Information on EC 3.1.7.2 - guanosine-3',5'-bis(diphosphate) 3'-diphosphatase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.1.7.2
-
RECOMMENDED NAME
GeneOntology No.
guanosine-3',5'-bis(diphosphate) 3'-diphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
guanosine 3',5'-bis(diphosphate) + H2O = GDP + diphosphate
show the reaction diagram
-
-
-
-
guanosine 3',5'-bis(diphosphate) + H2O = GDP + diphosphate
show the reaction diagram
RelMtb is a dual-function enzyme carrying out ATP: GTP/GDP/ITP 3-diphosphoryltransferase and (p)ppGpp 3-diphosphohydrolase reactions. The differential regulation of the opposing activities of RelMtb is dependent on the ratio of uncharged to charged tRNA and the association of enzyme with a complex containing tRNA, ribosomes, and mRNA, i.e. RAC
-
guanosine 3',5'-bis(diphosphate) + H2O = GDP + diphosphate
show the reaction diagram
RelSeq affects ppGpp synthesis and degradation activities. The C-terminal domain of RelSeq is involved in reciprocal regulation of the two opposing activities present in the N-terminal domain
-
guanosine 3',5'-bis(diphosphate) + H2O = GDP + diphosphate
show the reaction diagram
RelSeq affects ppGpp synthesis and degradation activities. The C-terminal domain of RelSeq is involved in reciprocal regulation of the two opposing activities present in the N-terminal domain
Streptococcus dysgalactiae subsp. equisimilis H46A
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ppGpp biosynthesis
-
-
ppGpp biosynthesis
-
-
Purine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
guanosine-3',5'-bis(diphosphate) 3'-diphosphohydrolase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
(ppGpp)ase
-
-
-
-
3',5'-bis(diphosphate) 3'-pyrophosphate hydrolase
-
-
-
-
guanosine-3',5'-bis(diphosphate) 3'-diphosphohydrolase
-
-
-
-
guanosine-3',5'-bis(diphosphate) 3'-pyrophosphatase
-
-
-
-
penta-phosphate guanosine-3'-diphosphohydrolase
-
-
-
-
penta-phosphate guanosine-3'-pyrophosphohydrolase
-
-
-
-
ppGpp hydrolase
-
-
-
-
ppGpp phosphohydrolase
-
-
-
-
ppGpp-3'-pyrophosphohydrolase
-
-
-
-
pyrophosphatase, guanosine 3',5'-bis(diphosphate) 3'-
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
70457-12-4
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
spoT gene product
-
-
Manually annotated by BRENDA team
Streptococcus dysgalactiae subsp. equisimilis H46A
H46A
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
Mesh1 deletion impairs starvation resistance in Drosophila, overview
additional information
-
crucial residues for the ppGpp hydrolysis activity of Mesh1 are Arg24, Glu65, Asp66 and Asn126
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
the substrate functions as a pleiotropic effector restricting metabolic processes such as synthesis of purine nucleotides, glycolytic esters, phospholipids, rRNA, tRNA, mRNA
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
the enzyme may be a bifunctional protein catalyzing either ppGpp synthesis or degradation
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
the enzyme may be a bifunctional protein catalyzing either ppGpp synthesis or degradation
-
?
ppGpp + H2O
Gpp + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?, r
ppGpp + H2O
Gpp + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?, r
ppGpp + H2O
Gpp + diphosphate
show the reaction diagram
Streptococcus dysgalactiae subsp. equisimilis H46A
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
?, r
pppGpp + H2O
pppG + diphosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
only ppGpp, and no other nucleotide, is effectively hydrolyzed by human MESH1
-
-
-
additional information
?
-
-
activity detection by usage of the chemosensor pyrene and bis(Zn2+-dipicolylamine), which generates fluorescence at 470 nm when it specifically binds to ppGpp, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
-
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
the substrate functions as a pleiotropic effector restricting metabolic processes such as synthesis of purine nucleotides, glycolytic esters, phospholipids, rRNA, tRNA, mRNA
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
the enzyme may be a bifunctional protein catalyzing either ppGpp synthesis or degradation
-
?
ppGpp + H2O
ppG + diphosphate
show the reaction diagram
-
the enzyme may be a bifunctional protein catalyzing either ppGpp synthesis or degradation
-
?
ppGpp + H2O
Gpp + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
r
ppGpp + H2O
Gpp + diphosphate
show the reaction diagram
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
r
ppGpp + H2O
Gpp + diphosphate
show the reaction diagram
Streptococcus dysgalactiae subsp. equisimilis H46A
-
i.e. guanosine-3',5'-bis(diphosphate)
i.e. guanosine 5'-diphosphate
r
additional information
?
-
-
only ppGpp, and no other nucleotide, is effectively hydrolyzed by human MESH1
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
activation
Co2+
-
activation
K+
-
activation
K+
-
200-300 mM required for optimal activity
Mg2+
-
activation
Mg2+
-
activates, but less effective than Mn2+
Mn2+
-
activation
Mn2+
-
activation; required
Mn2+
-
required, the optimal concentration is a 2-3fold molar excess over the nucleotide substrate, the addition in excess of optimal concentration decreases the rate of hydrolysis
Mn2+
-
activates, required
NH4+
-
activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
chlorotetracycline
-
-
Levallorphan
-
inhibitory action on the low molecular weight activation factor
Levallorphan
-
-
tetracycline
-
-
Thiostrepton
-
-
Uncharged tRNA
-
-
-
Uncharged tRNA
-
the ppGpp hydrolase activity is controlled by the concentration of uncharged tRNA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
activation by a low moelcular weight activation factor and ATP, inhibited by levallorphan
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.41
ppGpp
-
pH 8.0, 30C, KM is increased 3fold in the presence of the complex containing tRNA, ribosomes, and mRNA
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.97
ppGpp
-
pH 8.0, 30C, kcat is reduced 2fold in the presence of the complex containing tRNA, ribosomes, and mRNA
3 - 6
ppGpp
-
pH 8.0, 30C, kcat is reduced 2fold in the presence of the complex containing tRNA, ribosomes, and mRNA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.46
ppGpp
-
pH not specified in the publication, temperature not specified in the publication
3703
9.58
ppGpp
-
pH not specified in the publication, temperature not specified in the publication
3703
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.46
-
enzyme fragment NH 1-24
0.7
-
enzyme fragment NH 1-385
52
-
full-length enzyme NC 1-739
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 8
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65000
-
sucrose density gradient centrifugation
135701
80000
-
calculation from sequence of the spotT gene
135702
130000
-
dimeric enzyme form, gel filtration
135701
260000
-
tetrameric enzyme form, gel filtration
135701
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
MESH1 consists only of the hydrolase domain of bacterial SpoT and lack the synthetase and regulatory domains, structure comparisons, overview
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant full-length enzyme from Escherichia coli
-
fragments of the relMtb protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant expression of full-length enzyme in Escherichia coli and in S2 cells
-
preparation of mutants with null alleles at both, spoT and relA
-
spotT gene
-
recombinant expression of full-length enzyme in Escherichia coli and in HEK-293T cells
-
expression of fragment proteins in Escherichia coli BL21(DE3)
-
the pET22b expression system is used
-
cloning of relSeq fragments and the expression is regulated using pBAD vectors
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D81A
-
loss of hydrolytic activity with retention of synthesis
DElTA1-86/DELTA395-738
-
contains only (p)ppGpp synthesis activity, no hydrolysis activity
DELTA182-738
-
fragment contains only (p)ppGpp hydrolysis activity, no synthesis activity
DELTA395-738
-
frament contains both synthesis and hydrolysis activities
G241E
-
loss of synthetic activity and retention of hydrolysis
H344Y
-
loss of synthetic activity and retention of hydrolysis
additional information
-
Mesh1 deletion by imprecise excision of a P-element from the Drosophila Mesh1 G3858 allele, resulting in the Drosophila Mesh1 null allele, Mesh1 5A3. The Mesh1 null mutant is much more susceptible than wild-type flies to death from amino acid starvation, and this susceptibility is also completely rescued by Mesh1 expression
H80A
-
loss of hydrolytic activity with retention of synthesis
additional information
-
diverse deletion mutants show synthesis and degradation activities differing from those of full-length enzyme
additional information
Streptococcus dysgalactiae subsp. equisimilis H46A
-
diverse deletion mutants show synthesis and degradation activities differing from those of full-length enzyme
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
RelMtb is a key factor in Mycobacterium tuberculosis pathogenesis by regulating th intracellular concentration of (p)ppGpp.