Information on EC 3.6.1.40 - guanosine-5'-triphosphate,3'-diphosphate phosphatase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
3.6.1.40
-
RECOMMENDED NAME
GeneOntology No.
guanosine-5'-triphosphate,3'-diphosphate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
guanosine 5'-triphosphate 3'-diphosphate + H2O = guanosine 3',5'-bis(diphosphate) + phosphate
show the reaction diagram
-
-
-
-
guanosine 5'-triphosphate 3'-diphosphate + H2O = guanosine 3',5'-bis(diphosphate) + phosphate
show the reaction diagram
the hydrolytic base is E119, the dual specificity typical for the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family is due to a common active site for guanosine pentaphosphate and polyphosphate hydrolysis, R22 and R267, residing in different domains, are crucial for guanosine pentaphosphate specificity as they interact with the unique 3'-ribose phosphorylation
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric acid anhydride
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
ppGpp biosynthesis
-
Purine metabolism
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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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
exopolyphosphatase/guanosine pentaphosphate phosphohydrolase
-
-
guanosine 5'-triphosphate-3'-diphosphate 5'-phosphohydrolase
-
-
-
-
guanosine pentaphosphatase
-
-
-
-
guanosine pentaphosphate phosphatase
-
-
-
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guanosine pentaphosphate phosphohydrolase
-
-
-
-
phosphatase, guanosine 5'-triphosphate 3'-diphosphate 5'-
-
-
-
-
pppGpp 5'-phosphohydrolase
-
-
-
-
pppGpp-5'-phosphohydrolase
-
-
-
-
PPX/GPPA enzyme
-
-
guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase
-
-
-
-
additional information
-
the enzyme belongs to the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family
CAS REGISTRY NUMBER
COMMENTARY
85130-44-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain CA10
-
-
Manually annotated by BRENDA team
strain JF1599
-
-
Manually annotated by BRENDA team
Escherichia coli CA10
strain CA10
-
-
Manually annotated by BRENDA team
Escherichia coli JF1599
strain JF1599
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
guanosine 5'-triphosphate,3'-diphosphate + H2O
guanosine 5'-diphosphate,3'-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'-diphosphate + H2O
guanosine 5'-diphosphate,3'-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'-diphosphate + H2O
guanosine 5'-diphosphate,3'-diphosphate + phosphate
show the reaction diagram
-
involved in nutritional stress response via ppGpp
-
?
guanosine 5'-triphosphate,3'-diphosphate + H2O
guanosine 5'-diphosphate,3'-diphosphate + phosphate
show the reaction diagram
-
involved in nutritional stress response via ppGpp
-
?
guanosine 5'-triphosphate,3'-diphosphate + H2O
guanosine 5'-diphosphate,3'-diphosphate + phosphate
show the reaction diagram
-
substrate binding structure and involved residues, overview
-
-
?
guanosine 5'-triphosphate,3'-diphosphate + H2O
guanosine 5'-diphosphate,3'-diphosphate + phosphate
show the reaction diagram
Escherichia coli JF1599
-
-, involved in nutritional stress response via ppGpp
-
?
guanosine 5'-triphosphate,3'-diphosphate + H2O
guanosine 5'-diphosphate,3'-diphosphate + phosphate
show the reaction diagram
Escherichia coli CA10
-
-
-
?
guanosine 5'-triphosphate,3'-monophosphate + H2O
guanosine 5'-diphosphate,3'-monophosphate + phosphate
show the reaction diagram
Escherichia coli, Escherichia coli JF1599
-
-
-
?
guanosine 5'-triphosphate,3'-monophosphate-di(nucleotide monophosphate) + H2O
guanosine 5'-diphosphate,3'-monophosphate-di(nucleotide monophosphate) + phosphate
show the reaction diagram
-
cleavage of 5'-phosphate ends of RNA, poor substrate
-
?
guanosine 5'-triphosphate,3'-monophosphate-nucleotide monophosphate + H2O
guanosine 5'-diphosphate,3'-monophosphate-nucleotide monophosphate + phosphate
show the reaction diagram
Escherichia coli, Escherichia coli JF1599
-
cleavage of 5'-phosphate ends of RNA
-
?
additional information
?
-
-
not: GTP, ATP or adenosine 5'-triphosphate,3'-diphosphate, guanosine 5'-diphosphate,3'-diphosphate, guanosine 5'-triphosphate,3'-monophosphate-nucleotide, enzyme is rather nonspecific towards the 3'-OH substitutions of the substrates although a free, unsubstituted phosphate group at the 3'-OH position is essential
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-
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additional information
?
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enzyme also liberates phosphate by processive hydrolysis of the phosphoanhydride bonds of polyphosphate chains (1000 residues)
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-
-
additional information
?
-
Escherichia coli JF1599
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not: GTP, ATP or adenosine 5'-triphosphate,3'-diphosphate, guanosine 5'-diphosphate,3'-diphosphate, guanosine 5'-triphosphate,3'-monophosphate-nucleotide, enzyme is rather nonspecific towards the 3'-OH substitutions of the substrates although a free, unsubstituted phosphate group at the 3'-OH position is essential
-
-
-
additional information
?
-
Escherichia coli CA10
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enzyme also liberates phosphate by processive hydrolysis of the phosphoanhydride bonds of polyphosphate chains (1000 residues)
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
guanosine 5'-triphosphate,3'-diphosphate + H2O
guanosine 5'-diphosphate,3'-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'-diphosphate + H2O
guanosine 5'-diphosphate,3'-diphosphate + phosphate
show the reaction diagram
-
involved in nutritional stress response via ppGpp
-
?
guanosine 5'-triphosphate,3'-diphosphate + H2O
guanosine 5'-diphosphate,3'-diphosphate + phosphate
show the reaction diagram
-
involved in nutritional stress response via ppGpp
-
?
guanosine 5'-triphosphate,3'-diphosphate + H2O
guanosine 5'-diphosphate,3'-diphosphate + phosphate
show the reaction diagram
Escherichia coli JF1599
-
involved in nutritional stress response via ppGpp
-
?
guanosine 5'-triphosphate,3'-diphosphate + H2O
guanosine 5'-diphosphate,3'-diphosphate + phosphate
show the reaction diagram
Escherichia coli CA10
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
crystallization data
K+
-
monovalent cation required, NH4+ preferred over K+, Na+ ineffective
Mg2+
-
required, optimum activity above 1 mM
NH4+
-
monovalent cation required, NH4+ preferred over K+, Na+ ineffective
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.11
-
guanosine 5'-triphosphate,3'-diphosphate
-
-
0.13
-
guanosine 5'-triphosphate,3'-diphosphate
-
-
0.13
-
Guanosine 5'-triphosphate,3'-monophosphate
-
-
0.0000005
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Polyphosphate
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-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.023
-
guanosine 5'-triphosphate,3'-diphosphate
-
-
1.1
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Polyphosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.08
-
-
crude extract
22
-
-
NH4Cl precipitate
1513
-
-
partially purified enzyme
7000
-
-
purified enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
9
-
-
optimum activity in borate buffer
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
-
-
SDS-PAGE
100000
-
-
gel filtration
140000
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-
gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
PPX/GPPA Y19N mutant enzyme in complex with guanosine tetraphosphate, hanging-drop vapor diffusion method by mixing 0.002 ml of protein and 0.002 ml of reservoir solution containing 200 mM sodium acetate, pH 6.4, 100 mM 4-morpholineethanesulfonic acid, pH 5.7, and 50% methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.7 A resolution, modelling
-
two-domain structure, two crystal forms; X-ray diffraction structure determination and analysis of two crystal forms at 1.53 A and 2.15 A resolution, two domains
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unstable at 4°C, storable in liquid nitrogen
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His-tagged Y19N mutant by nickel affinity chromatography removal of His-tag, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of His-tagged Y19N mutant
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Y19N
-
site-directed mutagenesis, crystal structure