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 hide
3.6.1.40
-
RECOMMENDED NAME
GeneOntology No.
guanosine-5'-triphosphate,3'-diphosphate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
guanosine 5'-triphosphate 3'-diphosphate + H2O = guanosine 3',5'-bis(diphosphate) + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric acid anhydride
-
-
-
-
PATHWAY
BRENDA Link
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.
CAS REGISTRY NUMBER
COMMENTARY hide
85130-44-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain CA10
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-
Manually annotated by BRENDA team
strain JF1599
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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 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
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
additional information
?
-
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
guanosine 5'-triphosphate,3'-diphosphate + H2O
guanosine 5'-diphosphate,3'-diphosphate + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
crystallization data
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 0.13
guanosine 5'-triphosphate,3'-diphosphate
0.13
Guanosine 5'-triphosphate,3'-monophosphate
-
-
0.0000005
Polyphosphate
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023
guanosine 5'-triphosphate,3'-diphosphate
Escherichia coli
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-
1.1
Polyphosphate
Escherichia coli
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.08
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crude extract
22
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NH4Cl precipitate
1513
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partially purified enzyme
7000
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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optimum activity in borate buffer
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
SDS-PAGE
100000
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gel filtration
140000
-
gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
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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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable at 4°C, storable in liquid nitrogen
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Purification/COMMENTARY
ORGANISM
UNIPROT
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
LITERATURE
expression of His-tagged Y19N mutant
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y19N
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site-directed mutagenesis, crystal structure
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