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Information on EC 2.7.6.5 - GTP diphosphokinase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WHG9

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     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.
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WHG9
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Synonyms
(p)ppgpp synthetase, stringent factor, relmtb, (p)ppgpp synthase, alarmone synthetase, gtp pyrophosphokinase, (p)ppgpp synthetase i, guanosine pentaphosphate synthetase, sas 1, (p)ppgpp synthetase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(p)ppGpp synthetase
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(p)ppGpp synthetase I
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-
-
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(p)ppGpp synthetase II
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-
-
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(p)ppGpp synthetase/hydrolase
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ATP-GTP 3'-diphosphotransferase
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-
-
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GPSI
-
-
-
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GPSII
-
-
-
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GTP pyrophosphokinase
-
-
-
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guanosine 3',5'-polyphosphate synthase
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-
-
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guanosine 3',5'-polyphosphate synthetase
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-
-
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guanosine 5',3'-polyphosphate synthetase
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-
-
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guanosine pentaphosphate synthetase
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-
-
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RelMtb protein
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stringent factor
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diphosphate transfer
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:GTP 3'-diphosphotransferase
GDP can also act as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
63690-89-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
show the reaction diagram
-
-
-
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
show the reaction diagram
-
-
-
?
guanosine 3'-diphosphate 5'-diphosphate + H2O
GDP + diphosphate
show the reaction diagram
-
-
-
?
guanosine 3'-diphosphate 5'-triphosphate + H2O
GTP + diphosphate
show the reaction diagram
-
-
-
?
ATP + GTP
AMP + guanosine 5'-triphosphate 3'-diphosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + GDP
AMP + guanosine 3'-diphosphate 5'-diphosphate
show the reaction diagram
-
-
-
?
ATP + GTP
AMP + guanosine 3'-diphosphate 5'-triphosphate
show the reaction diagram
-
-
-
?
guanosine 3'-diphosphate 5'-diphosphate + H2O
GDP + diphosphate
show the reaction diagram
-
-
-
?
guanosine 3'-diphosphate 5'-triphosphate + H2O
GTP + diphosphate
show the reaction diagram
-
-
-
?
ATP + GTP
AMP + guanosine 5'-triphosphate 3'-diphosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
the optimal concentration for pppGpp synthesis is approximately equal to the total concentration of nucleotide substrates([ATP] + [GTP])
Mn2+
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the optimal concentration for pppGpp synthesis is approximately one-half of the total concentration of nucleotide substrates([ATP] + [GTP])
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.33 - 1.36
GTP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 8.4
GTP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00021
-
mol of PPi/s/mol of enzyme, fragment 1-181
0.027
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mol of PPi/s/mol of enzyme, fragment 1-394 monomer
0.028
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mol of PPi/s/mol of enzyme, full length enzyme
0.03
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mol of PPi/s/mol of enzyme, fragment 1-203
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene relA
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
Mycobacterium tuberculosis strains expressing the synthetase-dead RelMtb H344Y mutant do not persist in mice. Deletion of a second predicted (p)ppGpp synthetase has no effect on pathogenesis, demonstrating. Expression of an allele encoding the hydrolase-dead RelMtb mutant, RelMtb H80A, decreases the growth rate of Mycobacterium tuberculosis and changes the colony morphology of the bacteria. RelMtb H80A expression during acute or chronic Mycobacterium tuberculosis infection in mice is lethal to the infecting bacteria. Phenotypes, overview
physiological function
in Mycobacterium tuberculosis, the stringent response to amino acid starvation is mediated by the enzyme Rel (RelMtb), which 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. (p)ppGpp then influences numerous metabolic processes. RelMtb also encodes a second, distinct catalytic domain that hydrolyzes (p)ppGpp into diphosphate and GDP or GTP. RelMtb is required for chronic Mycobacterium tuberculosis infection in C57BL/6 mice. The RelMtb (p)ppGpp synthetase activity is required for maintaining bacterial titers during chronic infection, RelMtb is the major contributor to (p)ppGpp production during infection, RelMtb (p)ppGpp hydrolase activity is essential for acute and chronic infection of mice
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
240000
-
full-length enzyme, gel filtration
245000
-
full-length enzyme, calculated from amino acid sequence
82000
-
full-length enzyme, calculated from OD280
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
-
3 * 82000, gel filtration, calculated from OD280
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H344Y
site-directed mutagenesis, the mutant enzyme shows no synthase activity
H80A
site-directed mutagenesis, the mutant enzyme shows no hydrolase activity
C633A
-
20fold decrease in activity
D632A
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3.5fold decrease in activity
D81A
-
loss of hydrolytic activity with retention of synthesis
G241E
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loss of synthetic activity and retention of hydrolysis
H344Y
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loss of synthetic activity and retention of hydrolysis
H80A
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loss of hydrolytic activity with retention of synthesis
additional information
-
fragments 1-203 (22.7 kDa) and 1-181 (20.1 kDa) possess hydrolytic activity but are incapable of synthesis activity, fragment 1-156 (17.3 kDa) is not capable of either synthesis or hydolytic activity, relative acticity of fragment 1-181 decreases approximately 130fold compared to that of the wild type, fragment 87-394 (35.1 kDa) has only synthesis activity, fragment 1-394 (44.6 kDa) and 1-450 are capable of synthesis and hydrolysis, the trimer state of fragment 1-394 appears to be a catalytically less efficient state than the monomer state, fragment 395-738 is devoid of any activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and Mycobacterium smegmatis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Weiss, L.A.; Stallings, C.L.
Essential roles for Mycobacterium tuberculosis Rel beyond the production of (p)ppGpp
J. Bacteriol.
195
5629-5638
2013
Mycobacterium tuberculosis (P9WHG9), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WHG9)
Manually annotated by BRENDA team