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2'-dAMP + (phosphate)n
2'-dADP + (phosphate)n-1
2'-deoxy-AMP + [phosphate]n
2'-deoxy-ADP + [phosphate]n-1
-
-
-
-
?
ADP + (phosphate)n
AMP + (phosphate)n+1
ADP + (phosphate)n
ATP + (phosphate)n-1
ADP + [phosphate]n
AMP + [phosphate]n+1
AMP + (phosphate)3
ADP + (phosphate)2
AMP + (phosphate)n
ADP + (phosphate)n-1
AMP + (phosphate)n+1
ADP + (phosphate)n
AMP + [phosphate]n
ADP + [phosphate]n-1
CMP + [phosphate]n
CDP + [phosphate]n-1
dAMP + (phosphate)n+1
dADP + (phosphate)n
dAMP + [phosphate]n
dADP + [phosphate]n-1
18% of the activity with AMP
-
-
?
dCMP + [phosphate]n
dCDP + [phosphate]n-1
0.008% of the activity with AMP
-
-
?
dGMP + (phosphate)n+1
dGDP + (phosphate)n
dGMP + [phosphate]n
dGDP + [phosphate]n-1
2.6% of the activity with AMP
-
-
?
GDP + (phosphate)n
GMP + (phosphate)n+1
the enzyme prefers GDP over ADP
-
-
r
GDP + [phosphate]n
GMP + [phosphate]n+1
GMP + (phosphate)n+1
GDP + (phosphate)n
-
-
-
r
GMP + [phosphate]n
GDP + [phosphate]n-1
IMP + (phosphate)n+1
IDP + (phosphate)n
-
-
-
r
IMP + [phosphate]n
IDP + [phosphate]n-1
2.2% of the activity with AMP
-
-
?
TMP + [phosphate]n
TDP + [phosphate]n-1
0.012% of the activity with AMP
-
-
?
UMP + [phosphate]n
UDP + [phosphate]n-1
XMP + (phosphate)n+1
XDP + (phosphate)n
-
-
-
r
additional information
?
-
2'-dAMP + (phosphate)n
2'-dADP + (phosphate)n-1
-
-
-
-
?
2'-dAMP + (phosphate)n
2'-dADP + (phosphate)n-1
-
-
-
-
?
ADP + (phosphate)n
AMP + (phosphate)n+1
-
-
-
r
ADP + (phosphate)n
AMP + (phosphate)n+1
-
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
-
cf. EC 2.7.4.1
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
-
cf. EC 2.7.4.1
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
cf. EC 2.7.4.1
-
-
?, r
ADP + (phosphate)n
ATP + (phosphate)n-1
cf. EC 2.7.4.1
-
-
?, r
ADP + [phosphate]n
AMP + [phosphate]n+1
-
-
-
r
ADP + [phosphate]n
AMP + [phosphate]n+1
-
-
-
r
AMP + (phosphate)3
ADP + (phosphate)2
-
-
-
r
AMP + (phosphate)3
ADP + (phosphate)2
-
-
-
r
AMP + (phosphate)n
ADP + (phosphate)n-1
-
-
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
-
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
-
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
highest activity are found with polyphosphate molecules of 18 to 44 phosphate residues. The polyphosphate chain is degraded completely to ADP. The mechanism of the degradation is processive. No activity is obtained with ortho-, di-, tri-, and tetraphosphate
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
highest activity are found with polyphosphate molecules of 18 to 44 phosphate residues. The polyphosphate chain is degraded completely to ADP. The mechanism of the degradation is processive. No activity is obtained with ortho-, di-, tri-, and tetraphosphate
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
-
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
enzyme is involved in metabolism of polyphosphate
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
polyphosphate kinase and adenylate kinase together constitute the polyP:AMP phosphotransferase activity. Polyphosphate kinase and adenylate kinase form a complex in the presence of polyphosphate
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
polyphosphate kinase expresses poly(P):AMP phosphotransferase activity by coupling with adenylate kinase
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
polyphosphate kinase and adenylate kinase together constitute the polyP:AMP phosphotransferase activity. Polyphosphate kinase and adenylate kinase form a complex in the presence of polyphosphate
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
-
-
-
r
AMP + (phosphate)n
ADP + (phosphate)n-1
-
-
-
?, r
AMP + (phosphate)n
ADP + (phosphate)n-1
-
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
-
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
pap mutant is impaired in social motility, but shows only slightly reduced abilities in development and predation
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
-
-
-
?
AMP + (phosphate)n
ADP + (phosphate)n-1
-
the activity originates from combined action of the polyphosphate:ADP phosphotransferase and adenylate kinase
-
-
?
AMP + (phosphate)n+1
ADP + (phosphate)n
-
-
-
r
AMP + (phosphate)n+1
ADP + (phosphate)n
-
-
-
r
AMP + [phosphate]n
ADP + [phosphate]n-1
-
-
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
-
-
r
AMP + [phosphate]n
ADP + [phosphate]n-1
best substrate
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
polyphosphate with an average chain length of 35 phosphate groups is the best substrate
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
-
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
polyphosphate with an average chain length of 35 phosphate groups is the best substrate
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
-
-
r
AMP + [phosphate]n
ADP + [phosphate]n-1
best substrate
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
best substrate
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
-
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
-
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
-
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
-
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
best substrate
-
-
?
AMP + [phosphate]n
ADP + [phosphate]n-1
-
best substrate is [phosphate]15
-
-
?
CMP + [phosphate]n
CDP + [phosphate]n-1
low activity
-
-
?
CMP + [phosphate]n
CDP + [phosphate]n-1
0.09% of the activity with AMP
-
-
?
CMP + [phosphate]n
CDP + [phosphate]n-1
0.09% of the activity with AMP
-
-
?
dAMP + (phosphate)n+1
dADP + (phosphate)n
-
-
-
r
dAMP + (phosphate)n+1
dADP + (phosphate)n
-
-
-
r
dGMP + (phosphate)n+1
dGDP + (phosphate)n
-
-
-
r
dGMP + (phosphate)n+1
dGDP + (phosphate)n
-
-
-
r
GDP + [phosphate]n
GMP + [phosphate]n+1
-
-
-
r
GDP + [phosphate]n
GMP + [phosphate]n+1
-
-
-
r
GMP + [phosphate]n
GDP + [phosphate]n-1
-
-
-
-
?
GMP + [phosphate]n
GDP + [phosphate]n-1
-
-
-
?, r
GMP + [phosphate]n
GDP + [phosphate]n-1
-
-
-
-
r
GMP + [phosphate]n
GDP + [phosphate]n-1
10% of the activity with AMP
-
-
?
GMP + [phosphate]n
GDP + [phosphate]n-1
10% of the activity with AMP
-
-
?
GMP + [phosphate]n
GDP + [phosphate]n-1
-
-
-
-
?
GMP + [phosphate]n
GDP + [phosphate]n-1
-
-
-
-
?
UMP + [phosphate]n
UDP + [phosphate]n-1
low activity
-
-
?
UMP + [phosphate]n
UDP + [phosphate]n-1
0.13% of the activity with AMP
-
-
?
additional information
?
-
-
GMP, UMP, CMP and IMP are not converted to the corresponding diphosphates
-
-
?
additional information
?
-
-
development of a sensitive method for detecting AMP by using polyphosphate-AMP phosphotransferase, PPT, and adenylate kinase, ADK, from Acinetobacter johnsonii in conjugation with firefly luciferase, polyP65 is used as substrate with AMP and Mg2+, overview
-
-
?
additional information
?
-
-
no activity with ortho-, di-, tri-, and tetraphosphates, highest activities with polyphosphate of a degree of polymerization between 18 and 44 phosphate groups, overview
-
-
?
additional information
?
-
PAP acts as a poly(P)-dependent NMP kinase, activity for AMP by PAP is about 10times greater than that for GMP and 770 and about 1100times greater than that for UMP and CMP. ATP production by the coupled reactions of recombinant PAP and purified Escherichia coli poly(P) kinases from AMP. The purified recombinant PAP enzyme has not only strong PAP activity but also shows poly(P)-dependent nucleoside monophosphate kinase activity, by which it converts ribonucleoside monophosphates and deoxyribonucleoside monophosphates into ribonucleoside diphosphates and deoxyribonucleoside diphosphates, respectively
-
-
?
additional information
?
-
-
PPT substrate specificity, overview. GMP, UMP, CMP, and IMP are not converted to the corresponding diphosphates at significant rates
-
-
?
additional information
?
-
the forward reaction of polyphosphate utilization is preferred compared to the reverse reaction of polyphosphate synthesis. ADP is preferred over GDP as a phosphate donor for poly(P) synthesis. PAP of Acinetobacter johnsonii strain 210A is a type of poly(P) kinase that uses ADP and GDP as substrates, cf. EC 2.7.4.1. Analysis of the reversibility of the PAP reaction. The equilibrium ratio for the AMP and ADP formation by PAP is 1:19 in the presence of 100 mM MgCl2 and is changed to 1:9.6, i.e. 9.4% of 5 mM ADP is converted to AMP, in the presence of 20 mM MgCl2
-
-
?
additional information
?
-
-
the forward reaction of polyphosphate utilization is preferred compared to the reverse reaction of polyphosphate synthesis. ADP is preferred over GDP as a phosphate donor for poly(P) synthesis. PAP of Acinetobacter johnsonii strain 210A is a type of poly(P) kinase that uses ADP and GDP as substrates, cf. EC 2.7.4.1. Analysis of the reversibility of the PAP reaction. The equilibrium ratio for the AMP and ADP formation by PAP is 1:19 in the presence of 100 mM MgCl2 and is changed to 1:9.6, i.e. 9.4% of 5 mM ADP is converted to AMP, in the presence of 20 mM MgCl2
-
-
?
additional information
?
-
-
GMP, UMP, CMP and IMP are not converted to the corresponding diphosphates
-
-
?
additional information
?
-
-
PPT substrate specificity, overview. GMP, UMP, CMP, and IMP are not converted to the corresponding diphosphates at significant rates
-
-
?
additional information
?
-
-
no activity with ortho-, di-, tri-, and tetraphosphates, highest activities with polyphosphate of a degree of polymerization between 18 and 44 phosphate groups, overview
-
-
?
additional information
?
-
the forward reaction of polyphosphate utilization is preferred compared to the reverse reaction of polyphosphate synthesis. ADP is preferred over GDP as a phosphate donor for poly(P) synthesis. PAP of Acinetobacter johnsonii strain 210A is a type of poly(P) kinase that uses ADP and GDP as substrates, cf. EC 2.7.4.1. Analysis of the reversibility of the PAP reaction. The equilibrium ratio for the AMP and ADP formation by PAP is 1:19 in the presence of 100 mM MgCl2 and is changed to 1:9.6, i.e. 9.4% of 5 mM ADP is converted to AMP, in the presence of 20 mM MgCl2
-
-
?
additional information
?
-
-
the forward reaction of polyphosphate utilization is preferred compared to the reverse reaction of polyphosphate synthesis. ADP is preferred over GDP as a phosphate donor for poly(P) synthesis. PAP of Acinetobacter johnsonii strain 210A is a type of poly(P) kinase that uses ADP and GDP as substrates, cf. EC 2.7.4.1. Analysis of the reversibility of the PAP reaction. The equilibrium ratio for the AMP and ADP formation by PAP is 1:19 in the presence of 100 mM MgCl2 and is changed to 1:9.6, i.e. 9.4% of 5 mM ADP is converted to AMP, in the presence of 20 mM MgCl2
-
-
?
additional information
?
-
PAP acts as a poly(P)-dependent NMP kinase, activity for AMP by PAP is about 10times greater than that for GMP and 770 and about 1100times greater than that for UMP and CMP. ATP production by the coupled reactions of recombinant PAP and purified Escherichia coli poly(P) kinases from AMP. The purified recombinant PAP enzyme has not only strong PAP activity but also shows poly(P)-dependent nucleoside monophosphate kinase activity, by which it converts ribonucleoside monophosphates and deoxyribonucleoside monophosphates into ribonucleoside diphosphates and deoxyribonucleoside diphosphates, respectively
-
-
?
additional information
?
-
-
PAP acts as a poly(P)-dependent NMP kinase, activity for AMP by PAP is about 10times greater than that for GMP and 770 and about 1100times greater than that for UMP and CMP. ATP production by the coupled reactions of recombinant PAP and purified Escherichia coli poly(P) kinases from AMP. The purified recombinant PAP enzyme has not only strong PAP activity but also shows poly(P)-dependent nucleoside monophosphate kinase activity, by which it converts ribonucleoside monophosphates and deoxyribonucleoside monophosphates into ribonucleoside diphosphates and deoxyribonucleoside diphosphates, respectively
-
-
?
additional information
?
-
-
Escherichia coli strain JM109 possesses a very low level of intrinsic PAP activity that catalyzes the synthesis of ADP from AMP and polyphosphate. PPK and ADK together constitute the PAP activity, where it phosphorylates AMP with polyphosphate
-
-
?
additional information
?
-
-
Escherichia coli strain JM109 possesses a very low level of intrinsic PAP activity that catalyzes the synthesis of ADP from AMP and polyphosphate. PPK and ADK together constitute the PAP activity, where it phosphorylates AMP with polyphosphate
-
-
?
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
?
-
class III PPK2 shows broad substrate specificity over purine and pyrimidine bases. This class III PPK2 possesses both class I and II activities
-
-
?
additional information
?
-
class III PPK2 shows broad substrate specificity, the enzyme prefers polyphosphate of 25 to 50 in chain length. PPK2 also possesses PAP activity
-
-
?
additional information
?
-
class III PPK2 shows broad substrate specificity over purine and pyrimidine bases. This class III PPK2 possesses both class I and II activities
-
-
?
additional information
?
-
class III PPK2 shows broad substrate specificity, the enzyme prefers polyphosphate of 25 to 50 in chain length. PPK2 also possesses PAP activity
-
-
?
additional information
?
-
-
the partially purified polyphosphate:ADP phosphotransferase is independent of polyphosphate kinase, PPK, and can function as polyphosphate-dependent nucleoside diphosphate kinase, PADP, which most prefers GDP to the other three nucleoside diphosphates as a phospho-acceptor. Both of the polyphosphate-utilizing activities require short polyphosphate as a phospho-donor whose chain length is below 75. The PAP activity mainly originates from the combined action of adenylate kinase, ADK, and the PADP independent of PPK. Each partially purified enzyme alone cannot mediate phosphorylation of AMP with polyphosphate, but coincubation of the both enzymes results in a marked expression of PAP activity, confirming that PADP and ADK constitute the PAP
-
-
?
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0.055 - 0.11
(phosphate)3
0.0008 - 0.062
(Phosphate)n
8.3
ADP
reverse reaction of polyphosphate synthesis, pH 8.0, 37°C
0.0008
[phosphate]n
-
polyphosphate with an average chain length of 35 phosphate groups, pH 8.5, 30°C
-
0.055
(phosphate)3
wild type enzyme, with GMP as cosubstrate, at pH 8.0 temperature not specified in the publication
0.11
(phosphate)3
wild type enzyme, with AMP as cosubstrate, at pH 8.0 temperature not specified in the publication
0.0008
(Phosphate)n
-
pH and temperature not specified in the publication, polyphosphate with an average chain length of 35 phosphate groups
0.025
(Phosphate)n
wild type enzyme, with GMP as cosubstrate, at pH 8.0 temperature not specified in the publication
0.062
(Phosphate)n
wild type enzyme, with AMP as cosubstrate, at pH 8.0 temperature not specified in the publication
0.26
AMP
-
pH 8.5, 30°C
0.26
AMP
-
pH and temperature not specified in the publication
0.27
AMP
forward reaction of ADP synthesis, pH 8.0, 37°C
0.27
AMP
recombinant PAP, pH 8.0, 37°C
0.45
AMP
recombinant PAP, pH 8.0, 37°C, in presence of 50 mM (NH4)2SO4
0.82
AMP
wild type enzyme, at pH 8.0 temperature not specified in the publication
1.55
GMP
wild type enzyme, at pH 8.0 temperature not specified in the publication
4.4
GMP
recombinant PAP, pH 8.0, 37°C
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0.0002
-
ATP formation from AMP, pH 7.0, 37°C, PMM-resistant clone AG83
0.00047
-
ATP formation from AMP, pH 7.0, 37°C, wild-type clone AG83
0.0005
-
ATP formation from AMP, pH 7.0, 37°C, SSG-resistant clone AG83
0.00957
-
pH and temperature not specified in the publication
0.01
-
cell-free isolate, pH and temperature not specified in the publication
0.08
AMP to ATP activity of the mutant E126N, pH 7.0, 70°C
0.28
AMP to ATP activity of the mutant E126G, pH 7.0, 70°C
0.37
ADP to ATP activity of the mutant E126N, pH 7.0, 70°C
0.63
ADP to ATP activity of the mutant E126G, pH 7.0, 70°C
1.6
AMP to ATP activity of the wild-type enzyme, pH 7.0, 70°C
101.2
-
purified native enzyme, pH 8.5, 30°C
12
-
partially purified native enzyme, pH 8.0, 37°C, ADP synthesis
2.48
crude extract of recombinant Escherichia coli strain JM109, pH 8.0, 37°C
2.7
ADP to ATP activity of the wild-type enzyme, pH 7.0, 70°C
24.9
purified recombinant PAP tetramer, pH 8.0, 37°C
54.9
purified recombinant PAP dimer, pH 8.0, 37°C
9570
-
purified native enzyme, pH 7.4, 30°C
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evolution
polyphosphate kinases, responsible for the synthesis and utilization of polyphosphate, are divided into two families (PPK1 and PPK2) due to differences in amino acid sequence and kinetic properties. Phylogenetic analysis suggests that the PPK2 family is divided into three subfamilies (classes I, II, and III). Class I and II PPK2s catalyze nucleoside diphosphate and nucleoside monophosphate phosphorylation, respectively. Class III PPK2 catalyzes both nucleoside monophosphate and nucleoside diphosphate phosphorylation synthesizing ATP from AMP. Class III PPK2 shows broad substrate specificity over purine and pyrimidine bases. Class III PPK2 possesses both class I and II activities. The class III subfamily is closest to a PPK2 ancestor, overview
evolution
-
polyphosphate kinases, responsible for the synthesis and utilization of polyphosphate, are divided into two families (PPK1 and PPK2) due to differences in amino acid sequence and kinetic properties. Phylogenetic analysis suggests that the PPK2 family is divided into three subfamilies (classes I, II, and III). Class I and II PPK2s catalyze nucleoside diphosphate and nucleoside monophosphate phosphorylation, respectively. Class III PPK2 catalyzes both nucleoside monophosphate and nucleoside diphosphate phosphorylation synthesizing ATP from AMP. Class III PPK2 shows broad substrate specificity over purine and pyrimidine bases. Class III PPK2 possesses both class I and II activities. The class III subfamily is closest to a PPK2 ancestor, overview
-
physiological function
-
PPT from Acinetobacter johnsonii is specific for AMP and 2'-dAMP
physiological function
-
the inhibition of polyphosphate:AMP phosphotransferase-mediated degradation by diphosphate and triphosphate is abolished by the inorganic diphosphatase, EC 3.6.1.1
physiological function
enzyme PPK2 catalyzes preferentially polyphosphate-driven nucleotide phosphorylation (utilization of polyphosphate), which is important for the survival of microbial cells under conditions of stress or pathogenesis. Class III PPK2 catalyzes both nucleoside monophosphate and nucleoside diphosphate phosphorylation, synthesizing ATP from AMP by a single enzyme
physiological function
-
substrate level phosphorylation is essential for the survival of amastigote forms of Leishmania donovani
physiological function
-
enzyme PPK2 catalyzes preferentially polyphosphate-driven nucleotide phosphorylation (utilization of polyphosphate), which is important for the survival of microbial cells under conditions of stress or pathogenesis. Class III PPK2 catalyzes both nucleoside monophosphate and nucleoside diphosphate phosphorylation, synthesizing ATP from AMP by a single enzyme
-
physiological function
-
substrate level phosphorylation is essential for the survival of amastigote forms of Leishmania donovani
-
physiological function
-
PPT from Acinetobacter johnsonii is specific for AMP and 2'-dAMP
-
physiological function
-
the inhibition of polyphosphate:AMP phosphotransferase-mediated degradation by diphosphate and triphosphate is abolished by the inorganic diphosphatase, EC 3.6.1.1
-
additional information
-
ATP regeneration from AMP and polyphophate using PPT, firefly luciferase and hexokinase as model ATP-requiring enzymes, ADP can be converted to ATP by adenylate kinase, AdK. Establishment of a PPT/AdK system for ATP regeneration with coupled hexokinase, overview
additional information
-
overexpression in strain PAO1 leads to a massive production of polyphosphate kinase, PPK, and a marked enhancement of polyphosphate-synthesizing activity, while the PAP activity is not affected by overproduction of PPK
additional information
PAP contains two putative phosphate-binding motifs, P-loops. The similarity between PAP and the PPK2 homologues indicates that there is a common mechanism by which these enzymes use poly(P) for phosphorylation of nucleosides. The C-terminal region of PAP, including one P-loop (amino acids 286 to 292), is thought to be essential for poly(P)-dependent nucleotide phosphorylation. An additional P-loop in the N-terminal region (amino acids 45 to 51) of PAP may play a crucial role in binding with nucleoside monophosphate
additional information
-
polyphosphate kinase, PPK, responsible for the processive synthesis of inorganic polyphosphate from ATP in Escherichia coli, can transfer in reverse the terminal phosphate residue of polyphosphate to ADP to yield ATP. When coexpressed with adenylate kinase, ADK, in Escherichia coli, PPK and ADK together highly enhance the PAP activity in Escherichia coli
additional information
residue E126 is important for class III PPK2 activity. Structure homology modeling using the Arthrobacter aurescens PPK2 enzyme (PDB ID 3RHF) sequence as template
additional information
-
residue E126 is important for class III PPK2 activity. Structure homology modeling using the Arthrobacter aurescens PPK2 enzyme (PDB ID 3RHF) sequence as template
-
additional information
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ATP regeneration from AMP and polyphophate using PPT, firefly luciferase and hexokinase as model ATP-requiring enzymes, ADP can be converted to ATP by adenylate kinase, AdK. Establishment of a PPT/AdK system for ATP regeneration with coupled hexokinase, overview
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additional information
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PAP contains two putative phosphate-binding motifs, P-loops. The similarity between PAP and the PPK2 homologues indicates that there is a common mechanism by which these enzymes use poly(P) for phosphorylation of nucleosides. The C-terminal region of PAP, including one P-loop (amino acids 286 to 292), is thought to be essential for poly(P)-dependent nucleotide phosphorylation. An additional P-loop in the N-terminal region (amino acids 45 to 51) of PAP may play a crucial role in binding with nucleoside monophosphate
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additional information
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polyphosphate kinase, PPK, responsible for the processive synthesis of inorganic polyphosphate from ATP in Escherichia coli, can transfer in reverse the terminal phosphate residue of polyphosphate to ADP to yield ATP. When coexpressed with adenylate kinase, ADK, in Escherichia coli, PPK and ADK together highly enhance the PAP activity in Escherichia coli
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E126G
site-directed mutagenesis, ATP synthesis activity from AMP by the mutants is reduced to 17.5% and ATP synthesis activity from ADP to 23.3% of the wild-type enzyme
E126N
site-directed mutagenesis, ATP synthesis activity from AMP by the mutants is reduced to 5.0% of the wild-type enzyme
E126G
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site-directed mutagenesis, ATP synthesis activity from AMP by the mutants is reduced to 17.5% and ATP synthesis activity from ADP to 23.3% of the wild-type enzyme
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E126N
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site-directed mutagenesis, ATP synthesis activity from AMP by the mutants is reduced to 5.0% of the wild-type enzyme
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D307A
the mutation leads to strongly reduced activity compared to the wild type enzyme
D320A
the mutation leads to slightly reduced activity compared to the wild type enzyme
D323A
the mutation leads to slightly reduced activity compared to the wild type enzyme
E304A
the mutation leads to strongly reduced activity compared to the wild type enzyme
K311A
the mutation leads to strongly reduced activity compared to the wild type enzyme
K473A
the mutation leads to slightly reduced activity compared to the wild type enzyme
Q416A
the mutation leads to reduced activity compared to the wild type enzyme
R316A
the mutation leads to slightly reduced activity compared to the wild type enzyme
R325A
the mutation leads to slightly reduced activity compared to the wild type enzyme
R423A
the mutation leads to strongly reduced activity compared to the wild type enzyme
R477A
the mutation leads to slightly increased activity compared to the wild type enzyme
W408A
the mutation leads to strongly reduced activity compared to the wild type enzyme
Y447A
the mutation leads to reduced activity compared to the wild type enzyme
D307A
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the mutation leads to strongly reduced activity compared to the wild type enzyme
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D320A
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the mutation leads to slightly reduced activity compared to the wild type enzyme
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D323A
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the mutation leads to slightly reduced activity compared to the wild type enzyme
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R325A
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the mutation leads to slightly reduced activity compared to the wild type enzyme
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analysis
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sensitive method for detecting AMP by using polyphosphate(polyP)-AMP phosphotransferase and adenylate kinase from Acinetobacter johnsonii in conjugation with firefly luciferase. The method allows detection of AMP over the concentration range of 0.3-100 pmol per assay
diagnostics
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AMP is known to have potential for use as a reliable indicator in hygiene monitoring, the development of a sensitive method for detecting AMP, by using polyphosphate-AMP phosphotransferase and adenylate kinase in conjugation with firefly luciferase, is useful to detect food samples with high sensitivity
food industry
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AMP is known to have potential for use as a reliable indicator in hygiene monitoring, the development of a sensitive method for detecting AMP, by using polyphosphate-AMP phosphotransferase and adenylate kinase in conjugation with firefly luciferase, is useful to detect food samples with high sensitivity
additional information
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AMP is known to have potential for use as a reliable indicator in hygiene monitoring, the development of a sensitive method for detecting AMP, by using polyphosphate-AMP phosphotransferase and adenylate kinase in conjugation with firefly luciferase, is useful to detect food samples with high sensitivity
synthesis
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design of an ATP regeneration system with poylphosphate-AMP phosphotransferase and polyphosphate kinase. The ATP regeneration system can also be used as a GTP regeneration system
synthesis
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PPT catalyzes a key reaction in the cell-free regeneration of ATP from AMP and polyphosphate. The PPT/AdK system provides an alternative to existing enzymatic ATP regeneration systems in which phosphoenolpyruvate and acetylphosphate serve as phosphoryl donors and has the advantage that AMP and polyP are stable, inexpensive substrates
synthesis
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the phospho-conversion of AMP to ADP using polyphosphate as phosphate donor by polyphosphate-AMP phosphotransferase, PAP, followed by the synthesis of ATP from ADP through poylphosphate kinase, PPK, is used as an ATP regenrating system. The PAP-PPK ATP regeneration system can continously produce ATP in the coupled reaction from polyphosphate, whhich is a cheaper substrate than acetylphosphate, phosphoenolphosphate, or creatine phosphate. The system can also regenerate GTP from GMP. Method optimization, overview. ATP can be used for e.g. synthesis of acetly-CoA
synthesis
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the phospho-conversion of AMP to ADP using polyphosphate as phosphate donor by polyphosphate-AMP phosphotransferase, PAP, followed by the synthesis of ATP from ADP through poylphosphate kinase, PPK, is used as an ATP regenrating system. The PAP-PPK ATP regeneration system can continously produce ATP in the coupled reaction from polyphosphate, whhich is a cheaper substrate than acetylphosphate, phosphoenolphosphate, or creatine phosphate. The system can also regenerate GTP from GMP. Method optimization, overview. ATP can be used for e.g. synthesis of acetly-CoA
synthesis
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design of an ATP regeneration system with poylphosphate-AMP phosphotransferase and polyphosphate kinase. The ATP regeneration system can also be used as a GTP regeneration system
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synthesis
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the phospho-conversion of AMP to ADP using polyphosphate as phosphate donor by polyphosphate-AMP phosphotransferase, PAP, followed by the synthesis of ATP from ADP through poylphosphate kinase, PPK, is used as an ATP regenrating system. The PAP-PPK ATP regeneration system can continously produce ATP in the coupled reaction from polyphosphate, whhich is a cheaper substrate than acetylphosphate, phosphoenolphosphate, or creatine phosphate. The system can also regenerate GTP from GMP. Method optimization, overview. ATP can be used for e.g. synthesis of acetly-CoA
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synthesis
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PPT catalyzes a key reaction in the cell-free regeneration of ATP from AMP and polyphosphate. The PPT/AdK system provides an alternative to existing enzymatic ATP regeneration systems in which phosphoenolpyruvate and acetylphosphate serve as phosphoryl donors and has the advantage that AMP and polyP are stable, inexpensive substrates
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Kameda, A.; Shiba, T.; Kawazoe, Y.; Satoh, Y.; Ihara, Y.; Munekata, M.; Ishige, K.; Noguchi, T.
A novel ATP regeneration system using polyphosphate-AMP phosphotransferase and polyphosphate kinase
J. Biosci. Bioeng.
91
557-563
2001
Acinetobacter johnsonii, Myxococcus xanthus, Myxococcus xanthus DK101
brenda
van Groenstijn, J.W.; Bentvelsen, M.M.A.; Deinema, M.H.; Zehnder, A.J.B.
Polyphosphate-degrading enzymes in Acinetobacter spp. and activated sludge
Appl. Environ. Microbiol.
55
219-223
1989
Acinetobacter sp.
brenda
Resnick, S.M.; Zehnder, A.J.B.
In vitro ATP regeneration from polyphosphate and AMP by polyphosphate:AMP phosphotransferase and adenylate kinase from Acinetobacter johnsonii 210A
Appl. Environ. Microbiol.
66
2045-2051
2000
Acinetobacter johnsonii, Acinetobacter johnsonii 210A
brenda
Ishige, K.; Noguchi, T.
Polyphosphate:AMP phosphotransferase and polyphosphate:ADP phosphotransferase activities of Pseudomonas aeruginosa
Biochem. Biophys. Res. Commun.
281
821-826
2001
Pseudomonas aeruginosa
brenda
Tanaka, S.; Kuroda, A.; Kato, J.; Ikeda, T.; Takiguchi, N.; Ohtake, H.
A sensitive method for detecting AMP by utilizing polyphosphate-dependent ATP regeneration and bioluminescence reactions
Biochem. Eng. J.
9
193-197
2001
Acinetobacter johnsonii
-
brenda
Shiba, T.; Tsutsumi, K.; Ishige, K.; Noguchi, T.
Inorganic polyphosphate and polyphosphate kinase: their novel biological function and applications
Biochemistry
65
375-384
2000
Escherichia coli
-
brenda
Bonting, C.F.C.; Kortstee, G.J.J.; Zehnder, A.J.B.
Properties of polyphosphate:AMP phosphotransferase of Acinetobacter strain 210A
J. Bacteriol.
173
6484-6488
1991
Acinetobacter johnsonii, Acinetobacter sp., Acinetobacter johnsonii 210A, Acinetobacter sp. 210A
brenda
Ishige, K.; Noguchi, T.
Inorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli
Proc. Natl. Acad. Sci. USA
97
14168-14171
2000
Escherichia coli, Escherichia coli JM109
brenda
Zhang, H.; Rao, N.N.; Shiba, T.; Kornberg, A.
Inorganic polyphosphate in the social life of Myxococcus xanthus: motility, development, and predation
Proc. Natl. Acad. Sci. USA
102
13416-13420
2005
Myxococcus xanthus (Q4JGY7)
brenda
Shi, X.; Rao, N.N.; Kornberg, A.
Inorganic polyphosphate in Bacillus cereus
Proc. Natl. Acad. Sci. USA
49
17061-17065
2004
Bacillus cereus
brenda
Bonting, C.; Gerards, R.; Zehnder, A.; Kortstee, G.
Purification and properties of pyrophosphatase of Acinetobacter johnsonii 210A and its involvement in the degradation of polyphosphate
Biodegradation
10
393-398
1999
Acinetobacter johnsonii, Acinetobacter johnsonii 210A
brenda
Bark, K.; Kaempfer, P.; Sponner, A.; Dott, W.
Polyphosphate-dependent enzymes in some coryneform bacteria isolated from sewage sludge
FEMS Microbiol. Lett.
107
133-138
1993
Cellulosimicrobium cellulans, no activity in Curtobacterium sp., no activity in Shewanella putrefaciens, no activity in Aureobacterium saperdae
brenda
Itoh, H.; Shiba, T.
Polyphosphate synthetic activity of polyphosphate:AMP phosphotransferase in Acinetobacter johnsonii 210A
J. Bacteriol.
186
5178-5181
2004
Acinetobacter johnsonii (Q83XD3), Acinetobacter johnsonii, Acinetobacter johnsonii 210A (Q83XD3), Acinetobacter johnsonii 210A
brenda
Shiba, T.; Itoh, H.; Kameda, A.; Kobayashi, K.; Kawazoe, Y.; Noguchi, T.
Polyphosphate:AMP phosphotransferase as a polyphosphate-dependent nucleoside monophosphate kinase in Acinetobacter johnsonii 210A
J. Bacteriol.
187
1859-1865
2005
Acinetobacter johnsonii (Q83XD3), Acinetobacter johnsonii 210A (Q83XD3), Acinetobacter johnsonii 210A
brenda
Motomura, K.; Hirota, R.; Okada, M.; Ikeda, T.; Ishida, T.; Kuroda, A.
A new subfamily of polyphosphate kinase 2 (class III PPK2) catalyzes both nucleoside monophosphate phosphorylation and nucleoside diphosphate phosphorylation
Appl. Environ. Microbiol.
80
2602-2608
2014
Meiothermus ruber (A0A806DL21), Meiothermus ruber NBRC 106122 (A0A806DL21)
brenda
Jyoti Roy, J.; Mondal, S.; Bera, T.
Polyphosphate kinase from Leishmania donovani amastigotes: A polyphosphate driven generator of ATP
Int. J. Drug Develop. Res.
6
159-164
2014
Leishmania donovani, Leishmania donovani MHOM/IN/83/AG83
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brenda
Nocek, B.; Kochinyan, S.; Proudfoot, M.; Brown, G.; Evdokimova, E.; Osipiuk, J.; Edwards, A.; Savchenko, A.; Joachimiaka, A.; Yakunin, A.
Polyphosphate-dependent synthesis of ATP and ADP by the family-2 polyphosphate kinases in bacteria
Proc. Natl. Acad. Sci. USA
105
17730-17735
2008
Pseudomonas aeruginosa (Q9HYF1), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9HYF1)
brenda