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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
ppGpp biosynthesis
-
Purine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
guanosine-3',5'-bis(diphosphate) 3'-diphosphohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(p)ppGpp synthetase/hydrolase
-
-
(ppGpp)ase
-
-
-
-
3',5'-bis(diphosphate) 3'-pyrophosphate hydrolase
-
-
-
-
guanosine-3',5'-bis(diphosphate) 3'-diphosphohydrolase
-
-
-
-
guanosine-3',5'-bis(diphosphate) 3'-pyrophosphatase
-
-
-
-
HDDC3
-
-
metazoan SpoT homolog-1
-
Mesh1 consists only of the hydrolase domain of bacterial SpoT and lack the synthetase and regulatory domains
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
Streptococcus dysgalactiae subsp. equisimilis H46A
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
70457-12-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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 ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
activation by a low moelcular weight activation factor and ATP, inhibited by levallorphan
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9.46
-
ppGpp
-
pH not specified in the publication, temperature not specified in the publication
79417
9.58
-
ppGpp
-
pH not specified in the publication, temperature not specified in the publication
79417
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
65000
-
-
sucrose density gradient centrifugation
80000
-
-
calculation from sequence of the spotT gene
130000
-
-
dimeric enzyme form, gel filtration
260000
-
-
tetrameric enzyme form, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
recombinant full-length enzyme from Escherichia coli
-
fragments of the relMtb protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
RelMtb is a key factor in Mycobacterium tuberculosis pathogenesis by regulating th intracellular concentration of (p)ppGpp.