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Information on EC 2.7.7.35 - ADP ribose phosphorylase
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2.7.7.35 ADP ribose phosphorylaseIUBMB Comments
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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The enzyme appears in viruses and cellular organisms
Synonyms
adenosine diphosphoribose phosphorylase, adenylyltransferase, ribose 5-phosphate, ADP ribose phosphorylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine diphosphoribose phosphorylase
-
-
-
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adenylyltransferase, ribose 5-phosphate
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-
-
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ADP ribose phosphorylase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ADP + D-ribose 5-phosphate = phosphate + ADP-D-ribose
ping-pong reaction mechanism
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ADP + D-ribose 5-phosphate = phosphate + ADP-D-ribose
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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-
-
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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
9054-55-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphate + ADP
ADP + phosphate
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ADP/phosphate-exchange reaction, inorganic phosphate is incorporated into terminal position of ADP
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r
phosphate + ADP
ADP + phosphate
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IDP can replace ADP with 16% efficiency
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r
phosphate + ADP
ADP + phosphate
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IDP can replace ADP with 16% efficiency
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r
phosphate + ADP
ADP + phosphate
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IDP can replace ADP with 16% efficiency
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r
phosphate + ADP-ribose
ADP + D-ribose 5-phosphate
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highly specific
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ir
phosphate + ADP-ribose
ADP + D-ribose 5-phosphate
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highly specific
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ir
phosphate + deamino-NAD+
?
-
inosine diphosphoribose, not adenosine triphosphoribose
-
-
?
phosphate + deamino-NAD+
?
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inosine diphosphoribose, not adenosine triphosphoribose
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-
?
additional information
?
-
-
no activity with CDP, GDP, UDP, ADP-glucose and UDP-glucose
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-
?
additional information
?
-
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no activity with crude polyadenylic acid, RNA from Euglena, and NAD(H), NADP(H), coenzyme A, FAD
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?
additional information
?
-
-
no activity with CDP, GDP, UDP, ADP-glucose and UDP-glucose
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-ribose 5-phosphate
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competitive to phosphate with ADP, noncompetitive to phosphate with ADP-ribose
additional information
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no inhibition by CN-, 1,10-phenanthroline, 2,2'-dipyridyl, ribose 1-phosphate, ribose 1,5-diphosphate, glucose 1-phosphate, glucose 6-phosphate; no inhibition by NADP+, EDTA, ribose
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additional information
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no inhibition by adenosine, deoxyadenosine, 3'-AMP, CMP, CDP, UDP, NADH, NAD+, ADPglucose, UDPglucose, IAA, NEM; no inhibition by NADP+, EDTA, ribose
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
heterotrophically or autotrophically grown cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Evans, W.R.; Pietro, A.S.
Phosphorolysis of adenosine diphosphoribose
Arch. Biochem. Biophys.
113
236-244
1966
Euglena gracilis, no activity in Chlorella sp., no activity in Gloeocapsa sp., no activity in Pisum sativum, no activity in Spinacia oleracea, Ochromonas danica
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Stern, A.I.; Avron, M.
An adenosine 5-diphosphate ribose:orthophosphate adenylyltransferase from Euglena gracilis
Biochim. Biophys. Acta
118
577-591
1966
Euglena gracilis, no activity in Chlorella pyrenoidosa
brenda
Evans, W.R.
Adenosine diphosphoribose phosphorylase from Euglena gracilis
Methods Enzymol.
23A
566-570
1971
Euglena gracilis, Ochromonas danica
-
brenda
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