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Information on EC 3.1.7.2 - guanosine-3',5'-bis(diphosphate) 3'-diphosphatase
for references in articles please use BRENDA:EC3.1.7.2
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.7 Diphosphoric-monoester hydrolases
3.1.7.2 guanosine-3',5'-bis(diphosphate) 3'-diphosphatase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 3.1.7.2
- rela
-
alarmone
- rsh
- synthetases
-
tetra
-
sass
-
di-gmp
-
pppgpp-mediated
-
enterococcal
-
pppgpp0
- medicine
showSynonyms
mesh1, (p)ppgpp synthetase/hydrolase, ppgpp hydrolase, hddc3, (ppgpp)ase, metazoan spot homolog-1, more
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SYNONYM 
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
-
-
-
-
MESH1
metazoan SpoT homolog-1
penta-phosphate guanosine-3'-diphosphohydrolase
-
-
-
-
penta-phosphate guanosine-3'-pyrophosphohydrolase
-
-
-
-
ppGpp hydrolase
ppGpp phosphohydrolase
-
-
-
-
ppGpp-3'-pyrophosphohydrolase
-
-
-
-
pyrophosphatase, guanosine 3',5'-bis(diphosphate) 3'-
-
-
-
-
RelSeq
SpoT
metazoan SpoT homolog-1
-
Mesh1 consists only of the hydrolase domain of bacterial SpoT and lack the synthetase and regulatory domains
metazoan SpoT homolog-1
-
Mesh1 consists only of the hydrolase domain of bacterial SpoT and lack the synthetase and regulatory domains
ppGpp hydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
guanosine 3',5'-bis(diphosphate) + H2O = GDP + diphosphate
-
-
-
-
guanosine 3',5'-bis(diphosphate) + H2O = GDP + diphosphate
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
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
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
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
guanosine-3',5'-bis(diphosphate) 3'-diphosphohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
70457-12-4
-
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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
ppGpp + H2O
Gpp + diphosphate
-
Substrates: i.e. guanosine-3',5'-bis(diphosphate)
Products: i.e. guanosine 5'-diphosphate
Products: i.e. guanosine 5'-diphosphate
?, r
ppGpp + H2O
Gpp + diphosphate
-
Substrates: i.e. guanosine-3',5'-bis(diphosphate)
Products: i.e. guanosine 5'-diphosphate
Products: i.e. guanosine 5'-diphosphate
?, r
ppGpp + H2O
Gpp + diphosphate
-
Substrates: i.e. guanosine-3',5'-bis(diphosphate)
Products: i.e. guanosine 5'-diphosphate
Products: i.e. guanosine 5'-diphosphate
?, r
ppGpp + H2O
ppG + diphosphate
-
Substrates: i.e. guanosine-3',5'-bis(diphosphate)
Products: i.e. guanosine 5'-diphosphate
Products: i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
-
Substrates: i.e. guanosine-3',5'-bis(diphosphate)
Products: i.e. guanosine 5'-diphosphate
Products: i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
-
Substrates: i.e. guanosine-3',5'-bis(diphosphate)
Products: i.e. guanosine 5'-diphosphate
Products: i.e. guanosine 5'-diphosphate
?
ppGpp + H2O
ppG + diphosphate
-
Substrates: -
Products: -
Products: -
?
ppGpp + H2O
ppG + diphosphate
-
Substrates: the substrate functions as a pleiotropic effector restricting metabolic processes such as synthesis of purine nucleotides, glycolytic esters, phospholipids, rRNA, tRNA, mRNA
Products: -
Products: -
?
ppGpp + H2O
ppG + diphosphate
-
Substrates: the enzyme may be a bifunctional protein catalyzing either ppGpp synthesis or degradation
Products: -
Products: -
?
ppGpp + H2O
ppG + diphosphate
-
Substrates: i.e. guanosine-3',5'-bis(diphosphate)
Products: i.e. guanosine 5'-diphosphate
Products: i.e. guanosine 5'-diphosphate
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: only ppGpp, and no other nucleotide, is effectively hydrolyzed by human MESH1
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
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
additional information
?
-
-
Substrates: only ppGpp, and no other nucleotide, is effectively hydrolyzed by human MESH1
Products: -
Products: -
?
ppGpp + H2O
Gpp + diphosphate
-
Substrates: i.e. guanosine-3',5'-bis(diphosphate)
Products: i.e. guanosine 5'-diphosphate
Products: i.e. guanosine 5'-diphosphate
r
ppGpp + H2O
Gpp + diphosphate
-
Substrates: i.e. guanosine-3',5'-bis(diphosphate)
Products: i.e. guanosine 5'-diphosphate
Products: i.e. guanosine 5'-diphosphate
r
ppGpp + H2O
Gpp + diphosphate
-
Substrates: i.e. guanosine-3',5'-bis(diphosphate)
Products: i.e. guanosine 5'-diphosphate
Products: i.e. guanosine 5'-diphosphate
r
ppGpp + H2O
ppG + diphosphate
-
Substrates: -
Products: -
Products: -
?
ppGpp + H2O
ppG + diphosphate
-
Substrates: the substrate functions as a pleiotropic effector restricting metabolic processes such as synthesis of purine nucleotides, glycolytic esters, phospholipids, rRNA, tRNA, mRNA
Products: -
Products: -
?
ppGpp + H2O
ppG + diphosphate
-
Substrates: the enzyme may be a bifunctional protein catalyzing either ppGpp synthesis or degradation
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
Mn2+
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+
required. A manganese ion is coordinated within the central cavity by two histidine residues (H40, H70) and two aspartates (D71, D131)
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Levallorphan
-
inhibitory action on the low molecular weight activation factor
Uncharged tRNA
-
the ppGpp hydrolase activity is controlled by the concentration of uncharged tRNA
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
activation by a low moelcular weight activation factor and ATP, inhibited by levallorphan
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Abscess
Transcriptome analysis of Enterococcus faecalis during mammalian infection shows cells undergo adaptation and exist in a stringent response state.
Infections
Transcriptome analysis of Enterococcus faecalis during mammalian infection shows cells undergo adaptation and exist in a stringent response state.
Neoplasms
The regulation of ferroptosis by MESH1 through the activation of the integrative stress response.
Starvation
A meet-up of two second messengers: the c-di-AMP receptor DarB controls (p)ppGpp synthesis in Bacillus subtilis.
Starvation
A metazoan ortholog of SpoT hydrolyzes ppGpp and functions in starvation responses.
Starvation
Stringent response governs the oxidative stress resistance and virulence of Francisella tularensis.
Tuberculosis
Atomic structure of, and valine binding to the regulatory ACT domain of the Mycobacterium tuberculosis Rel protein.
Tuberculosis
Functional regulation of the opposing (p)ppGpp synthetase/hydrolase activities of RelMtb from Mycobacterium tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.604
pppGpp
presence of Mn2+, 37°C, pH not specified in the publication
0.378
ppGpp
presence of Mn2+, 37°C, pH not specified in the publication
0.41
ppGpp
-
pH 8.0, 30°C, KM is increased 3fold in the presence of the complex containing tRNA, ribosomes, and mRNA
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.97
ppGpp
-
pH 8.0, 30°C, kcat is reduced 2fold in the presence of the complex containing tRNA, ribosomes, and mRNA
3 - 6
ppGpp
-
pH 8.0, 30°C, kcat is reduced 2fold in the presence of the complex containing tRNA, ribosomes, and mRNA
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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
9.58
ppGpp
-
pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional (p)ppGpp synthase/hydrolase SpoT, catalyzes reactions of EC 2.7.6.5 and EC 3.1.7.2
UniProt
brenda
bifunctional (p)ppGpp synthase/hydrolase SpoT, catalyzes reactions of EC 2.7.6.5 and EC 3.1.7.2
UniProt
brenda
bifunctional (p)ppGpp synthase/hydrolase SpoT, catalyzes reactions of EC 2.7.6.5 and EC 3.1.7.2
UniProt
brenda
bifunctional (p)ppGpp synthase/hydrolase SpoT, catalyzes reactions of EC 2.7.6.5 and EC 3.1.7.2
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the C-terminal domain interacts with the ribosome, which is largely dependent on the TGS motif
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
Mesh1 deletion impairs starvation resistance in Drosophila, overview
physiological function
additional information
-
crucial residues for the ppGpp hydrolysis activity of Mesh1 are Arg24, Glu65, Asp66 and Asn126
physiological function
the level of ppGpp controls the length of diauxic lag via control of the level of acetyl phosphate
physiological function
in vivo, under relaxed conditions, as well as in vitro, the C-terminal regulatory domain CTD inhibits synthetase activity but is not required for hydrolase activity. Under stringent conditions, the CTD is essential for (p)ppGpp synthesis. A mutant lacking the CTD exhibits net hydrolase activity when expressed in Staphylococcus aureus but net (p)ppGpp synthetase activity when expressed in Escherichia coli. The conserved TGS and DC motifs within the CTD are required for correct stringent response, whereas the conserved ACT motif is dispensable. The enzyme primarily exists in a synthetase-off/hydrolase-on state
physiological function
SpoT requires the ACT domain to efficiently hydrolyze (p)ppGpp. The phosphorylated version of EIIANtr interacts directly with the ACT and inhibits the hydrolase activity of SpoT
physiological function
anti-sigma factor Rsd directly interacts with SpoT and stimulates its (p)ppGpp hydrolase activity. Dephosphorylated histidine-containing phosphocarrier protein HPr of the phosphoenolpyruvate-dependent sugar phosphotransferase system can antagonize the stimulatory effect of Rsd on SpoT (p)ppGpp hydrolase activity
physiological function
Mesh1 overexpression in Escherichia coli strongly suppresses cell growth in amino acid-free minimal medium through dramatically lowering the cellular ppGpp level. Escherichia coli cells overexpressing the Mesh1 H62F variant lacking the ppGpp hydrolyzing activity, exhibit no growth defects in all the growth conditions tested
physiological function
-
RSH1 is all able to complete growth of an Escherichia coli SpoT/RelA double mutant. RSH1 is a bifunctional RSH enzyme with both (p)ppGpp synthetase and hydrolase activity. Isoforms RSH4a and RSH4b are exclusive (p)ppGpp synthetase enzymes
physiological function
A Brucella abortus Rsh deletion mutant is unable to grow in minimal medium, it is unable to survive in stationary phase in rich medium and it is unable to proliferate inside RAW 264.7 macrophages
physiological function
enzyme promiscuously hydrolyses (p)ppGpp and (p)ppApp in a strictly manganese-dependent manner. The activity is dispensable for Pseudomonas aeruginosa growth or swimming, swarming, and twitching motilities, but is required for biofilm formation. (p)ppApp-degradation by SAH provides protection against the type VI secretion system (p)ppApp synthetase effector Tas1
physiological function
-
SpoT requires the ACT domain to efficiently hydrolyze (p)ppGpp. The phosphorylated version of EIIANtr interacts directly with the ACT and inhibits the hydrolase activity of SpoT
-
physiological function
Brucella abortus bv. 1 9-941
-
A Brucella abortus Rsh deletion mutant is unable to grow in minimal medium, it is unable to survive in stationary phase in rich medium and it is unable to proliferate inside RAW 264.7 macrophages
-
Show AA Sequence and Transmembrane Helices (4670 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
MESH1 consists only of the hydrolase domain of bacterial SpoT and lack the synthetase and regulatory domains, structure comparisons, overview
additional information
-
MESH1 consists only of the hydrolase domain of bacterial SpoT and lack the synthetase and regulatory domains, structure comparisons, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E319Q
mutant lacks (p)ppGpp synthase activity but retains hydrolase activity
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
D71A
mutation of metal-coordinating residue, completely abolished the ability to degrade ppGpp
H70A
mutation of metal-coordinating residue, completely abolished the ability to degrade ppGpp
K100A
about 40% residual activity with ppGpp, about 80% with pppGpp
additional information
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
additional information
-
diverse deletion mutants show synthesis and degradation activities differing from those of full-length enzyme
additional information
-
diverse deletion mutants show synthesis and degradation activities differing from those of full-length enzyme
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant full-length enzyme from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of relSeq fragments and the expression is regulated using pBAD vectors
-
expression in Escherichia coli
recombinant expression of full-length enzyme in Escherichia coli and in HEK-293T cells
-
recombinant expression of full-length enzyme in Escherichia coli and in S2 cells
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
-
RelMtb is a key factor in Mycobacterium tuberculosis pathogenesis by regulating th intracellular concentration of (p)ppGpp.
analysis
assay to detect (p)ppGpp hydrolase activity using the Escherichia coli RelA/SpoT203 mutant strain. In this mutant strain SpoT is defective for (p)ppGpp hydrolase activity while retaining (p)ppGpp synthetase activity, which results in the constitutive over-accumulation of (p)ppGpp and a slow growth phenotype. Normal growth can be restored by expression of an enzyme with (p)ppGpp hydrolase activity
analysis
-
assay to detect (p)ppGpp hydrolase activity using the Escherichia coli RelA/SpoT203 mutant strain. In this mutant strain SpoT is defective for (p)ppGpp hydrolase activity while retaining (p)ppGpp synthetase activity, which results in the constitutive over-accumulation of (p)ppGpp and a slow growth phenotype. Normal growth can be restored by expression of an enzyme with (p)ppGpp hydrolase activity
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Belitzky, B.R.; Shakulov, R.S.
Functioning of spo T gene product in Bacillus subtilis cells
FEBS Lett.
138
226-228
1982
Bacillus subtilis
brenda
Sy, J.
Activation of ppGpp-3-pyrophosphohydrolase by a supernatant factor and ATP
J. Biol. Chem.
255
10056-10059
1980
Escherichia coli
brenda
Richter, D.
Uncharged tRNA inhibits guanosine 3,5-bis (diphosphate) 3-pyrophosphohydrolase [ppGppase], the spoT gene product, from Escherichia coli
Mol. Gen. Genet.
178
325-327
1980
Escherichia coli
brenda
Richter, D.
In vitro degradation of guanosine 3,5-bis(diphosphate) [ppGpp] by the spoT gene product [ppGppase] from auxotrophic strains of Escherichia coli: effects of various antibiotics and drugs
Arch. Microbiol.
124
229-232
1980
Escherichia coli
brenda
Richter, D.; Fehr, S.; Harder, R.
The guanosine 3,5-bis(diphosphate) (ppGpp) cycle. Comparison of synthesis and degradation of guanosine 3,5-bis(diphosphate) in various bacterial systems
Eur. J. Biochem.
99
57-64
1979
Bacillus subtilis, Brevibacillus brevis, Escherichia coli, Geobacillus stearothermophilus
brenda
An, G.; Justesen, J.; Watson, R.J.; Friesen, J.D.
Cloning the spoT gene of Escherichia coli: identification of the spoT gene product
J. Bacteriol.
137
1100-1110
1979
Escherichia coli
brenda
Heinemeyer, E.A.; Richter, D.
Characterization of the guanosine 5-triphosphate 3-diphosphate and guanosine 5-diphosphate 3-diphosphate degradation reaction catalyzed by a specific pyrophosphorylase from Escherichia coli
Biochemistry
17
5368-5372
1978
Escherichia coli
brenda
Xiao, H.; Kalman, M.; Ikehara, K.; Zemel, S.; Glaser, G.; Cashel, M.
Residual guanosine 3',5'-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations
J. Biol. Chem.
266
5980-5990
1991
Escherichia coli
brenda
Murray, K.D.; Bremer, H.
Control of spoT-dependent ppGpp synthesis and degradation in Escherichia coli
J. Mol. Biol.
259
41-57
1996
Escherichia coli
brenda
Avarbock, D.; Avarbock, A.; Rubin, H.
Differential regulation of opposing RelMtb activities by the aminoacylation state of a tRNA ribosome mRNA elMtb complex
Biochemistry
39
11640-11648
2000
Mycobacterium tuberculosis
brenda
Mechold, U.; Murphy, H.; Brown, L.; Cashel, M.
Intramolecular regulation of the opposing (p)ppGpp catalytic activities of RelSeq, the Rel/Spo enzyme from Streptococcus equisimilis
J. Bacteriol.
184
2878-2888
2002
Streptococcus dysgalactiae subsp. equisimilis, Streptococcus dysgalactiae subsp. equisimilis H46A
brenda
Avarbock, A.; Avarbock, D.; Teh, J.S.; Buckstein, M.; Wang, Z.m.; Rubin, H.
Functional Regulation of the Opposing (p)ppGpp Synthetase/Hydrolase Activities of RelMtb from Mycobacterium tuberculosis
Biochemistry
44
9913-9923
2005
Mycobacterium tuberculosis
brenda
Sun, D.; Lee, G.; Lee, J.H.; Kim, H.Y.; Rhee, H.W.; Park, S.Y.; Kim, K.J.; Kim, Y.; Kim, B.Y.; Hong, J.I.; Park, C.; Choy, H.E.; Kim, J.H.; Jeon, Y.H.; Chung, J.
A metazoan ortholog of SpoT hydrolyzes ppGpp and functions in starvation responses
Nat. Struct. Mol. Biol.
17
1188-1194
2010
Drosophila melanogaster, Homo sapiens
brenda
Fernandez-Coll, L.; Cashel, M.
Contributions of SpoT hydrolase, SpoT synthetase, and RelA synthetase to carbon source diauxic growth transitions in Escherichia coli
Front. Microbiol.
9
1802
2018
Escherichia coli (P0AG24)
brenda
Ronneau, S.; Caballero-Montes, J.; Coppine, J.; Mayard, A.; Garcia-Pino, A.; Hallez, R.
Regulation of (p)ppGpp hydrolysis by a conserved archetypal regulatory domain
Nucleic Acids Res.
47
843-854
2019
Caulobacter vibrioides (A0A0H3C9W6), Caulobacter vibrioides, Caulobacter vibrioides NA1000 (A0A0H3C9W6)
brenda
Gratani, F.; Horvatek, P.; Geiger, T.; Borisova, M.; Mayer, C.; Grin, I.; Wagner, S.; Steinchen, W.; Bange, G.; Velic, A.; Macek, B.; Wolz, C.
Regulation of the opposing (p)ppGpp synthetase and hydrolase activities in a bifunctional RelA/SpoT homologue from Staphylococcus aureus
PLoS Genet.
14
e1007514
2018
Staphylococcus aureus (W8U368)
brenda
Lee, J.W.; Park, Y.H.; Seok, Y.J.
Rsd balances (p)ppGpp level by stimulating the hydrolase activity of SpoT during carbon source downshift in Escherichia coli
Proc. Natl. Acad. Sci. USA
115
E6845-E6854
2018
Escherichia coli (P0AG24), Escherichia coli
brenda
Steinchen, W.; Ahmad, S.; Valentini, M.; Eilers, K.; Majkini, M.; Altegoer, F.; Lechner, M.; Filloux, A.; Whitney, J.C.; Bange, G.
Dual role of a (p)ppGpp- and (p)ppApp-degrading enzyme in biofilm formation and interbacterial antagonism
Mol. Microbiol.
115
1339-1356
2021
Pseudomonas aeruginosa (Q9I686)
brenda
Zhu, M.; Dai, X.
Growth suppression by altered (p)ppGpp levels results from non-optimal resource allocation in Escherichia coli
Nucleic Acids Res.
47
4684-4693
2019
Drosophila melanogaster (Q9VAM9)
brenda
Van der Henst, M.; Carlier, E.; De Bolle, X.
Intracellular growth and cell cycle progression are dependent on (p)ppGpp synthetase/hydrolase in Brucella abortus
Pathogens
9
571
2020
Brucella abortus bv. 1 (Q57E90), Brucella abortus bv. 1 9-941 (Q57E90)
brenda
Avilan, L.; Puppo, C.; Villain, A.; Bouveret, E.; Menand, B.; Field, B.; Gontero, B.
RSH enzyme diversity for (p)ppGpp metabolism in Phaeodactylum tricornutum and other diatoms
Sci. Rep.
9
17682
2019
Escherichia coli (P0AG24), Phaeodactylum tricornutum
brenda
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