate
additional information
additional information
-
kinetic study
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 1.5
AMP
0.41 - 0.57
arsenate
1.3 - 2.9
ATP
0.09 - 4
D-ribose 5-phosphate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.51
-
partially purified enzyme
1.3
-
partially purified enzyme
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
ADP/phosphate-exchange
7.5 - 7.8
-
ADP/phosphate-exchange
7.8 - 8
-
-
8
-
ADP-ribose phosphorolysis
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4 - 8.1
-
ADP/phosphate-exchange, about half-maximal activity at pH 6.4 and pH 8.1
6.7 - 8.5
-
ADP/phosphate-exchange, about 60% of maximal activity at pH 6.7 and about half-maximal activity at pH 8.5
6.8 - 9
-
ADP-ribose phosphorolysis, about half-maximal activity at pH 6.8 and about 90% of maximal activity at pH 9.0
6.8 - 9.4
-
about half-maximal activity at pH 6.8 and pH 9.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29 - 56
-
about half-maximal activity at 29°C and 56°C
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
3 min, inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
solution of lyophilized enzyme, 2 mg/ml, stable to repeated freeze-thaw cycles during 2 weeks
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, undialyzed purified enzyme, lyophilized and placed under vacuum, 35% loss of activity within 2 months
-
frozen, fairly stable in the presence of EDTA
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.7.35)
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)