Information on EC 2.7.7.35 - ADP ribose phosphorylase

for references in articles please use BRENDA:EC2.7.7.35
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
2.7.7.35
-
top print hide
RECOMMENDED NAME
GeneOntology No.
ADP ribose phosphorylase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ADP + D-ribose 5-phosphate = phosphate + ADP-D-ribose
show the reaction diagram
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
top print hide
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.
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
9054-55-1
-
top print hide
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
top print hide
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
?
-
top print hide
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
top print hide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
top print hide
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
-
top print hide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no activation by EDTA
-
top print hide
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
-
top print hide
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
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.51
-
partially purified enzyme
1.3
-
partially purified enzyme
additional information
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.8
-
ADP/phosphate-exchange
7.5
-
ADP/phosphate-exchange
7.8 - 8
-
-
8
-
ADP-ribose phosphorolysis
top print hide
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
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29 - 56
-
about half-maximal activity at 29°C and 56°C
top print hide
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
top print hide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
3 min, inactivation
top print hide
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
solution of lyophilized enzyme, 2 mg/ml, stable to repeated freeze-thaw cycles during 2 weeks
-
top print hide
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
-
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
top
top
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)