HOME
login
history
all enzymes
BRENDA home
History
Information on EC 2.7.4.1 - polyphosphate kinase
for references in articles please use BRENDA:EC2.7.4.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.4.1 polyphosphate kinaseSpecify your search results
Word Map
- 2.7.4.1
- phosphorus
- exopolyphosphatase
- molecular biology
-
wastewater
- sludge
- polyhydroxyalkanoates
- polyphosphatase
- accumulibacter
-
phosphoanhydride
- medicine
-
candidatus
- phosphatis
- synthesis
- drug development
- analysis
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
ATP:polyphosphate phosphotransferase, class II polyphosphate kinase, family-2 polyphosphate kinase, glycogen-bound polyphosphate kinase, kinase, polyphosphate (phosphorylating), More, PA3455 protein, paPpx, plyphosphate kinase 1, poly P kinase 1, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP:polyphosphate phosphotransferase
family-2 polyphosphate kinase
kinase, polyphosphate (phosphorylating)
poly P kinase 1
poly(P) kinase 1
A0MH70, A7XVX1, A7XVX6, A7XVX7, A7XVY1, A7XVY3, A7XVY6, A7XVY9, A7XVZ2, A7XVZ5, A7XVZ7, A7XVZ9, A7XW05, A7XW08, A7XW11, A7XW13, A7XW15, A7XW17, A7XW18, A7XW22, A7XW24, A7XW27, A7XW29, A7XW30, A7XW33, A7XW35, A7XW38, A7XW41, A7XW42, A7XW45, A7XW47, A7XW48, A7XW52, A7XW54, A7XW56, A7XW57, A7XW59
-
poly(P) kinase 2
A0MH70, A7XVX1, A7XVX6, A7XVX7, A7XVY1, A7XVY3, A7XVY6, A7XVY9, A7XVZ2, A7XVZ5, A7XVZ7, A7XVZ9, A7XW05, A7XW08, A7XW11, A7XW13, A7XW15, A7XW17, A7XW18, A7XW22, A7XW24, A7XW27, A7XW29, A7XW30, A7XW33, A7XW35, A7XW38, A7XW41, A7XW42, A7XW45, A7XW47, A7XW48, A7XW52, A7XW54, A7XW56, A7XW57, A7XW59
-
poly-P kinase 1
polyP kinase
polyphosphate kinase
polyphosphate kinase 1
polyphosphate kinase 2
polyphosphate-dependent nucleoside diphosphate kinase
polyphosphoric acid kinase
-
-
-
-
PPK
PPK1
PPK2
PPK2-1
PPK2-2
PPK2-3
PPK2a
PPK2B
PPK2c
PPK2d
PPK2e
SPO0224
SPO1256
SPO1727
kinase, polyphosphate (phosphorylating)
-
-
-
-
polyphosphate kinase 1
A0MH70, A7XVX1, A7XVX6, A7XVX7, A7XVY1, A7XVY3, A7XVY6, A7XVY9, A7XVZ2, A7XVZ5, A7XVZ7, A7XVZ9, A7XW05, A7XW08, A7XW11, A7XW13, A7XW15, A7XW17, A7XW18, A7XW22, A7XW24, A7XW27, A7XW29, A7XW30, A7XW33, A7XW35, A7XW38, A7XW41, A7XW42, A7XW45, A7XW47, A7XW48, A7XW52, A7XW54, A7XW56, A7XW57, A7XW59
-
PPK1
A0MH70, A7XVX1, A7XVX6, A7XVX7, A7XVY1, A7XVY3, A7XVY6, A7XVY9, A7XVZ2, A7XVZ5, A7XVZ7, A7XVZ9, A7XW05, A7XW08, A7XW11, A7XW13, A7XW15, A7XW17, A7XW18, A7XW22, A7XW24, A7XW27, A7XW29, A7XW30, A7XW33, A7XW35, A7XW38, A7XW41, A7XW42, A7XW45, A7XW47, A7XW48, A7XW52, A7XW54, A7XW56, A7XW57, A7XW59
-
PPK2
A0MH70, A7XVX1, A7XVX6, A7XVX7, A7XVY1, A7XVY3, A7XVY6, A7XVY9, A7XVZ2, A7XVZ5, A7XVZ7, A7XVZ9, A7XW05, A7XW08, A7XW11, A7XW13, A7XW15, A7XW17, A7XW18, A7XW22, A7XW24, A7XW27, A7XW29, A7XW30, A7XW33, A7XW35, A7XW38, A7XW41, A7XW42, A7XW45, A7XW47, A7XW48, A7XW52, A7XW54, A7XW56, A7XW57, A7XW59
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + (phosphate)n = ADP + (phosphate)n+1
-
-
-
-
ATP + (phosphate)n = ADP + (phosphate)n+1
mechanism
-
ATP + (phosphate)n = ADP + (phosphate)n+1
short chain polyphosphates are incorporated at the ends of the long chain product
-
ATP + (phosphate)n = ADP + (phosphate)n+1
both polyphosphate synthesis and polyphosphate utilization follow a processive mechanism
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ATP:polyphosphate phosphotransferase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9026-44-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (phosphate)n+1
ADP + (phosphate)n
-
-
-
r
ATP + ATP
ADP + (phosphate)n+1
-
polyP not required as primer
-
-
r
GDP + (phosphate)20
GTP + (phosphate)19
-
isoform PPK1 affinity for the ADP as a substrate is about 70fold high as opposed to GDP
-
-
r
GTP + (phosphate)n+1
GDP + (phosphate)n
-
-
-
r
ADP + (phosphate)45
ATP + (phosphate)44
-
similar catalytic activities with either (phosphate)65 or (phosphate)45. Isoform PPK2 catalyzes polyphosphate-dependent phosphorylation of ADP to ATP at a rate 838times higher than the rate of polyphosphate synthesis
-
-
r
ADP + (phosphate)45
ATP + (phosphate)44
-
similar catalytic activities with either (phosphate)65 or (phosphate)45. Isoform PPK2 catalyzes polyphosphate-dependent phosphorylation of ADP to ATP at a rate 838times higher than the rate of polyphosphate synthesis
-
-
r
ADP + (phosphate)65
ATP + (phosphate)64
-
similar catalytic activities with either (phosphate)65 or (phosphate)45. Isoform PPK2 catalyzes polyphosphate-dependent phosphorylation of ADP to ATP at a rate 838times higher than the rate of polyphosphate synthesis
-
-
r
ADP + (phosphate)65
ATP + (phosphate)64
-
similar catalytic activities with either (phosphate)65 or (phosphate)45. Isoform PPK2 catalyzes polyphosphate-dependent phosphorylation of ADP to ATP at a rate 838times higher than the rate of polyphosphate synthesis
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
?
ADP + (phosphate)n
ATP + (phosphate)n-1
not (phosphate)3, (phosphate)4 as preferred phosphate donor
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
polyphosphate kinase directly or indirectly regulates DNA polymerase activity or fidelity
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
substrates are polyphosphates or hexametaphosphate
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
no activity with GDP, diphosphate or tripolyphosphate
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
enzyme is involved in polyphosphate synthesis. The polyphosphate kinase gene is transcribed from a sigma(E) dependent promoter, which could be responsive to environmental stresses
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
GDP is preferred over ADP over nucleoside diphosphate acceptors
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
enzyme is involved in polyphosphate synthesis. The polyphosphate kinase gene is transcribed from a sigma(E) dependent promoter, which could be responsive to environmental stresses
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
GDP is preferred over ADP over nucleoside diphosphate acceptors
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
no activity with AMP
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
the enzyme protects Salmonella enterica from weak organic acid stress. Polyphosphate may acts as a chemical chaperone that helps refold homoserine transsuccinylase and/or may stimulate proteolysis of toxic denatured protein. The instability of homoserine transsuccinylase may provide a metabolic fuse that blocks growth under conditions that denature proteins. The sensitivity of this fuse is modulated by polyphosphate
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
no activity with CTP, GTP and TTP
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate utilization and accumulation contribute significantly to Campylobacter jejuni pathogenesis and affect its ability to adapt to specific stresses and stringencies
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate utilization and accumulation contribute significantly to Campylobacter jejuni pathogenesis and affect its ability to adapt to specific stresses and stringencies
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
ir
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK2B forms polyphopshate with an average chain length of about 125
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK2B forms polyphopshate with an average chain length of about 125 and prefers the polyphosphate synthesis reaction direction
polyphosphate product chain length determination by NMR spectroscopy
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK2B forms polyphopshate with an average chain length of about 125
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK2B forms polyphopshate with an average chain length of about 125 and prefers the polyphosphate synthesis reaction direction
polyphosphate product chain length determination by NMR spectroscopy
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
DdPPK1 products are heterogeneous in chain length, with broad-range chain lengths of 50-300 Pi residues, and shorter compared to those of Escherichia coli
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
PPK1 is the principal enzyme responsible for reversible synthesis of polyphosphate from the terminal phosphate of ATP
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
polyphosphate chains of lenths of 700-800 residues
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
autophosphorylation, i.e. the gamma-phosphate of ATP becomes covalently attached to the enzyme under condition of polyphosphate synthesis, 0.52-0.92 mol phosphate per mol enzyme
via phosphorylated enzyme intermediate
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
best substrates are polyphosphates with more than 132 residues
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
no activity with phosphates of 5 residues or below
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
no primer substrate required
via phosphorylated enzyme intermediate
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
incorporates gamma-phosphate of ATP into long-chain polyphosphate molecules
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
polyphosphate kinase may be involved in nucleotide metabolism
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
involved in phosphate metabolism of bacteria
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
Escherichia coli B / ATCC 11303
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
essential role of the enzyme during the initial steps of colonisation of the mouse gastric mucosa. The enzyme may act on the virulence of Helicobacter pylori partly through an energy dependent mechanism
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
autophosphorylation, i.e. the gamma-phosphate of ATP becomes covalently attached to the enzyme under condition of polyphosphate synthesis, 0.52-0.92 mol phosphate per mol enzyme
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
autophosphorylation, i.e. the gamma-phosphate of ATP becomes covalently attached to the enzyme under condition of polyphosphate synthesis, 0.52-0.92 mol phosphate per mol enzyme
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
autophosphorylation, i.e. the gamma-phosphate of ATP becomes covalently attached to the enzyme under condition of polyphosphate synthesis, 0.52-0.92 mol phosphate per mol enzyme
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
strictly processive mechanism of polyphosphate elongation, phosphate or short-chains of polyphosphates serve as primers, majority of the synthesized polyphosphates is 750 residues long
polyphosphate as primer: product with 750 residues, phosphate as primer: product with 300-2000 residues, i.e. major form with chain length of 2000
?
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate kinase 1 and 2
polyphosphate with 200-800 residues
?
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate kinase 1 and 2
poyphosphate with 500-800 residues
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
essential for biofilm development, quorum sensing, and virulence of Pseudomonas aeruginosa
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK1 is essential for a successful ocular infection by the organism
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
very slow reverse reaction
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
no activity with AMP
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
enzyme synthesizes polyphosphates of 300000-400000 Da
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
incorporates gamma-phosphate of ATP into long-chain polyphosphate molecules
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
glycogen-bound polyphosphate kinase
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
the enzyme does not require the presence of histones for its activity
-
-
?
CDP + (phosphate)n
CTP + (phosphate)n-1
-
-
-
?
CDP + (phosphate)n+1
CTP + (phosphate)n
-
the efficiency of polyphosphate utilization by PKK3 is 100%
-
-
?
GDP + (phosphate)n
GTP + (phosphate)n-1
-
-
-
r
GDP + (phosphate)n
GTP + (phosphate)n-1
-
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
efficiency of NDP substrates in descending order: ADP, dADP, dGDP, GDP, TDP, UDP, CDP, dCDP
-
ir
GDP + (phosphate)n+1
GTP + (phosphate)n
-
PPK2 catalyses the synthesis of GTP from GDP using polyphosphate rather than ATP as phosphate donor, PPK2 preferentially synthesizes GTP over CTP or UTP in vitro
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
PPK2 catalyses the synthesis of GTP from GDP using polyphosphate rather than ATP as phosphate donor, PPK2 preferentially synthesizes GTP over CTP or UTP in vitro
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
PPK2 catalyses the synthesis of GTP from GDP using polyphosphate rather than ATP as phosphate donor, PPK2 preferentially synthesizes GTP over CTP or UTP in vitro
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
PPK2 catalyses the synthesis of GTP from GDP using polyphosphate rather than ATP as phosphate donor, PPK2 preferentially synthesizes GTP over CTP or UTP in vitro
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
10times higher activity than Escherichia coli polyphosphate kinase
-
ir
GDP + (phosphate)n+1
GTP + (phosphate)n
-
chains of 30-50 residues are optimal, chains of 15-700 residues can also serve. GDP is preferred over ADP over nucleoside diphosphate acceptors
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
chains of 30-50 residues are optimal, chains of 15-700 residues can also serve. GDP is preferred over ADP over nucleoside diphosphate acceptors
-
-
?
GDP + (phosphate)n+2
guanosine 5'-tetraphosphate + (phosphate)n
-
-
-
?
GDP + (phosphate)n+2
guanosine 5'-tetraphosphate + (phosphate)n
-
diphosphate group transfer
-
ir
GTP + (phosphate)n
GDP + (phosphate)n+1
-
lower activity compared to ATP
-
-
r
GTP + (phosphate)n
GDP + (phosphate)n+1
polyphosphate kinase 2
-
?
ITP + (phosphate)n
IDP + (phosphate)n+1
-
lower activity compared to ATP
-
-
r
UDP + (phosphate)n
UTP + (phosphate)n-1
-
-
-
?
additional information
?
-
-
accumulation of high levels of cytosolic phosphorus in the form of polyphosphate involving classII polyphosphate kinase isozymes, granular poly P, i.e. volutin, can make up to 37% of the internal cell volume, overview
-
-
?
additional information
?
-
-
PKK2B also shows NDP kinase activity
-
-
?
additional information
?
-
-
accumulation of high levels of cytosolic phosphorus in the form of polyphosphate involving classII polyphosphate kinase isozymes, granular poly P, i.e. volutin, can make up to 37% of the internal cell volume, overview
-
-
?
additional information
?
-
-
PKK2B also shows NDP kinase activity
-
-
?
additional information
?
-
the organism also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
-
-
?
additional information
?
-
-
the organism also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
-
-
?
additional information
?
-
the enzyme from Dictyostelium discoideum performs autophosphorylation and has an unique N-terminal extension of 370 amino acids, lacking homology with any known protein, that is necessary for its enzymatic activity, cellular localization, and physiological functions, overview
-
-
?
additional information
?
-
-
the enzyme from Dictyostelium discoideum performs autophosphorylation and has an unique N-terminal extension of 370 amino acids, lacking homology with any known protein, that is necessary for its enzymatic activity, cellular localization, and physiological functions, overview
-
-
?
additional information
?
-
the substrate specificity of FtPPK2 includes purine but not pyrimidine nucleotides. No activity with UDP and CDP as substrates. No formation of ADP or GDP from AMP or GMP
-
-
?
additional information
?
-
-
maximum PPK activity is observed for wild-type AG83 Leishmania donovani amastigotes when ADP is the phosphate group acceptor from polyphosphate, the activity is 29 times higher than with GDP as phosphate group acceptor from polyphosphate. When AMP is the phosphate group acceptor from polyphosphate, the activity of PPK is 97times less than with ADP, existence of both PPK1 and PPK2 activity is probable in Leishmania donovani amastigotes. ATP formation from AMP shows lowest activity
-
-
?
additional information
?
-
-
maximum PPK activity is observed for wild-type AG83 Leishmania donovani amastigotes when ADP is the phosphate group acceptor from polyphosphate, the activity is 29 times higher than with GDP as phosphate group acceptor from polyphosphate. When AMP is the phosphate group acceptor from polyphosphate, the activity of PPK is 97times less than with ADP, existence of both PPK1 and PPK2 activity is probable in Leishmania donovani amastigotes. ATP formation from AMP shows lowest activity
-
-
?
additional information
?
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
-
the enzyme is unable to use triphosphate or pentaphosphate as phosphate donors
-
-
?
additional information
?
-
-
the enzyme is unable to use triphosphate or pentaphosphate as phosphate donors
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, mprAB-sigE-rel signalling cascade, overview. PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium smegmatis, overview
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, mprAB-sigE-rel signalling cascade, overview. PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium smegmatis, overview
-
-
?
additional information
?
-
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, mprAB-sigE-rel signalling cascade, overview. PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium smegmatis, overview
-
-
?
additional information
?
-
-
PA3455 protein is also active with (phosphate)3 as a phosphodonor, but its activity and substrate affinity are lower than those with (phosphate)12-13
-
-
?
additional information
?
-
-
paPpx is an exopolyphosphatase (EC 3.6.1.11), and is also a polyphosphate:ADP phosphotransferase, and the active site is the same as that one involved in the hydrolase activity
-
-
-
additional information
?
-
gene ppk regulates the transcription accumulation of the stationary-phase sigma factor RpoS encoded by the rpoS gene, overview
-
-
?
additional information
?
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
-
the enzyme PPK from Streptomyces lividans also exhibits weak phospholipase D activity, EC 3.1.4.4, hydrolysing phosphatidylcholine, quantification of [3H]phosphatidic acid released from [3H]PC-labeled ELT3 cell membranes from phospholipase D-deficient cells, overview
-
-
?
additional information
?
-
-
production of choline from hydrolysis of 1,2-dioleoyl-sn-glycero-3-phosphocholine in the presence of the Amplex Red reagent by enzyme PPK
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
polyphosphate kinase directly or indirectly regulates DNA polymerase activity or fidelity
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
enzyme is involved in polyphosphate synthesis. The polyphosphate kinase gene is transcribed from a sigma(E) dependent promoter, which could be responsive to environmental stresses
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
enzyme is involved in polyphosphate synthesis. The polyphosphate kinase gene is transcribed from a sigma(E) dependent promoter, which could be responsive to environmental stresses
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
the enzyme protects Salmonella enterica from weak organic acid stress. Polyphosphate may acts as a chemical chaperone that helps refold homoserine transsuccinylase and/or may stimulate proteolysis of toxic denatured protein. The instability of homoserine transsuccinylase may provide a metabolic fuse that blocks growth under conditions that denature proteins. The sensitivity of this fuse is modulated by polyphosphate
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate utilization and accumulation contribute significantly to Campylobacter jejuni pathogenesis and affect its ability to adapt to specific stresses and stringencies
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate utilization and accumulation contribute significantly to Campylobacter jejuni pathogenesis and affect its ability to adapt to specific stresses and stringencies
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK2B forms polyphopshate with an average chain length of about 125
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK2B forms polyphopshate with an average chain length of about 125
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
PPK1 is the principal enzyme responsible for reversible synthesis of polyphosphate from the terminal phosphate of ATP
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
polyphosphate kinase may be involved in nucleotide metabolism
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
involved in phosphate metabolism of bacteria
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
essential role of the enzyme during the initial steps of colonisation of the mouse gastric mucosa. The enzyme may act on the virulence of Helicobacter pylori partly through an energy dependent mechanism
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK1 is essential for a successful ocular infection by the organism
-
-
?
CDP + (phosphate)n
CTP + (phosphate)n-1
-
-
-
?
GDP + (phosphate)n
GTP + (phosphate)n-1
-
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
efficiency of NDP substrates in descending order: ADP, dADP, dGDP, GDP, TDP, UDP, CDP, dCDP
-
ir
GDP + (phosphate)n+1
GTP + (phosphate)n
-
10times higher activity than Escherichia coli polyphosphate kinase
-
ir
UDP + (phosphate)n
UTP + (phosphate)n-1
-
-
-
?
additional information
?
-
-
accumulation of high levels of cytosolic phosphorus in the form of polyphosphate involving classII polyphosphate kinase isozymes, granular poly P, i.e. volutin, can make up to 37% of the internal cell volume, overview
-
-
?
additional information
?
-
-
accumulation of high levels of cytosolic phosphorus in the form of polyphosphate involving classII polyphosphate kinase isozymes, granular poly P, i.e. volutin, can make up to 37% of the internal cell volume, overview
-
-
?
additional information
?
-
the organism also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
-
-
?
additional information
?
-
-
the organism also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
-
-
?
additional information
?
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, mprAB-sigE-rel signalling cascade, overview. PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium smegmatis, overview
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, mprAB-sigE-rel signalling cascade, overview. PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium smegmatis, overview
-
-
?
additional information
?
-
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, mprAB-sigE-rel signalling cascade, overview. PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium smegmatis, overview
-
-
?
additional information
?
-
gene ppk regulates the transcription accumulation of the stationary-phase sigma factor RpoS encoded by the rpoS gene, overview
-
-
?
additional information
?
-
-
the enzyme PPK from Streptomyces lividans also exhibits weak phospholipase D activity, EC 3.1.4.4, hydrolysing phosphatidylcholine, quantification of [3H]phosphatidic acid released from [3H]PC-labeled ELT3 cell membranes from phospholipase D-deficient cells, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
-
1.5-2.5fold lower activation than with Mg2+, inhibitory with Mg2+ as activator
K+
KCl
Mg2+
Mn2+
NH4+
-
activates wild-type, full-length enzyme paPpx(1-506). The activity curve obtained with NH4+ is sigmoid and reaches its maximum activity at concentrations of 30 mM. Km(app)NH4+ is 10 mM
Zn2+
additional information
K+
-
a nonessential activator of paPpx, presence of K+ does not affect the affinity of the enzyme for Mg2+, activates wild-type, full-length enzyme paPpx(1-506). The activity curve obtained with K+ is sigmoid and reaches its maximum activity at concentrations of 80 mM. Km(app)K+ is 42 mM
KCl
Dictyostelium discoideum also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
Mg2+
-
maximal activity of polyphosphate synthesis, ATP and GTP synthesis, and guanosine 5'-tetraphosphate synthesis at 5.0, 2.0, 1.0 and 0.2 mM
Mg2+
polyphosphate kinase 2, preferred in ATP synthesis over Mn2+
Mg2+
-
5fold higher activation than Mn2+, at optimal concentration of 10 mM
Mg2+
-
no activity in the absence of a divalent metal cation, Mg2+ is the most effective metal, whereas low activity is observed with Co2+ or Ni2+ and no activity is observed in the presence of Mn2+ or Ca2+
Mg2+
-
required, values of Km(app)Mg2+ in paPpx(1-506) and NpaPpx(1-314) are 0.30 mM and 0.28 mM, respectively. The interaction between paPpx(1-506) and Mg2+ occurs in the N-terminal domain
Mg2+
no activity in the absence of a divalent metal cation, Mg2+ is the most effective metal, whereas low activity is observed with Co2+ or Ni2+ and no activity is observed in the presence of Mn2+ or Ca2+
Mn2+
polyphosphate kinase 2, 10 mM preferred in polyphosphate synthesis over Mg2+
Mn2+
-
Mg2+ shows 5fold higher activation than Mn2+, at optimal concentration of 10 mM
additional information
lower optimal concentration for Mn2+ ions than Mg2+ ions
additional information
-
Fe2+, Zn2+, Cu2+ cannot be used by the enzyme
additional information
-
behavior of the full-length paPpx(1-506) and N-paPpx(1-314) against different concentration of divalent ions such as Mg2+, Zn2+, Ca2+, and Mn2+ as effectors, in presence of a saturating concentration (0.008 mM) for the substrate polyphosphate65. The activation of both enzyme variants by Mg2+ is similar and shows no inhibition at high concentrations of this ion. The activation by Ca2+ and Mn2+ is negligible. Li+ and Na+ have no effects on enzyme activity, while NH4+, K+, Rb+, and Cs+ are activators of paPpx(1-506). Tetramethylammonium is not an activator of paPpx(1-506)
additional information
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
not activated by NH4Cl
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ellagic acid
Q9S646
ellagic acid derivatives from Terminalia chebula increase the susceptibility of Pseudomonas aeruginosa to stress by inhibiting polyphosphate kinase, oveview. Ellagic acid derivatives completely inhibit PPK1 activity at 0.5 mg/ml. Ellagic acid derivatives-treated Pseudomonas aeruginosa cells show marked reduction in polyphosphate granules in cytosol. Ellagic acid derivatives from Terminalia chebula inhibit PPK1 expression and its activity and increase the sensitivity of Pseudomonas aeruginosa to desiccation and oxidative stress while reducing tolerance to piperacillin
histone
-
reverse reaction, strong, activates forward reaction in the presence of phosphate
NH4Cl
-
200 mM, approx. 50% inhibition of glycogen-bound polyphosphate kinase
phalloidin
a heptapeptide toxin from the mushroom Amanita phalloides, which binds tightly and specifically to polymerized actin, inhibits DdPPK2 and DdPPK1, the latter by 80% at 10 nM, the molar ratio of phalloidin to DdPPK1 of 10:15 results in complete inhibition of DdPPK1 activity
(NH4)2SO4
-
activation up to 100 mM; inhibition at higher concentrations; strong inhibition
ADP
-
0.025 mM, 0.05 mM, 0.1 mM and 0.25 mM, 56%, 68%, 77% and 100% inhibition, respectively of polyphosphate synthesis in crude extracts
ADP
-
50%, 70% and 93% inhibition at 0.08 mM, 0.15 mM and 0.2 mM ADP, respectively
ADP
-
0.25 mM, approx. 50% inhibition, 1 mM, complete inhibition
ADP
-
2 mM, 50% inhibition of glycogen-bound polyphosphate kinase; product inhibition, about 50% inhibition at 2 mM
AMP
-
15% and 70% inhibition of the forward reaction at AMP/ADP ratios of 1 and 10, respectiverly
Co2+
complete inhibition; complete inhibition; complete inhibition
diphosphate
-
10 mM, 66% inhibition of polyphosphate synthesis, 75% inhibition of GTP synthesis
GMP
-
competitive inhibition of polyphosphate 750 and GDP in guanosine 5'-tetraphosphate synthesis
phosphate
-
5.5 mM and 11 mM, 33% and 49% inhibition of forward reaction
phosphate
-
2 mM, 50% inhibition of glycogen-bound polyphosphate kinase; strong inhbition
Polyphosphate
-
65 residues, competitive inhibition of polyphosphate 750 and GDP in guanosine 5'-tetraphosphate synthesis
additional information
-
not inhibited by 2,4-dinitrophenol or potassium arsenate
-
additional information
MIC values of wild-type and mutant strain ExPEC for diverse antibiotics, i.e. beta-lactams cefotaxime, ceftazidime, ampicillin, cefazolin, tazobactam, and ticarcillin, glycopeptide vancomycin, aminoglycosides gentamicin, gentamicin sulfate, amikacin macrolide, erythromycin, quinolones norfloxacin and levofloxacin, sulfonamide trimethoprim, sulfadiazine nitrofurans macrodantin, and lipopeptde polymyxin B, overview. Biofilm-grown DELTAppk and wild-type cells are similarly tolerant and more tolerant than planktonic cells
-
additional information
-
MIC values of wild-type and mutant strain ExPEC for diverse antibiotics, i.e. beta-lactams cefotaxime, ceftazidime, ampicillin, cefazolin, tazobactam, and ticarcillin, glycopeptide vancomycin, aminoglycosides gentamicin, gentamicin sulfate, amikacin macrolide, erythromycin, quinolones norfloxacin and levofloxacin, sulfonamide trimethoprim, sulfadiazine nitrofurans macrodantin, and lipopeptde polymyxin B, overview. Biofilm-grown DELTAppk and wild-type cells are similarly tolerant and more tolerant than planktonic cells
-
additional information
-
not inhibited by KCl; not inhibited by NaCl; not inhibited by phosphate; not inhibited by polyphosphate
-
additional information
-
a G9-quadruplex DNA aptamer inhibits isoform PPK2 with an IC50 of 40 nM and exhibits noncompetitive inhibition kinetics
-
additional information
-
a G9-quadruplex DNA aptamer inhibits isoform PPK2 with an IC50 of 105 nM and exhibits noncompetitive inhibition kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
actin
Dictyostelium discoideum also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
diphosphate
-
10 mM, 100% activation of guanosine 5'-tetraphosphate synthesis
Guanidine HCl
-
5 mM, 20% activation of guanosine 5'-tetraphosphate synthesis
Tetrapolyphosphate
-
activation, removes lag-phase in synthesis at low ATP-levels, not phosphate, diphosphate or tripolyphosphate
bovine serum albumin
-
activation, can substitute for histone only in the absence of phosphate
-
bovine serum albumin
-
activation, can substitute for histone only in the absence of phosphate
-
casein
-
activation, can substitute for histone only in the absence of phosphate
casein
-
activation, can substitute for histone only in the absence of phosphate
phosphate
-
10fold higher rate of polyphosphate synthesis
additional information
polyphosphate or ATP promote oligomerization of the enzyme in vitro, polyphosphate activates about 10fold
-
additional information
-
polyphosphate or ATP promote oligomerization of the enzyme in vitro, polyphosphate activates about 10fold
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Foot-and-Mouth Disease
Active protein aggregates induced by terminally attached self-assembling peptide ELK16 in Escherichia coli.
Infections
Ellagic acid derivatives from Terminalia chebula Retz. increase the susceptibility of Pseudomonas aeruginosa to stress by inhibiting polyphosphate kinase.
Infections
Inactivation of ppk differentially affects virulence and disrupts ATP homeostasis in Salmonella enterica serovars Typhimurium and Gallinarum.
Infections
Trypanosoma brucei vacuolar transporter chaperone 4 (TbVtc4) is an acidocalcisome polyphosphate kinase required for in vivo infection.
Starvation
Inorganic polyphosphate kinase is required to stimulate protein degradation and for adaptation to amino acid starvation in Escherichia coli.
Starvation
Transcription of ppk from Acinetobacter sp. strain ADP1, encoding a putative polyphosphate kinase, is induced by phosphate starvation.
Tuberculosis
Amino acids involved in polyphosphate synthesis and its mobilization are distinct in polyphosphate kinase-1 from Mycobacterium tuberculosis.
Tuberculosis
Aptamer-Mediated Inhibition of Mycobacterium tuberculosis Polyphosphate Kinase 2.
Tuberculosis
Author Correction: Establishing Virulence Associated Polyphosphate Kinase 2 as a drug target for Mycobacterium tuberculosis.
Tuberculosis
Establishing Virulence Associated Polyphosphate Kinase 2 as a drug target for Mycobacterium tuberculosis.
Tuberculosis
Polyphosphate kinase 1, a central node in the stress response network of Mycobacterium tuberculosis, connects the two-component systems MprAB and SenX3-RegX3 and the extracytoplasmic function sigma factor, sigma E.
Tuberculosis
Polyphosphate kinase from M. tuberculosis: an interconnect between the genetic and biochemical role.
Tuberculosis
The polyphosphate kinase gene ppk2 is required for mycobacterium tuberculosis inorganic polyphosphate regulation and virulence.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
(phosphate)45
-
polyphosphate synthesis reaction, in 50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
-
0.006
(phosphate)45
-
polyphosphate utilization reaction, in 50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
-
0.0054
(phosphate)65
-
polyphosphate synthesis reaction, in 50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
-
0.0063
(phosphate)65
-
polyphosphate utilization reaction, in 50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
-
0.1
ADP
-
in 50 mM Tris-HCl pH-7.5, 10 mM NH4SO4,10 mM KPO4, pH 7.0, 4 mM MgCl2, 50 mM NaCl, at 37°C
0.16
ADP
-
isoform PPK1, pH and temperature not specified in the publication
0.176
ADP
-
mutant H510Q of isoform PPK1, pH and temperature not specified in the publication
0.18
ADP
-
mutant H480Q of isoform PPK1, pH and temperature not specified in the publication
0.2
ADP
-
mutant H480A of isoform PPK1, pH and temperature not specified in the publication
2
ADP
-
mutant Y524A of isoform PPK1, pH and temperature not specified in the publication
6.8
ADP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
8
ADP
-
isoform PPK2, pH and temperature not specified in the publication
0.8
ATP
-
in 50 mM Tris-HCl pH-7.5, 10 mM NH4SO4,10 mM KPO4, pH 7.0, 4 mM MgCl2, 50 mM NaCl, at 37°C
0.83
ATP
-
pH 7.0, 20°C, polyphosphate kinase activity in cell extracts, detrmined with Robinson and Wood method
1.18
ATP
-
pH 7.0, 20°C, polyphosphate kinase activity in cell extracts, kinetic analysis
1.35
ATP
-
isoform PPK1, pH and temperature not specified in the publication
1.38
ATP
-
mutant H480Q of isoform PPK1, pH and temperature not specified in the publication
1.47
ATP
-
mutant H480A of isoform PPK1, pH and temperature not specified in the publication
1.5 - 2
ATP
-
mutant H510Q of isoform PPK1, pH and temperature not specified in the publication
5.2
ATP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
13
ATP
-
mutant Y524A of isoform PPK1, pH and temperature not specified in the publication
11.3
GDP
-
isoform PPK1, pH and temperature not specified in the publication
additional information
additional information
-
exponential kinetics
-
additional information
additional information
Michalis-Menten steady state kinetic analysis of FtPPK2 substrate specificity, overview
-
additional information
additional information
-
kinetic analysis of recombinant wild-type and truncated mutant enzymes, polyphosphatase activity (EC 3.6.1.11) and polyphosphate:ADP phosphotransferase activity, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
(phosphate)45
-
polyphosphate synthesis reaction, in 50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
-
50
(phosphate)45
-
polyphosphate utilization reaction, in 50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
-
0.02
(phosphate)65
-
polyphosphate synthesis reaction, in 50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
-
53
(phosphate)65
-
polyphosphate utilization reaction, in 50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
-
210
ADP
-
isoform PPK2, pH and temperature not specified in the publication
332
ADP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
622
ADP
-
mutant H510Q of isoform PPK1, pH and temperature not specified in the publication
943
ADP
-
isoform PPK1, pH and temperature not specified in the publication
950
ADP
-
mutant H480A of isoform PPK1, pH and temperature not specified in the publication
971
ADP
-
mutant H480Q of isoform PPK1, pH and temperature not specified in the publication
994
ADP
-
mutant Y524A of isoform PPK1, pH and temperature not specified in the publication
44.6
ATP
-
mutant H510Q of isoform PPK1, pH and temperature not specified in the publication
45
ATP
-
mutant H480Q of isoform PPK1, pH and temperature not specified in the publication
45.6
ATP
-
mutant H480A of isoform PPK1, pH and temperature not specified in the publication
46.9
ATP
-
isoform PPK1, pH and temperature not specified in the publication
55
ATP
-
mutant Y524A of isoform PPK1, pH and temperature not specified in the publication
55.4
ATP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
645
GDP
-
isoform PPK1, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4
(phosphate)45
-
polyphosphate synthesis reaction, in 50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
-
8300
(phosphate)45
-
polyphosphate utilization reaction, in 50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
-
3.704
(phosphate)65
-
polyphosphate synthesis reaction, in 50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
-
8400
(phosphate)65
-
polyphosphate utilization reaction, in 50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
-
25.5
ADP
-
isoform PPK2, pH and temperature not specified in the publication
49
ADP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
998
ADP
-
mutant Y524A of isoform PPK1, pH and temperature not specified in the publication
3529
ADP
-
mutant H510Q of isoform PPK1, pH and temperature not specified in the publication
4690
ADP
-
mutant H480A of isoform PPK1, pH and temperature not specified in the publication
5222
ADP
-
mutant H480Q of isoform PPK1, pH and temperature not specified in the publication
5743
ADP
-
isoform PPK1, pH and temperature not specified in the publication
4.2
ATP
-
mutant Y524A of isoform PPK1, pH and temperature not specified in the publication
10.5
ATP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
29
ATP
-
mutant H510Q of isoform PPK1, pH and temperature not specified in the publication
31
ATP
-
mutant H480A of isoform PPK1, pH and temperature not specified in the publication
32.6
ATP
-
mutant H480Q of isoform PPK1, pH and temperature not specified in the publication
34.7
ATP
-
isoform PPK1, pH and temperature not specified in the publication
57
GDP
-
isoform PPK1, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007
GMP
-
pH 7.5, 37°C, competitive inhibition of GDP in guanosine 5'-tetraphosphate synthesis
0.0014
GMP
-
pH 7.5, 37°C, competitive inhibition of polyphosphate 750 in guanosine 5'-tetraphosphate synthesis
0.0012
polyphosphate 65
-
pH 7.5, 37°C, competitive inhibition of GDP in guanosine 5'-tetraphosphate synthesis
-
0.0076
polyphosphate 65
-
pH 7.5, 37°C, competitive inhibition of polyphosphate 750 in guanosine 5'-tetraphosphate synthesis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.13
-
polyphosphate kinase activity in crude extracts measured with a modified toluidine blue assay
0.15
14
-
purified recombinant wild-type enzyme, polyphosphate synthesis with GTP
15
-
recombinant truncated enzyme, pH 8.0, 37°C, ATP formation, in presence of 80 mM K+
18
-
purified recombinant wild-type enzyme, polyphosphate synthesis with ITP
20
-
recombinant full-length enzyme, pH 8.0, 37°C, ATP formation, in presence of 80 mM K+
26.7
-
recombinant truncated enzyme, pH 8.0, 37°C, ATP formation, in presence of 25 mM NH4+
31
-
purified recombinant wild-type enzyme, polyphosphate synthesis with ATP
3126.7
-
recombinant full-length enzyme, pH 8.0, 37°C, ATP formation, in presence of 5 mM Mg2+ and 80 mM K+
3150
-
recombinant full-length enzyme, pH 8.0, 37°C, ATP formation, in presence of 5 mM Mg2+ and 25 mM NH4+
32
-
purified recombinant wild-type enzyme, polyphosphate dephosphorylation
3223.3
-
recombinant full-length enzyme, pH 8.0, 37°C, ATP formation, in presence of 5 mM Mg2+
35
-
recombinant full-length enzyme, pH 8.0, 37°C, ATP formation, in presence of 25 mM NH4+
645
-
recombinant truncated enzyme, pH 8.0, 37°C, ATP formation, in presence of 5 mM Mg2+ and 80 mM K+
655
-
recombinant truncated enzyme, pH 8.0, 37°C, ATP formation, in presence of 5 mM Mg2+
715
-
recombinant truncated enzyme, pH 8.0, 37°C, ATP formation, in presence of 5 mM Mg2+ and 25 mM NH4+
additional information
additional information
-
relative activity of mutant enzymes compared to the wild-type in both reaction directions, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.4
8 - 9.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8
-
approx. 10% of maximal activity at pH 5.5 and pH 8.0 respectively
5.8 - 7
-
approx. half-maximal activity at pH 5.8, approx. 85% of maximal activity at pH 7.0
6.2 - 8.2
-
approx. 45% of maximal activity at pH 6.2, approx. 75% of maximal activity at pH 8.2
additional information
maximal activity at pH 8.0, sharp drop-off in activity at pH 9
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
70
75