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Information on EC 3.6.1.40 - guanosine-5'-triphosphate,3'-diphosphate phosphatase and Organism(s) Escherichia coli and UniProt Accession P25552

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IUBMB Comments
Also hydrolyses other guanosine 5'-triphosphate derivatives with at least one unsubstituted phosphate group on the 3'-position, but not GTP, ATP or adenosine 5'-triphosphate 3'-diphosphate.
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This record set is specific for:
Escherichia coli
UNIPROT: P25552
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
pppgpp-5'-phosphohydrolase, exopolyphosphatase/guanosine pentaphosphate phosphohydrolase, guanosine pentaphosphatase, guanosine pentaphosphate phosphohydrolase, guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase, pppgpp phosphohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pppGpp phosphohydrolase
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guanosine 5'-triphosphate-3'-diphosphate 5'-phosphohydrolase
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guanosine pentaphosphatase
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guanosine pentaphosphate phosphatase
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guanosine pentaphosphate phosphohydrolase
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guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase
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phosphatase, guanosine 5'-triphosphate 3'-diphosphate 5'-
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pppGpp 5'-phosphohydrolase
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pppGpp-5'-phosphohydrolase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric acid anhydride
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
guanosine-5'-triphosphate,3'-diphosphate 5'-phosphohydrolase
Also hydrolyses other guanosine 5'-triphosphate derivatives with at least one unsubstituted phosphate group on the 3'-position, but not GTP, ATP or adenosine 5'-triphosphate 3'-diphosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
85130-44-5
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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
guanosine 5'-triphosphate 3'-diphosphate + H2O
guanosine 3',5'-bis(diphosphate) + phosphate
show the reaction diagram
-
-
-
?
guanosine 5'-triphosphate,3'-diphosphate + H2O
guanosine 5'-diphosphate,3'-diphosphate + phosphate
show the reaction diagram
guanosine 5'-triphosphate,3'-monophosphate + H2O
guanosine 5'-diphosphate,3'-monophosphate + phosphate
show the reaction diagram
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-
-
?
polyphosphate + H2O
?
show the reaction diagram
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-
-
-
?
pppGpNp + H2O
ppGpNp + phosphate
show the reaction diagram
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cleavage of 5'-phosphate ends of RNA
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?
pppGpNp-RNA + H2O
ppGpNp-RNA + phosphate
show the reaction diagram
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cleavage of 5'-phosphate ends of RNA, poor substrate
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?
additional information
?
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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
guanosine 5'-triphosphate 3'-diphosphate + H2O
guanosine 3',5'-bis(diphosphate) + phosphate
show the reaction diagram
-
-
-
?
guanosine 5'-triphosphate,3'-diphosphate + H2O
guanosine 5'-diphosphate,3'-diphosphate + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required for activity
K+
-
monovalent cation required, NH4+ preferred over K+, Na+ ineffective
Mg2+
-
required, optimum activity above 1 mM
NH4+
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monovalent cation required, NH4+ preferred over K+, Na+ ineffective
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04951
guanosine 5'-triphosphate 3'-diphosphate
at pH 7.4 and 37°C
0.11 - 0.13
guanosine 5'-triphosphate,3'-diphosphate
0.13
Guanosine 5'-triphosphate,3'-monophosphate
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-
0.0000005
Polyphosphate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.406
guanosine 5'-triphosphate 3'-diphosphate
at pH 7.4 and 37°C
0.023
guanosine 5'-triphosphate,3'-diphosphate
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1.1
Polyphosphate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1513
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partially purified enzyme
22
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NH4Cl precipitate
4.08
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crude extract
7000
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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optimum activity in borate buffer
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
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gel filtration
140000
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gel filtration
50000
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SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
2 * 233000, small-angle X-ray scattering
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, apoenzyme, using 10% (w/v) PEG 3350, 0.1 M HEPES (pH 7.5), and 0.2 M magnesium chloride
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable at 4°C, storable in liquid nitrogen
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Sephacryl S-200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli MG1655 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Keasling, J.D.; Bertsch, L.; Kornberg, A.
Guanosine pentaphosphate phosphohydrolase of Escherichia coli is a long-chain exopolyphosphatase
Proc. Natl. Acad. Sci. USA
90
7029-7033
1993
Escherichia coli, Escherichia coli CA10
Manually annotated by BRENDA team
Hara, A.; Sy, J.
Guanosine 5'-triphosphate, 3'-diphosphate 5'-phosphohydrolase. Purification and substrate specificity
J. Biol. Chem.
258
1678-1683
1983
Escherichia coli, Escherichia coli JF1599
Manually annotated by BRENDA team
Reizer, J.; Reizer, A.; Saier, M.H.
Exopolyphosphate phosphatase and guanosine pentaphosphate phosphatase belong to the sugar kinase/actin/hsp 70 superfamily
Trends Biochem. Sci.
18
247-248
1993
Escherichia coli
Manually annotated by BRENDA team
Song, H.; Dharmasena, M.N.; Wang, C.; Shaw, G.X.; Cherry, S.; Tropea, J.E.; Jin, D.J.; Ji, X.
Structure and activity of PPX/GppA homologs from Escherichia coli and Helicobacter pylori
FEBS J.
287
1865-1885
2019
Escherichia coli (P25552), Helicobacter pylori (C7BYL8), Helicobacter pylori B38 (C7BYL8)
Manually annotated by BRENDA team