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Ligand Polyphosphate

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (13 results)

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Show Natural Substrate (13 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.63

(phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate

659420, 721374, 721367, 737862, 739015, 737557, 760392, 761859, 641755

-

2.7.1.63

(phosphate)n + mannose = (phosphate)n-1 + mannose 6-phosphate

739015

-

2.7.4.1

ADP + (phosphate)n = ATP + (phosphate)n-1

756630, 738411, 737886, 737921

-

2.7.4.1

ATP + (phosphate)n = ADP + (phosphate)n+1

676086, 645121, 695092, 738473, 760795, 690520, 674956, 761394, 737506, 738966, 739001, 645127, 645114, 661793, 680262, 674343, 694850, 671494, 760406, 760941

-

2.7.4.1

CDP + (phosphate)n = CTP + (phosphate)n-1

737921

-

2.7.4.1

GDP + (phosphate)n = GTP + (phosphate)n-1

737921

-

2.7.4.1

UDP + (phosphate)n = UTP + (phosphate)n-1

737921

-

2.7.1.63

2 entries

2.7.4.1

5 entries

2.7.4.20

dolichyl diphosphate + (phosphate)n = dolichyl phosphate + (phosphate)n+1

642550, 642549

-

2.7.4.33

ADP + (phosphate)n = ATP + (phosphate)n-1

738411, 737499

-

2.7.4.33

AMP + (phosphate)n = ADP + (phosphate)n-1

738411, 737499, 720949, 720887

-

2.7.4.33

2 entries

2.7.4.34

GTP + (phosphate)n = GDP + (phosphate)n+1

761927, 762302

-

3.6.1.11

(phosphate)n + H2O = (phosphate)n-1 + phosphate

685297, 685307, 688364, 690206, 701387, 696296, 697460

-

7.1.3.1

polyphosphate + H2O = ?

656234

-

In Vivo Product in Enzyme-catalyzed Reactions (9 results)

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Show Natural Product (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.4.1

ADP + (phosphate)n+1 = ATP + (phosphate)n

0

-

2.7.4.1

CDP + (phosphate)n+1 = CTP + (phosphate)n

645125

-

2.7.4.1

dADP + (phosphate)n+1 = dATP + (phosphate)n

645125

-

2.7.4.1

dCDP + (phosphate)n+1 = dCTP + (phosphate)n

645125

-

2.7.4.1

dGDP + (phosphate)n+1 = dGTP + (phosphate)n

645125

-

2.7.4.1

GDP + (phosphate)n+1 = GTP + (phosphate)n

645125

-

2.7.4.1

TDP + (phosphate)n+1 = TTP + (phosphate)n

645125

-

2.7.4.1

UDP + (phosphate)n+1 = UTP + (phosphate)n

645125

-

2.7.4.1

8 entries

2.7.4.34

GDP + (phosphate)n+1 = GTP + (phosphate)n

0

-

Substrate in Enzyme-catalyzed Reactions (37 results)

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Show Substrate (37 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.23

polyphosphate + NAD+ = (phosphate)n-1 + NADP+

661147, 660762

-

2.7.1.23

polyphosphate + NAD+ = ?

641187, 641191, 641186

-

2.7.1.63

(phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate

641744, 673712, 641745, 641746, 659420, 641754, 641748, 721374, 641747, 641753, 641752, 721367, 737862, 739015, 737557, 760392, 761859, 641749, 641743, 641751, 641750, 641755

-

2.7.1.63

(phosphate)n + D-mannose = (phosphate)n-1 + D-mannose 6-phosphate

641753, 641754

-

2.7.1.63

(phosphate)n + glucosamine = (phosphate)n-1 + D-glucosamine 6-phosphate

641753

-

2.7.1.63

(phosphate)n + mannose = (phosphate)n-1 + mannose 6-phosphate

739015

-

2.7.4.1

ADP + (phosphate)n = ATP + (phosphate)n-1

723676, 721876, 722134, 756630, 723523, 738411, 737886, 737921, 674956

-

2.7.4.1

ATP + (phosphate)n = ADP + (phosphate)n+1

645113, 645114, 722321, 722134, 722867, 645117, 676086, 672491, 701795, 706869, 680262, 706486, 701716, 645121, 671494, 760406, 645119, 723523, 723545, 701817, 721387, 645110, 645123, 645128, 674343, 676890, 695092, 738473, 674956, 760795, 690520, 706871, 702927, 702901, 761394, 701814, 737506, 760742, 738966, 739001, 760249, 760384, 762301, 645129, 694850, 645132, 645124, 645120, 645131, 645122, 645115, 645133, 645116, 645111, 645112, 645118, 645127, 661793, 663267, 760941

-

2.7.4.1

CDP + (phosphate)n = CTP + (phosphate)n-1

737921

-

2.7.4.1

GDP + (phosphate)n = GTP + (phosphate)n-1

738411, 737886, 737921

-

2.7.4.1

GTP + (phosphate)n = GDP + (phosphate)n+1

671494, 645131

-

2.7.4.1

ITP + (phosphate)n = IDP + (phosphate)n+1

671494

-

2.7.4.1

UDP + (phosphate)n = UTP + (phosphate)n-1

737921

-

2.7.1.23

2 entries

2.7.1.63

4 entries

2.7.4.1

7 entries

2.7.4.20

dolichyl diphosphate + (phosphate)n = dolichyl phosphate + (phosphate)n+1

642550, 642549

-

2.7.4.33

2'-dAMP + (phosphate)n = 2'-dADP + (phosphate)n-1

718620

-

2.7.4.33

ADP + (phosphate)n = AMP + (phosphate)n+1

758213

-

2.7.4.33

ADP + (phosphate)n = ATP + (phosphate)n-1

738411, 737499

-

2.7.4.33

AMP + (phosphate)n = ADP + (phosphate)n-1

720949, 738411, 645130, 718617, 718620, 720887, 737499, 719681, 720883, 718947, 718728

-

2.7.4.33

GDP + (phosphate)n = GMP + (phosphate)n+1

758213

-

2.7.4.33

5 entries

2.7.4.34

GTP + (phosphate)n = GDP + (phosphate)n+1

760742, 761927, 760384, 762302, 762301

-

2.7.4.B7

ATP + (phosphate)n = ADP + (phosphate)n+1

762661

-

2.7.4.B7

CTP + (phosphate)n = CDP + (phosphate)n+1

762661

-

2.7.4.B7

dTTP + (phosphate)n = dTDP + (phosphate)n+1

762661

-

2.7.4.B7

GTP + (phosphate)n = GDP + (phosphate)n+1

762661

-

2.7.4.B7

UTP + (phosphate)n = UDP + (phosphate)n+1

762661

-

2.7.4.B7

5 entries

2.7.7.53

NDP + polyphosphate = polyphosphate + NDP

643514

-

3.1.3.2

polyphosphate + H2O = ?

653439

-

3.1.3.2

polyphosphate + H2O = phosphate

716625

-

3.1.3.2

2 entries

3.1.3.26

polyphosphate + H2O = ?

653518

-

3.1.3.8

polyphosphate + H2O = ?

653518

-

3.6.1.1

polyphosphate + H2O = ?

712277

-

3.6.1.10

polyphosphate + H2O = oligophosphate

209837, 209836, 209835, 209834, 209833

-

3.6.1.11

(phosphate)n + H2O = (phosphate)n-1 + phosphate

685297, 685307, 687678, 688364, 690206, 720842, 701387, 696296, 697460

-

3.6.1.11

polyphosphate + H2O = ?

668027

-

3.6.1.11

2 entries

3.6.1.40

polyphosphate + H2O = ?

209848

-

3.6.1.52

polyphosphate + H2O = ?

757172

-

7.1.3.1

polyphosphate + H2O = ?

656234

-

Product in Enzyme-catalyzed Reactions (33 results)

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Show Product (33 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.17

cob(I)inamide + ATP = 5'-deoxy-5'-adenosyl-cob(I)inamide + polyphosphate

636868

-

2.5.1.17

cob(I)yric acid + ATP = 5'-deoxy-5'-adenosyl-cob(I)yric acid + polyphosphate

636868

-

2.5.1.17

cob(I)yrinic acid a,c-diamide + ATP = 5'-deoxy-5'-adenosyl-cob(I)yrinic acid a,c-diamide + polyphosphate

636868

-

2.7.4.1

ADP + (phosphate)n+1 = ATP + (phosphate)n

645116, 645125, 0, 645124, 645117

-

2.7.4.1

AMP + (phosphate)n+1 = ADP + (phosphate)n

0

-

2.7.4.1

AMP + (phosphate)n+2 = ATP + (phosphate)n

0

-

2.7.4.1

ATP + (phosphate)n+1 = ADP + (phosphate)n

0

-

2.7.4.1

CDP + (phosphate)n+1 = CTP + (phosphate)n

645125, 0

-

2.7.4.1

dADP + (phosphate)n+1 = dATP + (phosphate)n

645125, 0

-

2.7.4.1

dAMP + (phosphate)n+1 = dADP + (phosphate)n

0

-

2.7.4.1

dCDP + (phosphate)n+1 = dCTP + (phosphate)n

645125

-

2.7.4.1

dGDP + (phosphate)n+1 = dGTP + (phosphate)n

645125

-

2.7.4.1

GDP + (phosphate)n+1 = GTP + (phosphate)n

645129, 0, 645125

-

2.7.4.1

GDP + (phosphate)n+2 = guanosine 5'-tetraphosphate + (phosphate)n

645129, 645125

-

2.7.4.1

GMP + (phosphate)n+1 = GDP + (phosphate)n

0

-

2.7.4.1

GTP + (phosphate)n+1 = GDP + (phosphate)n

0

-

2.7.4.1

TDP + (phosphate)n+1 = TTP + (phosphate)n

645125

-

2.7.4.1

UDP + (phosphate)n+1 = UTP + (phosphate)n

645125

-

2.7.4.33

AMP + (phosphate)n+1 = ADP + (phosphate)n

0

-

2.7.4.33

dAMP + (phosphate)n+1 = dADP + (phosphate)n

0

-

2.7.4.33

dGMP + (phosphate)n+1 = dGDP + (phosphate)n

0

-

2.7.4.33

GMP + (phosphate)n+1 = GDP + (phosphate)n

0

-

2.7.4.33

IMP + (phosphate)n+1 = IDP + (phosphate)n

0

-

2.7.4.33

XMP + (phosphate)n+1 = XDP + (phosphate)n

0

-

2.7.4.34

ADP + (phosphate)n+1 = ATP + (phosphate)n

0

-

2.7.4.34

GDP + (phosphate)n+1 = GTP + (phosphate)n

0

-

2.7.4.34

GMP + (phosphate)n+2 = GTP + (phosphate)n

0

-

2.7.4.B7

ADP + (phosphate)n+1 = ATP + (phosphate)n

0

-

2.7.4.B7

CDP + (phosphate)n+1 = CTP + (phosphate)n

0

-

2.7.4.B7

dTDP + (phosphate)n+1 = dTTP + (phosphate)n

0

-

2.7.4.B7

GDP + (phosphate)n+1 = GTP + (phosphate)n

0

-

2.7.4.B7

UDP + (phosphate)n+1 = UTP + (phosphate)n

0

-

2.5.1.17

3 entries

2.7.4.1

15 entries

2.7.4.33

6 entries

2.7.4.34

3 entries

2.7.4.B7

5 entries

2.7.7.53

NDP + polyphosphate = polyphosphate + NDP

643514

-

Activator in Enzyme-catalyzed Reactions (13 results)

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Show Activating Compound (13 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.30

addition of inorganic polyphosphate (PPin) inhibits or activates glycerol kinase due to the complexation of PPin with Mg2+ that shifts Mg2+ to ATP molar ratio below or to the optimum level

761883

-

2.7.1.7

dependent on, can be substituted by ATP, nonprocessive utilization, binding site is the same as for ATP binding

641754

-

2.7.4.1

activation of polyphosphate kinase 2

645131

-

2.7.4.1

stimulation

762301

-

2.7.4.1

2 entries

2.7.4.34

stimulation

762301

-

3.4.21.38

-

753067, 753351

-

3.4.21.5

PolyP, secreted by activated platelets, a highly anionic polymer, polyphosphate plus beta-thrombin accelerates plasma clotting and enhances thrombin generation, kinetics, overview. Thrombin binds with high affinity to immobilized polyphosphate. Polyphosphate accelerates factor XI autoactivation and factor XIa autolysis

717429

-

3.4.21.53

changes substrate preference of enzyme and its oligomeric structure

668624

-

3.4.21.53

forms a complex with lon, which enables lon to degrade free ribosomal proteins. Polyphosphate with a shorter chain length is less potent in stimulating. Polyphosphate-binding site is within the ATPase domain fo lon between amino acids 320 and 437

678789

-

3.4.21.53

its binding within the ATPase domain of lon promotes the specific association and degradation of free ribosomal proteins

681850

-

3.4.21.53

stimulates lon proteolytic activity, affects substrate preference and oligomeric state of the enzyme

682821

-

3.4.21.53

stimulates lon-mediated proteolysis of free ribosomal proteins and thereby down-regulates translation

678475

-

3.4.21.53

upon binding to a site in the ATPase domain, stimulation of degradation of ribosomal protein and inhibition of DNA-enzyme complex formation

669248

-

3.4.21.53

6 entries

Inhibitor in Enzyme-catalyzed Reactions (13 results)

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Show Inhibitors (13 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.30

addition of inorganic polyphosphate (PPin) inhibits or activates glycerol kinase due to the complexation of polyphosphate with Mg2+ that shifts Mg2+ to ATP molar ratio below or to the optimum level

761883

-

2.7.4.1

65 residues, competitive inhibition of polyphosphate 750 and GDP in guanosine 5'-tetraphosphate synthesis

645129

-

2.7.4.1

substrate inhibition at 2 mM

645121

-

2.7.7.19

inhibition depends on chain length, P3 10% at 0.001 mM, P4 60% at 0.001 mM, P15 90% at 0.001 mM, P35 100% at 0.001 mM

642980

-

2.7.7.19

potent inhibitor of poly(A) polymerase activity, almost complete inhibition at 200 nM

694438

-

2.7.7.19

with 20 nM to 0.002 mM of polyphosphate the length of the products is reduced but inhibition is not complete

694438

-

2.7.4.1

2 entries

2.7.7.19

3 entries

3.1.3.26

substrate inhibition above 5 mM

653518

-

3.1.3.8

substrate inhibition above 5 mM

653518

-

3.2.1.28

-

679765

-

3.4.21.53

competitively blocks DNA binding by lon in vitro and in vivo

678475

-

3.4.21.53

slightly inhibits degradation of a maltose-binding protein-SulA fusion. At the ATP domain competes with DNA for binding to lon, completely inhibits the formation of a DNA-lon complex

678789

-

3.4.21.53

2 entries

3.6.1.11

polyP15, 50% inhibition at 200fold polymer molar excess over the long-chain polyphosphate substrate

209844

-

4.1.2.13

-

4943

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (14 results)

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Show Turnover Number (14 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.7.1.63

0.3

-

at pH 7.7 and 28°C

737862

2.7.1.63

48.2

-

at pH 7.5 and 28°C

739015

2.7.4.1

1.04

-

pH 7.5, 37°C, guanosine 5'-tetraphosphate synthesis

645129

2.7.4.1

77

-

pH 7.2, 30°C, recombinant wild-type enzyme

671494

2.7.4.33

6.7

-

wild type enzyme, with GMP as cosubstrate, at pH 8.0 temperature not specified in the publication

758213

2.7.4.33

37.7

-

wild type enzyme, with AMP as cosubstrate, at pH 8.0 temperature not specified in the publication

758213

3.6.1.11

0.14

-

pH 7.2, 25°C, recombinant mutant D127N

687678

3.6.1.11

0.52

-

pH 7.2, 25°C, recombinant mutant H149N

687678

3.6.1.11

0.66

-

pH 7.2, 25°C, recombinant mutant H148N

687678

3.6.1.11

2.2

-

pH 7.2, 25°C, recombinant mutant N35H

687678

3.6.1.11

1150

-

pH 7.2, 25°C, recombinant wild-type enzyme

687678

3.6.1.11

1550

-

37°C, recombinant enzyme

688364

2.7.1.63

2 entries

2.7.4.1

2 entries

2.7.4.33

2 entries

3.6.1.11

6 entries

3.6.1.40

1.1

-

-

209848

7.1.3.1

3.5

-

in the presence of Zn2+, pH 7.5, 25°C

656234

K_M Value (27 results)

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Show KM Value (27 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.7.1.23

2.2

-

mutant S199A, 37°C, pH 8.0

661147

2.7.1.23

2.2

-

mutant T195A, 37°C, pH 8.0

661147

2.7.1.23

2.5

-

wild-type, 37°C, pH 8.0

661147

2.7.1.23

2.7

-

mutant G208A, 37°C, pH 8.0

661147

2.7.1.63

0.00176

-

at pH 7.5 and 28°C

739015

2.7.1.63

0.004

-

at pH 7.7 and 28°C

737862

2.7.1.63

0.175

-

pH 8.5, 37°C, in terms of acid-labile phosphate

641743

2.7.4.1

0.035

-

pH 7.5, 37°C, guanosine 5'-tetraphosphate synthesis

645129

2.7.4.1

1

-

-

645117

2.7.4.1

15

-

-

671494

2.7.4.1

15

-

pH 7.2, 30°C, recombinant wild-type enzyme

671494

2.7.4.33

0.0008

-

pH and temperature not specified in the publication, polyphosphate with an average chain length of 35 phosphate groups

719681

2.7.4.33

0.025

-

wild type enzyme, with GMP as cosubstrate, at pH 8.0 temperature not specified in the publication

758213

2.7.4.33

0.062

-

wild type enzyme, with AMP as cosubstrate, at pH 8.0 temperature not specified in the publication

758213

2.7.1.23

4 entries

2.7.1.63

3 entries

2.7.4.1

4 entries

2.7.4.33

3 entries

3.1.3.2

0.378

-

pH 4.8, 37°C

653439

3.1.3.26

3.3

-

-

653518

3.1.3.8

3.3

-

-

653518

3.6.1.11

0.0035

-

208 phosphate residues, pH 7.2

667765

3.6.1.11

0.075

-

15 phosphate residues, pH 7.2

667765

3.6.1.11

1.1

-

3 phosphate residues, pH 7.2

667765

3.6.1.11

5

-

pH 7.2, 25°C, recombinant wild-type enzyme

687678

3.6.1.11

6

-

pH 7.2, 25°C, recombinant mutant H149N

687678

3.6.1.11

7.5

-

pH 7.2, 25°C, recombinant mutant H148N

687678

3.6.1.11

9

-

pH 7.2, 25°C, recombinant mutant N35H

687678

3.6.1.11

12

-

pH 7.2, 25°C, recombinant mutant D127N

687678

3.6.1.11

8 entries

3.6.1.40

0.0000005

-

-

209848

7.1.3.1

0.014

-

in the presence of Zn2+, pH 7.5, 25°C

656234

References & Links

Literature References (150)

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Show Reference (150 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4943

7872790

Properties of fructose-1,6-bisphosphate aldolase from Escherichia coli: an NMR analysis

1995

Szwergold, B.S.; Ugurbil, K.; Brown, T.R.

Arch. Biochem. Biophys.

317

244-252

209833

-

Enzymatic breakdown of polymetaphosphate V. Purification and specificity of the enzyme

1952

Malmgren, H.

Acta Chem. Scand.

6

16-26

209834

-

The enzymes of polyphosphate metabolism in vesicular-arbuscular mycorrhizas

1982

Capaccio, L.C.M.; Callow, J.A.

New Phytol.

91

81-91

209835

-

The study of polyphosphate depolymerase activity of Neurospora crassa

1971

Kritsky, M.S.; Chernyshova, E.K.

React. Mech. Control Prop. Phosphotransferases, Int. Symp. Meeting, Akad. Verl. Berlin

-

49-56

209836

8396361

Determination of endopolyphosphatase using polyphosphate glucokinase

1993

Kowalczyk, T.H.; Phillips, N.F.B.

Anal. Biochem.

212

194-205

209837

8900207

Endopolyphosphatase for long chain inorganic polyphosphate in yeast and mammals

1996

Kumble, K.; Kornberg, A.

J. Biol. Chem.

271

27146-27151

209844

8380170

An exopolyphosphatase of Escherichia coli. The enzyme and its ppx gene in a polyphosphate operon

1993

Akiyama, M.; Crooke, E.; Kornberg, A.

J. Biol. Chem.

268

633-639

209848

8394006

Guanosine pentaphosphate phosphohydrolase of Escherichia coli is a long-chain exopolyphosphatase

1993

Keasling, J.D.; Bertsch, L.; Kornberg, A.

Proc. Natl. Acad. Sci. USA

90

7029-7033

636868

1917862

Purification and partial characterization of Cob(I)alamin adenosyltransferase from Pseudomonas denitrificans

1991

Debussche, L.; Couder, M.; Thibaut, D.; Cameron, B.; Crouzet, J.; Blanche, F.

J. Bacteriol.

173

6300-6302

641186

12897004

Allosteric regulation of Bacillus subtilis NAD kinase by quinolinic acid

2003

Garavaglia, S.; Galizzi, A.; Rizzi, M.

J. Bacteriol.

185

4844-4850

641187

11526331

Crystallization and preliminary X-ray analysis of NAD kinase from Mycobacterium tuberculosis H37Rv

2001

Mori, S.; Kawai, S.; Mikami, B.; Murata, K.

Acta Crystallogr. Sect. D

57

1319-1320

641191

12951510

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Appl. Microbiol. Biotechnol.

93

1109-1117

721387

22218771

Simultaneous removal of phosphorus and nitrogen in a sequencing batch biofilm reactor with transgenic bacteria expressing polyphosphate kinase

2012

Du, H.; Yang, L.; Wu, J.; Xiao, L.; Wang, X.; Jiang, L.

Appl. Microbiol. Biotechnol.

96

265-272

721876

22878192

Mevalonate-dependent enzymatic synthesis of amorphadiene driven by an ATP-regeneration system using polyphosphate kinase

2012

Shimane, M.; Sugai, Y.; Kainuma, R.; Natsume, M.; Kawaide, H.

Biosci. Biotechnol. Biochem.

76

1558-1560

722134

22112830

Improved hydrogen production under microaerophilic conditions by overexpression of polyphosphate kinase in Enterobacter aerogenes

2011

Lu, Y.; Zhang, C.; Lai, Q.; Zhao, H.; Xing, X.H.

Enzyme Microb. Technol.

48

187-192

722321

22393893

Polyphosphate kinase 1 is required for the pathogenesis process of meningitic Escherichia coli K1 (RS218)

2012

Peng, L.; Luo, W.Y.; Zhao, T.; Wan, C.S.; Jiang, Y.; Chi, F.; Zhao, W.; Cao, H.; Huang, S.H.

Future Microbiol.

7

411-423

722867

-

Alteration of energy metabolism in Enterobacter aerogenes by external addition of pyrophosphates and overexpression of polyphosphate kinase for enhanced hydrogen production

2012

Lu, Y.; Lai, Q.; Zhang, C.; Zhao, H.; Xing, X.

J. Chem. Technol. Biotechnol.

87

996-1003

723523

21179463

Polyphosphate kinase from M. tuberculosis: an interconnect between the genetic and biochemical role

2010

Jagannathan, V.; Kaur, P.; Datta, S.

PLoS ONE

5

e14336

723545

22110640

Amino acids involved in polyphosphate synthesis and its mobilization are distinct in polyphosphate kinase-1 from Mycobacterium tuberculosis

2011

Mittal, P.; Karthikeyan, S.; Chakraborti, P.K.

PLoS ONE

6

e27398

723676

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Feasibility of thermophilic adenosine triphosphate-regeneration system using Thermus thermophilus polyphosphate kinase

2011

Restiawaty, E.; Iwasa, Y.; Maya, S.; Honda, K.; Omasa, T.; Hirota, R.; Kuroda, A.; Ohtake, H.

Process Biochem.

46

1747-1752

737499

24532069

A new subfamily of polyphosphate kinase 2 (class III PPK2) catalyzes both nucleoside monophosphate phosphorylation and nucleoside diphosphate phosphorylation

2014

Motomura, K.; Hirota, R.; Okada, M.; Ikeda, T.; Ishida, T.; Kuroda, A.

Appl. Environ. Microbiol.

80

2602-2608

737506

26407880

Formation of polyphosphate by polyphosphate kinases and its relationship to poly(3-hydroxybutyrate) accumulation in Ralstonia eutropha strain H16

2015

Tumlirsch, T.; Sznajder, A.; Jendrossek, D.

Appl. Environ. Microbiol.

81

8277-8293

737557

25978980

Biochemistry and regulatory functions of bacterial glucose kinases

2015

Romero-Rodríguez, A.; Ruiz-Villafan, B.; Rocha-Mendoza, D.; Manzo-Ruiz, M.; Sanchez, S.

Arch. Biochem. Biophys.

577-578

1-10

737862

24200789

Characterization of polyphosphate glucokinase SCO5059 from Streptomyces coelicolor A3(2)

2013

Koide, M.; Miyanaga, A.; Kudo, F.; Eguchi, T.

Biosci. Biotechnol. Biochem.

77

2322-2324

737886

26582818

Biochemical and structural characterization of polyphosphate kinase 2 from the intracellular pathogen Francisella tularensis

2016

Batten, L.E.; Parnell, A.E.; Wells, N.J.; Murch, A.L.; Oyston, P.C.; Roach, P.L.

Biosci. Rep.

36

e00294

737921

24930102

Degradation of polyphosphates by polyphosphate kinases from Ruegeria pomeroyi

2014

Achbergerova, L.; Nahalka, J.

Biotechnol. Lett.

36

2029-2035

738411

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Polyphosphate kinase from Leishmania donovani amastigotes: A polyphosphate driven generator of ATP

2014

Jyoti Roy, J.; Mondal, S.; Bera, T.

Int. J. Drug Develop. Res.

6

159-164

738473

25640983

Ellagic acid derivatives from Terminalia chebula Retz. increase the susceptibility of Pseudomonas aeruginosa to stress by inhibiting polyphosphate kinase

2015

Sarabhai, S.; Harjai, K.; Sharma, P.; Capalash, N.

J. Appl. Microbiol.

118

817-825

738966

26233310

Involvement of polyphosphate kinase in virulence and stress tolerance of uropathogenic Proteus mirabilis

2016

Peng, L.; Jiang, Q.; Pan, J.; Deng, C.; Yu, J.; Wu, X.; Huang, S.; Deng, X.

Med. Microbiol. Immunol.

205

97-109

739001

25541179

Polyphosphate kinase of Lysinibacillus sphaericus and its effects on accumulation of polyphosphate and bacterial growth

2015

Shi, T.; Ge, Y.; Zhao, N.; Hu, X.; Yuan, Z.

Microbiol. Res.

172

41-47

739015

25320362

All1371 is a polyphosphate-dependent glucokinase in Anabaena sp. PCC 7120

2014

Klemke, F.; Beyer, G.; Sawade, L.; Saitov, A.; Korte, T.; Maldener, I.; Lockau, W.; Nuernberg, D.J.; Volkmer, T.

Microbiology

160

2807-2819

753067

28069606

Proteolytic properties of single-chain factor XII a mechanism for triggering contact activation

2017

Ivanov, I.; Matafonov, A.; Sun, M.F.; Cheng, Q.; Dickeson, S.K.; Verhamme, I.M.; Emsley, J.; Gailani, D.

Blood

129

1527-1537

753351

28604413

Single-chain factor XII a new form of activated factor XII

2017

Ivanov, I.; Matafonov, A.; Gailani, D.

Curr. Opin. Hematol.

24

411-418

756630

26576296

Pseudomonas aeruginosa exopolyphosphatase is also a polyphosphate ADP phosphotransferase

2015

Beassoni, P.R.; Gallarato, L.A.; Boetsch, C.; Garrido, M.N.; Lisa, A.T.

Enzyme Res.

2015

404607

757172

26828065

A novel inositol pyrophosphate phosphatase in Saccharomyces cerevisiae Siw14 protein selectively cleaves the beta-phosphate from 5-diphosphoinositol pentakisphosphate (5PP-IP5)

2016

Steidle, E.A.; Chong, L.S.; Wu, M.; Crooke, E.; Fiedler, D.; Resnick, A.C.; Rolfes, R.J.

J. Biol. Chem.

291

6772-6783

758213

19001261

Polyphosphate-dependent synthesis of ATP and ADP by the family-2 polyphosphate kinases in bacteria

2008

Nocek, B.; Kochinyan, S.; Proudfoot, M.; Brown, G.; Evdokimova, E.; Osipiuk, J.; Edwards, A.; Savchenko, A.; Joachimiaka, A.; Yakunin, A.

Proc. Natl. Acad. Sci. USA

105

17730-17735

760249

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Structural insights into substrate selectivity and activity of bacterial polyphosphate kinases

2018

Nocek, B.; Khusnutdinova, A.; Ruszkowski, M.; Flick, R.; Burda, M.; Batyrova, K.; Brown, G.; Mucha, A.; Joachimiak, A.; Berlicki, L.; Yakunin, A.

ACS Catal.

8

10746-10760

760384

24532069

A new subfamily of polyphosphate kinase 2 (class III PPK2) catalyzes both nucleoside monophosphate phosphorylation and nucleoside diphosphate phosphorylation

2014

Motomura, K.; Hirota, R.; Okada, M.; Ikeda, T.; Ishida, T.; Kuroda, A.

Appl. Environ. Microbiol.

80

2602-2608

760392

29884753

Coevolution of both Thermostability and activity of polyphosphate glucokinase from Thermobifida fusca YX

2018

Zhou, W.; Huang, R.; Zhu, Z.; Zhang, Y.P.J.

Appl. Environ. Microbiol.

84

e01224-18

760406

28417169

Rational design of substrate binding pockets in polyphosphate kinase for use in cost-effective ATP-dependent cascade reactions

2017

Cao, H.; Nie, K.; Li, C.; Xu, H.; Wang, F.; Tan, T.; Liu, L.

Appl. Microbiol. Biotechnol.

101

5325-5332

760742

26582818

Biochemical and structural characterization of polyphosphate kinase 2 from the intracellular pathogen Francisella tularensis

2016

Batten, L.; Parnell, A.; Wells, N.; Murch, A.; Oyston, P.; Roach, P.

Biosci. Rep.

36

e00294

760795

32847519

Rice EARLY SENESCENCE 2, encoding an inositol polyphosphate kinase, is involved in leaf senescence

2020

Yang, S.; Fang, G.; Zhang, A.; Ruan, B.; Jiang, H.; Ding, S.; Liu, C.; Zhang, Y.; Jaha, N.; Hu, P.; Xu, Z.; Gao, Z.; Wang, J.; Qian, Q.

BMC Plant Biol.

20

393

760941

29127456

Catalytic activity profile of polyphosphate kinase 1 from Myxococcus xanthus

2018

Kamatani, S.; Takegawa, K.; Kimura, Y.

Curr. Microbiol.

75

379-385

761394

29311274

Mutations in Escherichia coli polyphosphate kinase that lead to dramatically increased in vivo polyphosphate levels

2018

Rudat, A.K.; Pokhrel, A.; Green, T.J.; Gray, M.J.

J. Bacteriol.

200

e00697-17

761859

30769875

ATP-and polyphosphate-dependent glucokinases from aerobic methanotrophs

2019

Reshetnikov, A.; Solntseva, N.; Rozova, O.; Mustakhimov, I.; Trotsenko, Y.; Khmelenina, V.

Microorganisms

7

52

761883

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Mechanistic and kinetics elucidation of Mg2+/ATP molar ratio effect on glycerol kinase

2018

Molla, G.; Himmelspach, A.; Wohlgemuth, R.; Haupt, E.; Liese, A.

Mol. Catal.

445

36-42

761927

19843229

Polyphosphate kinase 2 a modulator of nucleoside diphosphate kinase activity in mycobacteria

2009

Sureka, K.; Sanyal, S.; Basu, J.; Kundu, M.

Mol. Microbiol.

74

1187-1197

762301

12486232

A polyphosphate kinase (PPK2) widely conserved in bacteria

2002

Zhang, H.; Ishige, K.; Kornberg, A.

Proc. Natl. Acad. Sci. USA

99

16678-16683

762302

12482933

Polyphosphate kinase (PPK2), a potent, polyphosphate-driven generator of GTP

2002

Ishige, K.; Zhang, H.; Kornberg, A.

Proc. Natl. Acad. Sci. USA

99

16684-16688

762661

32500270

A universal polyphosphate kinase PPK2c of Ralstonia eutropha accepts purine and pyrimidine nucleotides including uridine diphosphate

2020

Hildenbrand, J.C.; Teleki, A.; Jendrossek, D.

Appl. Microbiol. Biotechnol.

104

6659-6667

Links to other databases for Polyphosphate

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