Information on EC 2.7.7.35 - ADP ribose phosphorylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.7.35
-
RECOMMENDED NAME
GeneOntology No.
ADP ribose phosphorylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ADP + D-ribose 5-phosphate = phosphate + ADP-D-ribose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-55-1
-
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
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
?
-
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no activation by EDTA
-
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
-
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.51
-
partially purified enzyme
1.3
-
partially purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.8
-
ADP/phosphate-exchange
7.5
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ADP/phosphate-exchange
7.8 - 8
-
-
8
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ADP-ribose phosphorolysis
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4 - 8.1
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ADP/phosphate-exchange, about half-maximal activity at pH 6.4 and pH 8.1
6.7 - 8.5
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ADP/phosphate-exchange, about 60% of maximal activity at pH 6.7 and about half-maximal activity at pH 8.5
6.8 - 9
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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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29 - 56
-
about half-maximal activity at 29C and 56C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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3 min, inactivation
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
-15C, undialyzed purified enzyme, lyophilized and placed under vacuum, 35% loss of activity within 2 months
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frozen, fairly stable in the presence of EDTA
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE