Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.6.1.13 - ADP-ribose diphosphatase and Organism(s) Synechocystis sp. and UniProt Accession Q55928

for references in articles please use BRENDA:EC3.6.1.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.13 ADP-ribose diphosphatase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Synechocystis sp.
UNIPROT: Q55928 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Synechocystis sp.
The enzyme appears in selected viruses and cellular organisms
Synonyms
nudt5, nudt9, adp-ribose pyrophosphatase, adprase, atnudt7, adpribase-mn, atnudx7, adp-ribose hydrolase, nudt5 protein, adpr pyrophosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NMN adenylyltransferase/ADP-ribose pyrophosphatase
-
adenosine diphosphoribose pyrophosphatase
-
-
-
-
ADP-ribose diphosphatase
-
-
-
-
ADP-ribose phosphohydrolase
-
-
-
-
ADP-ribose pyrophosphatase
-
-
-
-
ADP-ribose pyrophosphatase Sll1054
-
-
ADP-ribose pyrophosphatase Slr0920
-
-
ADP-ribose pyrophosphatase Slr1134
-
-
ADPR-PPase
-
-
-
-
ADPRibase
-
-
-
-
ADPribose pyrophosphatase
-
-
-
-
pyrophosphatase, adenosine diphosphoribose
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate
show the reaction diagram
substrate binding mode in the active site of the ADPRase domain and catalytic mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
ADP-D-ribose ribophosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9024-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
show the reaction diagram
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.065 - 0.29
ADP-ribose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 20
ADP-ribose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme in complex with co-purified NAD and diphosphate complexed in the NadM-domain active site, and with ADPR substrate complexed in the Nudix-domain, hanging drop vapor diffusion method, 0.0015 ml of 15 mg/ml protein solution is mixed with an equal volume of reservoir solution containing 100 mM Tris, pH 7.5, and 1.5 M Li2SO4, 20°C, 3 days to 2 weeks, X-ray diffraction structure determination and analysis at 2.6 A resolution, selenomethionyl MAD phasing method
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain Bl21 by nickel affinity and anion exchange chromatography, and gel filtration
ADP-ribose pyrophosphatase Sll1054
-
ADP-ribose pyrophosphatase Slr0920
-
ADP-ribose pyrophosphatase Slr1134
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the His-tagged enzyme in Escherichia coli strain Bl21
expression in Escherichia coli, ADP-ribose pyrophosphatase Sll1054
-
expression in Escherichia coli, ADP-ribose pyrophosphatase Slr0920
-
expression in Escherichia coli, ADP-ribose pyrophosphatase Slr1134
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okuda, K.; Hayashi, H.; Nishiyama, Y.
Systematic characterization of the ADP-ribose pyrophosphatase family in the Cyanobacterium Synechocystis sp. strain PCC 6803
J. Bacteriol.
187
4984-4991
2005
Synechocystis sp.
Manually annotated by BRENDA team
Huang, N.; Sorci, L.; Zhang, X.; Brautigam, C.A.; Li, X.; Raffaelli, N.; Magni, G.; Grishin, N.V.; Osterman, A.L.; Zhang, H.
Bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase: structure and function in bacterial NAD metabolism
Structure
16
196-209
2008
Francisella tularensis (Q5NHR1), Francisella tularensis, Synechocystis sp. (Q55928), Synechocystis sp.
Manually annotated by BRENDA team