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Information on EC 2.7.6.5 - GTP diphosphokinase
for references in articles please use BRENDA:EC2.7.6.5
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.6 Diphosphotransferases
2.7.6.5 GTP diphosphokinase
IUBMB Comments
GDP can also act as acceptor.
The enzyme appears in viruses and cellular organisms
- 2.7.6.5
- pppgpp
- rela
- rsh
- tetraphosphate
-
a-site
-
actinorhodine
- mupirocin
-
ribosome-dependent
-
sass
- 3'-diphosphate
-
rela-spot
- thiostrepton
-
pyrophosphorylate
-
rela-dependent
- drug development
Synonyms
(p)ppgpp synthetase, stringent factor, relmtb, (p)ppgpp synthase, alarmone synthetase, gtp pyrophosphokinase, sas 1, (p)ppgpp synthetase i, guanosine pentaphosphate synthetase, atp:gtp 3'-pyrophosphotransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(p)ppGpp synthase
(p)ppGpp synthetase
(p)ppGpp synthetase I
-
-
-
-
(p)ppGpp synthetase II
-
-
-
-
alarmone synthetase
ATP-GTP 3'-diphosphotransferase
-
-
-
-
ATP:GTP 3'-pyrophosphotransferase
ATP:GTP pyrophosphoryl transferase
GPSI
-
-
-
-
GPSII
-
-
-
-
GTP pyrophosphokinase
guanosine 3',5'-polyphosphate synthase
-
-
-
-
guanosine 3',5'-polyphosphate synthetase
-
-
-
-
guanosine 5',3'-polyphosphate synthetase
-
-
-
-
guanosine pentaphosphate synthetase
-
-
-
-
ppGpp synthase I
Rel
RelA
RelMtb
SAS 1
SAS 2
SAS1
SF
small alarmone synthase 1
small alarmone synthase 2
small alarmone synthetase 1
stringent factor
YjbM
YwaC
GTP pyrophosphokinase
-
-
-
-
stringent factor
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
GDP can also act as acceptor
-
-
-
ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
bifunctional enzyme, additionally has polynucleotide phosphorylase activities
ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
the catalytic pathway of (p)ppGpp synthesis involves a sequentially ordered substrate binding, activation of ATP in a strained conformation, and transfer of diphosphate through a nucleophilic substitution (SN2) reaction. pppGpp, but not ppGpp, positively regulates the enzyme at an allosteric site
ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
the catalytic pathway of (p)ppGpp synthesis involves a sequentially ordered substrate binding, activation of ATP in a strained conformation, and transfer of diphosphate through a nucleophilic substitution (SN2) reaction. pppGpp, but not ppGpp, positively regulates the enzyme at an allosteric site
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diphosphate transfer
diphosphate transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:GTP 3'-diphosphotransferase
GDP can also act as acceptor.
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CAS REGISTRY NUMBER
COMMENTARY
63690-89-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-methyl-ATP + GTP
2'-methyl-AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
8-bromo-ATP + GTP
8-bromo-AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + guanosine 5'-tetraphosphate
AMP + guanosine 3'-diphosphate 5'-tetraphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + ITP
AMP + inosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
dATP + GTP
dAMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3',5'-bis-diphosphate
-
Substrates: the enzyme utilizes GDP less efficiently than GTP
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3',5'-bis-diphosphate
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
Substrates: the enzyme utilizes GDP less efficiently than GTP
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
Substrates: -
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
Substrates: -
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
-
Substrates: preferred substrate
Products: i.e ppGpp
Products: i.e ppGpp
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
-
Substrates: preferred substrate
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
Substrates: -
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: i.e. pppGpp
Products: i.e. pppGpp
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: RelA-mediated guanosine 3'-diphosphate 5'-triphosphate synthesis requires the presence of an uncharged tRNAVal in the A-Site of a mRNA programmed ribosome
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: high degree of specificity for GTP as a pyrophosphate acceptor, with no measurable turnover for GDP
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: the enzyme uses GTP approximately twice as well as GDP
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
Substrates: the enzyme uses GTP approximately twice as well as GDP
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 5'-triphosphate 3'-diphosphate
-
Substrates: -
Products: -
Products: -
r
ATP + GTP
AMP + guanosine 5'-triphosphate 3'-diphosphate
-
Substrates: -
Products: -
Products: -
r
ATP + GTP
AMP + guanosine 5'-triphosphate 3'-diphosphate
-
Substrates: -
Products: -
Products: -
r
ATP + GTP
AMP + guanosine 5'-triphosphate 3'-diphosphate
-
Substrates: bifunctional enzyme with synthetase and hydrolase activities
Products: -
Products: -
r
guanosine 3'-diphosphate 5'-diphosphate + H2O
GDP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-diphosphate + H2O
GDP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-diphosphate + H2O
GDP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-diphosphate + H2O
GDP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-triphosphate + H2O
GTP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-triphosphate + H2O
GTP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-triphosphate + H2O
GTP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-triphosphate + H2O
GTP + diphosphate
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is bifunctional showing synthase activity forming ppGpp and pppGpp, and hydrolase activity with the two compounds resulting in formation of GTP or GDP and diphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is bifunctional showing synthase activity forming ppGpp and pppGpp, and hydrolase activity with the two compounds resulting in formation of GTP or GDP and diphosphate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is bifunctional showing synthase activity forming ppGpp and pppGpp, and hydrolase activity with the two compounds resulting in formation of GTP or GDP and diphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: 5'(beta,gamma-imino)triphosphate, 1,N6-ethyladenosine triphosphate, no diphosphate acceptors: ATP, UTP, CTP, dGTP, dGDP, 2'-O-methyl-GDP, 7-methyl-GDP
Products: -
Products: -
?
additional information
?
-
-
Substrates: responsible for the synthesis of guanosine 3',5'-bisdiphosphate during stringent response to amino acid starvation
Products: -
Products: -
?
additional information
?
-
-
Substrates: (p)ppGpp synthetase II is responsible for (p)ppGpp accumulation during carbon source downshift
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme transfers a diphosphate from ATP to GDP or GTP to synthesize guanosine 3'-diphosphate 5'-diphosphate (ppGpp) and guanosine 3'-diphosphate 5'-triphosphate (pppGpp), respectively. Enzyme RelMtb also encodes a second, distinct catalytic domain that hydrolyzes (p)ppGpp into diphosphate and GDP or GTP
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme transfers a diphosphate from ATP to GDP or GTP to synthesize guanosine 3'-diphosphate 5'-diphosphate (ppGpp) and guanosine 3'-diphosphate 5'-triphosphate (pppGpp), respectively. Enzyme RelMtb also encodes a second, distinct catalytic domain that hydrolyzes (p)ppGpp into diphosphate and GDP or GTP
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme transfers a diphosphate from ATP to GDP or GTP to synthesize guanosine 3'-diphosphate 5'-diphosphate (ppGpp) and guanosine 3'-diphosphate 5'-triphosphate (pppGpp), respectively. Enzyme RelMtb also encodes a second, distinct catalytic domain that hydrolyzes (p)ppGpp into diphosphate and GDP or GTP
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also possesses a potent Mn2+-dependent guanosine tetraphosphate hydrolysis activity, with complete hydrolysis to GDP and diphosphate
Products: -
Products: -
?
additional information
?
-
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
Substrates: the enzyme also possesses a potent Mn2+-dependent guanosine tetraphosphate hydrolysis activity, with complete hydrolysis to GDP and diphosphate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
Substrates: -
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
Substrates: -
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
Substrates: -
Products: -
Products: -
?
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
Substrates: -
Products: -
Products: -
?
ATP + GTP
AMP + guanosine 5'-triphosphate 3'-diphosphate
-
Substrates: -
Products: -
Products: -
r
ATP + GTP
AMP + guanosine 5'-triphosphate 3'-diphosphate
-
Substrates: -
Products: -
Products: -
r
ATP + GTP
AMP + guanosine 5'-triphosphate 3'-diphosphate
-
Substrates: -
Products: -
Products: -
r
ATP + GTP
AMP + guanosine 5'-triphosphate 3'-diphosphate
-
Substrates: bifunctional enzyme with synthetase and hydrolase activities
Products: -
Products: -
r
guanosine 3'-diphosphate 5'-diphosphate + H2O
GDP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-diphosphate + H2O
GDP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-diphosphate + H2O
GDP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-diphosphate + H2O
GDP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-triphosphate + H2O
GTP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-triphosphate + H2O
GTP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-triphosphate + H2O
GTP + diphosphate
Substrates: -
Products: -
Products: -
?
guanosine 3'-diphosphate 5'-triphosphate + H2O
GTP + diphosphate
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: responsible for the synthesis of guanosine 3',5'-bisdiphosphate during stringent response to amino acid starvation
Products: -
Products: -
?
additional information
?
-
-
Substrates: (p)ppGpp synthetase II is responsible for (p)ppGpp accumulation during carbon source downshift
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme transfers a diphosphate from ATP to GDP or GTP to synthesize guanosine 3'-diphosphate 5'-diphosphate (ppGpp) and guanosine 3'-diphosphate 5'-triphosphate (pppGpp), respectively. Enzyme RelMtb also encodes a second, distinct catalytic domain that hydrolyzes (p)ppGpp into diphosphate and GDP or GTP
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme transfers a diphosphate from ATP to GDP or GTP to synthesize guanosine 3'-diphosphate 5'-diphosphate (ppGpp) and guanosine 3'-diphosphate 5'-triphosphate (pppGpp), respectively. Enzyme RelMtb also encodes a second, distinct catalytic domain that hydrolyzes (p)ppGpp into diphosphate and GDP or GTP
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme transfers a diphosphate from ATP to GDP or GTP to synthesize guanosine 3'-diphosphate 5'-diphosphate (ppGpp) and guanosine 3'-diphosphate 5'-triphosphate (pppGpp), respectively. Enzyme RelMtb also encodes a second, distinct catalytic domain that hydrolyzes (p)ppGpp into diphosphate and GDP or GTP
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
structure shows an iron-binding site at the dimer interface
Mg2+
Mn2+
Mg2+
-
required as a counter-ion for the nucleoside substrate, excess of Mg2+ is inhibitory
Mg2+
-
the magnesium concentration also affects the binding states of the tRNAs on the ribosome
Mg2+
-
the optimal concentration for pppGpp synthesis is approximately equal to the total concentration of nucleotide substrates([ATP] + [GTP])
Mg2+
-
the enzyme exploits a single Mg2+ ion to catalyze guanosine 3'-diphosphate 5'-triphosphate synthesis
Mg2+
-
essential for activation, the enzyme has a single Mg2+ binding site
Mn2+
-
the optimal concentration for pppGpp synthesis is approximately one-half of the total concentration of nucleotide substrates([ATP] + [GTP])
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mg2+
-
required as a counter ion for the nucleoside substrate, excess of Mg2+ is inhibitory
Mg2+
-
the enzyme shows a marked decrease in guanosine tetraphosphate synthesis activity with increasing Mg2+ ion concentration
tetracycline
-
endogenous diphoyphoryl transferase activity; ribosome-dependent activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dCDP
slightly stimulates synthesis of guanosine 3'-diphosphate 5'-triphosphate, inhibits polynucleotide phosphorylase activities of enzyme
ethanol
-
little activity unless activated either by a complex of 70S ribosomes, mRNA and uncharged tRNA or by a solvent like ethanol at approximately 20%
guanosine-5',3'-dibisphosphate
ppGpp, potential allosteric regulator, activates the enzyme with an EC50 of 0.060 mM
tRNA
-
uncharged or charged, stimulation, level of stimulation is greater in presence of RNA and poly(U) together than with either RNA alone
mRNA
-
little activity unless activated either by a complex of 70S ribosomes, mRNA and uncharged tRNA or by a solvent like ethanol at approximately 20%
mRNA
-
synthetic, e.g. poly(U), stimulates, level of stimulation is greater in presence of RNA and poly(U) together than with either RNA alone, no activation by ribosomes
additional information
-
little activity unless activated either by a complex of 70S ribosomes, mRNA and uncharged tRNA or by a solvent like ethanol at approximately 20%
-
additional information
-
addition of template, unacylated tRNA and ribosomes to the activity assay stimulates SF 30fold when using optimal conditions, activity of SF increases threefold in the presence of twice salt-washed tight-couple ribosomes and twofold in the presence of reassociated ribosomes compared to the endogenous activity of the enzyme
-
additional information
-
ribosome complexes formed with tight binding tRNAVal stimulate enzyme activity at lower concentrations than that required for ribosome complexes formed with the weaker binding tRNAPhe
-
additional information
activation of Francisella tularensis RelA by stalled ribosomal complexes formed with ribosomes purified from Escherichia coli MRE600, and significantly weaker activation with ribosomes isolated from Francisella philomiragia
-
additional information
-
GPS I can be activated by incubation with crude mycelial extract, activation is partially inhibited by the inclusion of trypsin inhibitor in reaction mixture
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Asthma
Asthma and sleep apnea in patients with morbid obesity: outcome after bariatric surgery.
Brucellosis
The stringent response mediator Rsh is required for Brucella melitensis and Brucella suis virulence, and for expression of the type IV secretion system virB.
Infections
Essential roles for Mycobacterium tuberculosis Rel beyond the production of (p)ppGpp.
Infections
Isolation of a lambda transducing bacteriophage carrying the relA gene of Escherichia coli.
Latent Infection
The role of RelMtb-mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice.
Persistent Infection
Essential roles for Mycobacterium tuberculosis Rel beyond the production of (p)ppGpp.
Persistent Infection
Stringent response protein as a potential target to intervene persistent bacterial infection.
Persistent Infection
The role of RelMtb-mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice.
Starvation
Combinatorial stress responses: direct coupling of two major stress responses in Escherichia coli.
Starvation
Induction of cat-86 by chloramphenicol and amino acid starvation in relaxed mutants of Bacillus subtilis.
Starvation
Inhibiting the stringent response blocks Mycobacterium tuberculosis entry into quiescence and reduces persistence.
Starvation
Intramolecular Interactions Dominate the Autoregulation of Escherichia coli Stringent Factor RelA.
Starvation
Regulation of Escherichia coli RelA requires oligomerization of the C-terminal domain.
Starvation
Stringent response of Bacillus stearothermophilus: evidence for the existence of two distinct guanosine 3',5'-polyphosphate synthetases.
Starvation
Subinhibitory Concentrations of Bacteriostatic Antibiotics Induce relA-Dependent and relA-Independent Tolerance to ?-Lactams.
Starvation
The global role of ppGpp synthesis in morphological differentiation and antibiotic production in Streptomyces coelicolor A3(2).
Starvation
The ribosome triggers the stringent response by RelA via a highly distorted tRNA.
Starvation
The stringent factor RelA adopts an open conformation on the ribosome to stimulate ppGpp synthesis.
Starvation
The stringent response is required for Helicobacter pylori survival of stationary phase, exposure to acid, and aerobic shock.
Tuberculosis
Essential roles for Mycobacterium tuberculosis Rel beyond the production of (p)ppGpp.
Tuberculosis
Functional regulation of the opposing (p)ppGpp synthetase/hydrolase activities of RelMtb from Mycobacterium tuberculosis.
Tuberculosis
Inhibiting the stringent response blocks Mycobacterium tuberculosis entry into quiescence and reduces persistence.
Tuberculosis
Mutational analysis of the (p)ppGpp synthetase activity of the Rel enzyme of Mycobacterium tuberculosis.
Tuberculosis
Stringent response protein as a potential target to intervene persistent bacterial infection.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
guanosine 3'-diphosphate 5'-diphosphate
pH 7.5, 37°C, recombinant enzyme
2
guanosine 3'-diphosphate 5'-triphosphate
pH 7.5, 37°C, recombinant enzyme
0.259 - 0.344
ATP
pH 8.0, 30°C, recombinant enzyme