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Ligand O-phosphoethanolamine

Basic Ligand Information

Molecular Structure

Related pathways

Pathway Source

Pathways

BRENDA

phosphatidylethanolamine bioynthesis, sphingosine metabolism

KEGG

Cationic antimicrobial peptide (CAMP) resistance, Glycerophospholipid metabolism, Glycosylphosphatidylinositol (GPI)-anchor biosynthesis, Sphingolipid metabolism, Sphingolipid signaling pathway

MetaCyc

ceramide and sphingolipid recycling and degradation (yeast), ceramide degradation (generic), choline biosynthesis I, phosphatidylcholine biosynthesis II, phosphatidylcholine biosynthesis III, phosphatidylcholine biosynthesis IV, phosphatidylethanolamine biosynthesis II, plasmalogen biosynthesis I (aerobic), plasmalogen degradation, sphingosine and sphingosine-1-phosphate metabolism more

Show all BRENDA pathways known for O-phosphoethanolamine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Natural Substrate (8 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.103

S-adenosyl-L-methionine + ethanolamine phosphate = S-adenosyl-L-homocysteine + N-methylethanolamine phosphate

485058, 485053, 485054, 485055, 485062, 485052, 485060, 485056, 485057, 485059, 485061, 660128, 659452, 671898, 674611, 733477, 734005, 734288, 735175, 735267, 777484, 778445, 778514, 776433

-

2.1.1.103

S-adenosyl-L-methionine + phosphoethanolamine = S-adenosyl-L-homocysteine + methylethanolamine phosphate

698812, 671898, 697676, 698872, 700120

-

2.1.1.103

2 entries

2.7.7.14

CTP + ethanolamine phosphate = diphosphate + CDP-ethanolamine

642882, 642883, 642884, 642887, 642881, 642886, 642885, 642888, 660968, 660979, 675978, 676425, 721549, 722415

-

3.1.3.75

O-phosphoethanolamine + H2O = ethanolamine + phosphate

654549, 664211, 664697, 751225

-

3.1.3.75

phosphoethanolamine + H2O = ethanolamine + phosphate

714872, 714360, 714357, 715704

-

4.2.3.2

ethanolamine phosphate + H2O = acetaldehyde + NH3 + phosphate

747739, 768346, 771385, 772879

-

4.2.3.2

ethanolamine phosphate = ?

137598

-

3.1.3.75

2 entries

4.2.3.2

2 entries

7.6.2.1

ATP + H2O + phosphoethanolamine/in = ADP + phosphate + phosphoethanolamine/out

685132

-

In Vivo Product in Enzyme-catalyzed Reactions (11 results)

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Show Natural Product (11 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.32

ethanolamine + ATP = O-phosphoethanolamine + ADP

-

-

2.7.1.82

ATP + ethanolamine = ADP + O-phosphoethanolamine

-

-

3.1.4.12

phosphatidylethanolamine + H2O = diacylglycerol + ethanolamine phosphate

649984

-

3.1.4.3

phosphatidylethanolamine + H2O = 1,2-diacyl-sn-glycerol + phosphoethanolamine

-

-

3.1.4.3

phosphatidylethanolamine + H2O = 1,2-sn-diacylglycerol + phosphoethanolamine

-

-

3.1.4.62

a phosphatidylethanolamine + H2O = a 1,2-diacyl-sn-glycerol + O-phosphoethanolamine

-

-

3.1.4.62

phosphatidylethanolamine + H2O = 1,2-diacyl-sn-glycerol + O-phosphoethanolamine

-

-

3.1.4.3

2 entries

3.1.4.62

2 entries

4.1.1.81

L-serine O-3-phosphate = ethanolamine-phosphate + CO2

-

-

4.1.2.27

sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde

-

-

4.1.2.27

sphingosine 1-phosphate = phosphoethanolamine + palmitaldehyde

650944

-

4.1.2.27

2 entries

7.6.2.1

ATP + H2O + phosphoethanolamine/in = ADP + phosphate + phosphoethanolamine/out

-

-

Substrate in Enzyme-catalyzed Reactions (24 results)

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Show Substrate (24 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.103

ethanolamine phosphate + S-adenosyl-L-methionine = N-methylethanolamine phosphate + S-adenosyl-L-homocysteine

758051, 757185

-

2.1.1.103

S-adenosyl-L-methionine + ethanolamine phosphate = S-adenosyl-L-homocysteine + N-methylethanolamine phosphate

485058, 485053, 485054, 485055, 485062, 485052, 485060, 485056, 485057, 485059, 485061, 660128, 659452, 663227, 671898, 674611, 698812, 733477, 734005, 734288, 735175, 735267, 755953, 758529, 777484, 778445, 778514, 776433

-

2.1.1.103

3 S-adenosyl-L-methionine + phosphoethanolamine = 3 S-adenosyl-L-homocysteine + phosphocholine

719167, 719039, 719978, 720011

-

2.1.1.103

S-adenosyl-L-methionine + phosphoethanolamine = S-adenosyl-L-homocysteine + methylethanolamine phosphate

698812, 671898, 697676, 698872, 700120

-

2.1.1.103

S-adenosyl-L-methionine + phosphoethanolamine = S-adenosyl-L-homocysteine + N-methylethanolamine phosphate

755953

-

2.1.1.103

S-adenosyl-L-methionine + phosphoethanolamine = S-adenosyl-L-homocysteine + phosphomonomethylethanolamine

719978, 720011

-

2.1.1.103

6 entries

2.7.7.103

CTP + ethanolamine phosphate = diphosphate + CDP-ethanolamine

760601

-

2.7.7.14

CTP + ethanolamine phosphate = CDP-ethanolamine + diphosphate

702465, 703850, 705786, 704542, 737597

-

2.7.7.14

CTP + ethanolamine phosphate = diphosphate + CDP-ethanolamine

642881, 642886, 642882, 642883, 642884, 642885, 642887, 642888, 660968, 660979, 675978, 676425, 671816, 693518, 693090, 693508, 721549, 722415

-

2.7.7.14

dCTP + ethanolamine phosphate = diphosphate + dCDP-ethanolamine

642886, 722415

-

2.7.7.14

3 entries

2.7.7.15

CTP + ethanolamine phosphate = diphosphate + CDPethanolamine

642907, 642922

-

3.1.3.1

O-phosphoethanolamine + H2O = ethanolamine + phosphate

772802

-

3.1.3.1

phosphoethanolamine + H2O = phosphate + ethanolamine

94572, 94573, 94616, 94613, 94607

-

3.1.3.2

O-phosphoethanolamine + H2O = ethanolamine + phosphate

134712, 134740, 134752, 134754

-

3.1.3.2

phosphorylethanolamine + H2O = ethanolamine + phosphate

666338

-

3.1.3.1

2 entries

3.1.3.2

2 entries

3.1.3.39

ethanolamine phosphate + H2O = ?

134853

-

3.1.3.75

O-phosphoethanolamine + H2O = ethanolamine + phosphate

654549, 664211, 664697, 680993, 751225, 771625, 775114, 775143

-

3.1.3.75

phosphoethanolamine + H2O = ethanolamine + phosphate

714872, 714360, 714357, 715704

-

3.1.3.75

2 entries

3.6.1.1

2-phosphorylethanolamine + H2O = ethanolamine + phosphate

718979

-

4.2.3.2

ethanolamine phosphate + H2O = acetaldehyde + NH3 + phosphate

137597, 137599, 137598, 747739, 768346, 771385, 772879

-

4.2.3.2

ethanolamine phosphate = ?

137598

-

4.2.3.2

2 entries

6.3.1.10

ATP + ethanolamine phosphate = norcobalamin + ?

674341

-

7.5.2.6

ATP + H2O + phosphoethanolamine[side 1] = ADP + phosphate + phosphoethanolamine[side 2]

749842

-

7.6.2.1

ATP + H2O + phosphoethanolamine/in = ADP + phosphate + phosphoethanolamine/out

685132

-

Product in Enzyme-catalyzed Reactions (50 results)

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Show Product (50 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.32

2-aminoethanol + ATP = ADP + 2-aminoethyl phosphate

-

-

2.7.1.32

ATP + ethanolamine = ADP + ethanolamine phosphate

-

-

2.7.1.32

ethanolamine + ATP = ADP + ethanolamine phosphate

-

-

2.7.1.32

ATP + ethanolamine = ADP + O-phosphoethanolamine

-

-

2.7.1.32

ethanolamine + ATP = O-phosphoethanolamine + ADP

-

-

2.7.1.32

ATP + ethanolamine = ADP + phosphoethanolamine

-

-

2.7.1.32

ethanolamine + ATP = phosphoethanolamine + ADP

-

-

2.7.1.82

ATP + ethanolamine = ADP + O-phosphoethanolamine

137599, -

-

2.7.1.82

GTP + ethanolamine = GDP + O-phosphoethanolamine

-

-

2.7.1.82

ITP + ethanolamine = IDP + O-phosphoethanolamine

-

-

3.1.4.12

phosphatidylethanolamine + H2O = diacylglycerol + ethanolamine phosphate

649984

-

3.1.4.12

CDP-ethanolamine + H2O = CMP + phosphoethanolamine

-

-

3.1.4.12

phosphatidylethanolamine + H2O = diacylglycerol + phosphorylethanolamine

-

-

3.1.4.13

D-serine-phosphoethanolamine + H2O = D-serine + ethanolamine phosphate

81109

-

3.1.4.13

L-serine-phosphoethanolamine + H2O = L-serine + ethanolamine phosphate

81109, 81110

-

3.1.4.13

L-threonine-phosphoethanolamine + H2O = L-threonine + ethanolamine phosphate

81109

-

3.1.4.3

phosphatidylethanolamine + H2O = 1,2-diacyl-sn-glycerol + ethanolamine phosphate

-

-

3.1.4.3

1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + H2O = 1,2-dihexanoyl-sn-glycerol + phosphoethanolamine

649967, -

-

3.1.4.3

1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + H2O = 1,2-dioleoyl-sn-glycerol + phosphoethanolamine

-

-

3.1.4.3

phosphatidylethanolamine + H2O = 1,2-diacyl-sn-glycerol + phosphoethanolamine

-

-

3.1.4.3

phosphatidylethanolamine + H2O = 1,2-sn-diacylglycerol + phosphoethanolamine

-

-

3.1.4.3

1,2-dioleoylphosphatidylethanolamine + H2O = 1,2-dioleoylglycerol + phosphorylethanolamine

135289

-

3.1.4.3

1,2-dipalmitoylphosphatidylethanolamine + H2O = 1,2-dipalmitoylglycerol + phosphorylethanolamine

135304

-

3.1.4.3

ceramide phosphorylethanolamine = N-acylsphingosine + phosphorylethanolamine

135298

-

3.1.4.3

phosphatidylethanolamine + H2O = phosphorylethanolamine + 1,2-diacylglycerol

-

-

3.1.4.3

phosphatidylethanolamine + H2O = phosphorylethanolamine + diacylglycerol

135301, 135289, 135286, 133931, 135299, 135304, 135308, 135298, 135292, 135305, 135306, 135307, -

-

2.7.1.32

7 entries

2.7.1.82

3 entries

3.1.4.12

3 entries

3.1.4.13

3 entries

3.1.4.3

10 entries

3.1.4.38

sn-glycerol-3-phosphoethanolamine + H2O = glycerol + phosphoethanolamine

-

-

3.1.4.62

1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine + H2O = 1-palmitoyl-2-oleoyl-sn-glycerol + O-phosphoethanolamine

-

-

3.1.4.62

a phosphatidylethanolamine + H2O = a 1,2-diacyl-sn-glycerol + O-phosphoethanolamine

-

-

3.1.4.62

NBD-phosphatidylethanolamine + H2O = NBD-1,2-diacyl-sn-glycerol + O-phosphoethanolamine

-

-

3.1.4.62

phosphatidylethanolamine + H2O = 1,2-diacyl-sn-glycerol + O-phosphoethanolamine

-

-

3.1.4.62

4 entries

3.6.1.13

CDP-ethanolamine + H2O = CMP + ethanolamine phosphate

-

-

3.6.1.53

CDP-ethanolamine + H2O = CMP + phosphoethanolamine

-

-

4.1.1.81

L-serine O-3-phosphate = ethanolamine-phosphate + CO2

-

-

4.1.2.27

4,4-difluoro-4-bora-3a,4a-diaza-s-indacene-labeled sphinganine 1-phosphate = phosphoethanolamine + 4,4-difluoro-4-bora-3a,4a-diaza-s-indacene-labeled palmitaldehyde

-

-

4.1.2.27

4D-Hydroxysphinganine 1-phosphate = Phosphoethanolamine + 2-hydroxyhexadecanal

5112, 5116

-

4.1.2.27

7-nitrobenz-2-oxa-1,3-diazole-sphingosine 1-phosphate = phosphoethanolamine + 7-nitrobenz-2-oxa-1,3-diazole-hexadec-2-enal

-

-

4.1.2.27

boron dipyrromethene difluoride-sphingosine 1-phosphate = phosphoethanolamine + boron dipyrromethene difluoride-hexadec-2-enal

-

-

4.1.2.27

C17-sphinganine-1-phosphate = phosphoethanolamine + pentadecanal

-

-

4.1.2.27

D-(+)-erythro-sphingosine 1-phosphate = phosphoethanolamine + (2E)-hexadecenal

-

-

4.1.2.27

dihydrosphingosine 1-phosphate = phosphoethanolamine + palmitaldehyde

-

-

4.1.2.27

omega-(7-nitro-2-1,3-benzoxadiazol-4-yl)-D-erythro-sphingosine 1-phosphate = phosphoethanolamine + omega-(7-nitro-2-1,3-benzoxadiazol-4-yl)-D-erythro-(2E)-hexadecenal

-

-

4.1.2.27

sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde

652375, 650324, 5116, 653122, 5113, 5117, 5118, 5121, 5122, 5112, 5114, -

-

4.1.2.27

sphingosine 1-phosphate = phosphoethanolamine + (2E)-hexadecenal

-

-

4.1.2.27

sphingosine 1-phosphate = phosphoethanolamine + hexadecanal

650944

-

4.1.2.27

sphingosine 1-phosphate = phosphoethanolamine + palmitaldehyde

652518, 5119, 5116, 650944, -

-

4.1.2.27

sphingosine-1-phosphate = phosphoethanolamine + (2E)-hexadecenal

-

-

4.1.2.27

umbelliferone-labled sphinganine 1-phosphate = phosphoethanolamine + 3-[(2-oxo-2H-chromen-7-yl)oxy]propanal

-

-

4.1.2.27

14 entries

7.5.2.6

ATP + H2O + phosphoethanolamine[side 1] = ADP + phosphate + phosphoethanolamine[side 2]

-

-

7.6.2.1

ATP + H2O + phosphoethanolamine/in = ADP + phosphate + phosphoethanolamine/out

-

-

Inhibitor in Enzyme-catalyzed Reactions (6 results)

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Show Inhibitors (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.82

-

641347

-

2.7.1.82

-

641350, 642036

-

2.7.1.82

not

642038

-

2.7.1.82

3 entries

2.7.7.15

competitive to phosphocholine

642907

-

3.1.3.2

substrate inhibition

666338

-

6.3.2.11

weak

989

-

3D Structure of Enzyme-Ligand-Complex (PDB) (35 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (35 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.3.5.1

8BQS, 3D-view

1.6.5.3

8BQS, 3D-view

2.4.1.182

8BQS, 3D-view

2.7.11.1

2R7B, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

8IJR, 3D-view

2.7.8.27

8W9W, 3D-view

2.7.8.27

30 entries

7.1.1.2

8BQS, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (26 results)

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Show Turnover Number (26 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.1.1.103

0.005

-

mutant enzyme D128N, at pH 8.0 and 20°C

734288

2.1.1.103

0.022

-

mutant enzyme D128A, at pH 8.0 and 20°C

734288

2.1.1.103

0.052

-

-

671898

2.1.1.103

0.09

-

pH 8.0, temperature not specified in the publication

757185

2.1.1.103

0.21

-

pH 8.0, temperature not specified in the publication

757185

2.1.1.103

0.27

-

pH 8.0, temperature not specified in the publication

757185

2.1.1.103

1.82

-

wild type enzyme, at pH 8.0 and 20°C

734288

2.1.1.103

1.82

-

pH and temperature not specified in the publication

720011

2.1.1.103

3.238

-

pH 7.8, 22°C, recombinant His-tagged enzyme

776433

2.1.1.103

5.58

-

pH 7.8, 22°C, recombinant His-tagged enzyme

776433

2.1.1.103

8.63

-

isozyme PMT1, in 0.1 M HEPES (pH 8.0), 2 mM Na2EDTA, 10% glycerol, at 25°C

719978

2.1.1.103

10.412

-

pH 7.8, 22°C, recombinant His-tagged enzyme

776433

2.1.1.103

16.11

-

pH 7.8, 22°C, recombinant His-tagged enzyme

776433

2.1.1.103

17.77

-

pH 7.8, 22°C, recombinant His-tagged enzyme

776433

2.1.1.103

117.85

-

pH 7.8, 22°C, recombinant His-tagged enzyme

776433

2.7.7.14

0.016

-

mutant H38A, pH 7.7, 37°C

737597

2.7.7.14

0.23

-

mutant H226A, pH 7.7, 37°C

737597

2.7.7.14

0.25

-

wild-type, pH 7.7, 37°C

737597

2.7.7.14

0.26

-

mutant H229A, pH 7.7, 37°C

737597

2.7.7.14

3.4

-

pH 8.0, 37°C, recombinant His-tagged wild-type enzyme

721549

2.7.7.14

4.1

-

pH 8.0, 37°C, recombinant His-tagged mutant H422A enzyme

721549

3.1.3.75

2.27

-

pH 6.7, 37°C, 2 mM Mg2+

654549

3.1.3.75

13

-

50 mM Hepes/NaOH buffer, pH 7.0, 37°C

714360

4.2.3.2

0.9

-

at pH 6.0 and 30°C

747739

4.2.3.2

1.2

-

at pH 7.4 and 30°C

747739

4.2.3.2

2.3

-

at pH 8.0 and 30°C

747739

2.1.1.103

15 entries

2.7.7.14

6 entries

3.1.3.75

2 entries

4.2.3.2

3 entries

K_M Value (60 results)

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Show KM Value (60 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.1.1.103

0.0099

-

-

671898

2.1.1.103

0.0217

-

pH 8.0, 30°C

755953

2.1.1.103

0.0217

-

at pH 8.0 and 30°C

755953

2.1.1.103

0.0292

-

pH 8.0, 30°C

755953

2.1.1.103

0.0292

-

at pH 8.0 and 30°C

755953

2.1.1.103

0.054

-

wild type enzyme, at pH 8.0 and 20°C

734288

2.1.1.103

0.0542

-

pH and temperature not specified in the publication

720011

2.1.1.103

0.062

-

pH 8.0, temperature not specified in the publication, wild-type enzyme

778514

2.1.1.103

0.065

-

-

485061

2.1.1.103

0.0661

-

-

698872

2.1.1.103

0.07337

-

pH 7.8, 22°C, recombinant His-tagged enzyme

776433

2.1.1.103

0.079

-

pH 8.6, 37°C

663227

2.1.1.103

0.08097

-

pH 7.8, 22°C, recombinant His-tagged enzyme

776433

2.1.1.103

0.085

-

pH 7.8, 22°C, recombinant His-tagged enzyme

776433

2.1.1.103

0.094

-

pH 8.0, temperature not specified in the publication, mutant S160A

778514

2.1.1.103

0.096

-

-

485056

2.1.1.103

0.09993

-

pH 7.8, 22°C, recombinant His-tagged enzyme

776433

2.1.1.103

0.1

-

at pH 8.6 and 37°C

735267

2.1.1.103

0.106

-

isozyme PMT1, in 0.1 M HEPES (pH 8.0), 2 mM Na2EDTA, 10% glycerol, at 25°C

719978

2.1.1.103

0.133

-

pH 8.0, temperature not specified in the publication, mutant Y127F

778514

2.1.1.103

0.148

-

pH 8.0, temperature not specified in the publication, mutant S155A

778514

2.1.1.103

0.156

-

pH 8.0, temperature not specified in the publication

757185

2.1.1.103

0.21

-

at pH 8.6 and 37°C

735267

2.1.1.103

0.284

-

pH 8.0, temperature not specified in the publication

757185

2.1.1.103

0.308

-

pH 7.8, 22°C, recombinant His-tagged enzyme

776433

2.1.1.103

0.315

-

pH 8.0, temperature not specified in the publication, mutant T178V

778514

2.1.1.103

0.408

-

pH 8.0, temperature not specified in the publication

757185

2.1.1.103

0.5

2

pH 8.0, temperature not specified in the publication, mutant H170A

778514

2.1.1.103

0.623

-

pH 8.0, temperature not specified in the publication, mutant M126I

778514

2.1.1.103

1.079

-

pH 7.8, 22°C, recombinant His-tagged enzyme

776433

2.1.1.103

7.99

-

mutant enzyme D128A, at pH 8.0 and 20°C

734288

2.1.1.103

21.17

-

mutant enzyme D128N, at pH 8.0 and 20°C

734288

2.7.7.14

0.01209

-

-

705786

2.7.7.14

0.053

-

-

671816

2.7.7.14

0.065

-

-

642886

2.7.7.14

0.065

-

pH 7.8, 37°C

642881

2.7.7.14

0.072

-

pH 7.8, 37°C

642887

2.7.7.14

0.1403

-

isozyme Pcyt2beta, at 37°C

693508

2.7.7.14

0.179

-

wild-type, pH 7.7, 37°C

737597

2.7.7.14

0.275

-

mutant H226A, pH 7.7, 37°C

737597

2.7.7.14

0.301

-

mutant H229A, pH 7.7, 37°C

737597

2.7.7.14

0.3184

-

isozyme Pcyt2alpha, at 37°C

693508

2.7.7.14

0.373

-

pH 8.0, 37°C, native enzyme

721549

2.7.7.14

0.452

-

pH 8.0, 37°C, recombinant His-tagged wild-type enzyme

721549

2.7.7.14

0.565

-

pH 8.0, 37°C, recombinant His-tagged mutant H422A enzyme

721549

2.7.7.14

0.88

-

mutant H38A, pH 7.7, 37°C

737597

2.7.7.15

1.43

-

pH 7, 37°C

642922

2.7.7.15

69.4

-

pH 7, 37°C

642907

2.1.1.103

32 entries

2.7.7.14

14 entries

2.7.7.15

2 entries

3.1.3.1

2.9

-

-

94573, 94616

3.1.3.2

0.7

-

pH 5.0, 37°C

666338

3.1.3.75

0.003

-

pH 6.7, 37°C, 2 mM Mg2+

654549

3.1.3.75

0.4

-

37°C, pH 7.0, enzyme BvPECP1S

775143

3.1.3.75

1.16

-

50 mM Hepes/NaOH buffer, pH 7.0, 37°C

714360

3.1.3.75

4.14

-

37°C, pH 7.0, enzyme BvPECP2L

775143

4.2.3.2

0.28

-

-

137599

4.2.3.2

0.32

-

-

137599

4.2.3.2

0.45

-

-

137599

4.2.3.2

0.61

-

-

137597

4.2.3.2

0.63

-

-

137597

4.2.3.2

1

-

at pH 7.4 and 30°C

747739

3.1.3.75

4 entries

4.2.3.2

6 entries

K_i Value (2 results)

top print hide

Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.7.7.15

16.7

-

pH 7, 37°C

642907

3.1.3.2

3

-

pH 5.0, 37°C

666338

References & Links

Literature References (139)

top print hide

Show Reference (139 entries)

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cDNA cloning of phosphoethanolamine N-methyltransferase from spinach by complementation in Schizosaccharomyces pombe and characterization of the recombinant enzyme

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12215503

Silencing of phosphoethanolamine N-methyltransferase results in temperature-sensitive male sterility and salt hypersensitivity in Arabidopsis

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Molecular and biochemical characterization of a cold-regulated phosphoethanolamine N-methyltransferase from wheat

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Interactions of phosphorylethanolamine analogs with phosphorylethanolamine-citidylyltransferase

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Immunological characterization, lipid dependence, and subcellular localization of CTP:phosphoethanolamine cytidylyltransferase purified from rat liver. Comparison with CTP:phosphocholine cytidylyltransferase

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642886

1323040

Ethanolamine-phosphate cytidylyltransferase

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642887

8130268

Substrate specificity of CTP: phosphoethanolamine cytidylyltransferase purified from rat liver

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642888

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NMDA receptor overactivation inhibits phospholipid synthesis by decreasing choline-ethanolamine phosphotransferase activity

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642907

1660305

Substrate specificity of CTP:phosphocholine cytidylyltransferase

1991

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335-339

642922

11466299

The licC gene of Streptococcus pneumoniae encodes a CTP:phosphocholine cytidylyltransferase

2001

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J. Bacteriol.

183

4927-4931

649967

10727235

The choline binding site of phospholipase C (Bacillus cereus): insights into substrate specificity

2000

Martin, S.F.; Follows, B.C.; Hergenrother, P.J.; Trotter, B.K.

Biochemistry

39

3410-3415

649984

10769141

Purification and characterization of neutral sphingomyelinase from Helicobacter pylori

2000

Chan, E.C.; Chang, C.C.; Li, Y.S.; Chang, C.A.; Chiou, C.C.; Wu, T.Z.

Biochemistry

39

4838-4845

650324

11018465

Human sphingosine-1-phosphate lyase: cDNA cloning, functional expression studies and mapping to chromosome 10q221

2000

Van Veldhoven, P.P.; Gijsbers, S.; Mannaerts, G.P.; Vermeesch, J.R.; Brys, V.

Biochim. Biophys. Acta

1487

128-134

650944

11566853

Sphingosine-1-phosphate lyase has a central role in the development of Dictyostelium discoideum

2001

Li, G.; Foote, C.; Alexander, S.; Alexander, H.

Development

128

3473-3483

652375

12584204

Sphingosine-1-phosphate lyase is involved in the differentiation of F9 embryonal carcinoma cells to primitive endoderm

2003

Kihara, A.; Ikeda, M.; Kariya, Y.; Lee, E.Y.; Lee, Y.M.; Igarashi, Y.

J. Biol. Chem.

278

14578-14585

652518

14570870

Sphingosine-phosphate lyase enhances stress-induced ceramide generation and apoptosis

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Reiss, U.; Oskouian, B.; Zhou, J.; Gupta, V.; Sooriyakumaran, P.; Kelly, S.; Wang, E.; Merrill, A.H., Jr.; Saba, J.D.

J. Biol. Chem.

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1281-1290

653122

10563331

Sphingosine-1-phosphate lyase

2000

Van Veldhoven, P.P.

Methods Enzymol.

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244-254

654549

15175005

Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities

2004

Roberts, S.J.; Stewart, A.J.; Sadler, P.J.; Farquharson, C.

Biochem. J.

382

59-65

659452

15664981

In vivo evidence for the specificity of Plasmodium falciparum phosphoethanolamine methyltransferase and its coupling to the Kennedy pathway

2005

Pessi, G.; Choi, J.Y.; Reynolds, J.M.; Voelker, D.R.; Mamoun, C.B.

J. Biol. Chem.

280

12461-12466

660128

15295103

The xipotl mutant of Arabidopsis reveals a critical role for phospholipid metabolism in root system development and epidermal cell integrity

2004

Cruz-Ramirez, A.; Lopez-Bucio, J.; Ramirez-Pimentel, G.; Zurita-Silva, A.; Sanchez-Calderon, L.; Ramirez-Chavez, E.; Gonzalez-Ortega, E.; Herrera-Estrella, L.

Plant Cell

16

2020-2034

660968

14759225

Control of the CDPethanolamine pathway in mammalian cells: effect of CTP:phosphoethanolamine cytidylyltransferase overexpression and the amount of intracellular diacylglycerol

2004

Bleijerveld, O.B.; Klein, W.; Vaandrager, A.B.; Helms, J.B.; Houweling, M.

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711-719

660979

15147238

Membrane lipid biosynthesis in Chlamydomonas reinhardtii: expression and characterization of CTP:phosphoethanolamine cytidylyltransferase

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Yang, W.; Mason, C.B.; Pollock, S.V.; Lavezzi, T.; Moroney, J.V.; Moore, T.S.

Biochem. J.

382

51-57

663227

15073329

A pathway for phosphatidylcholine biosynthesis in Plasmodium falciparum involving phosphoethanolamine methylation

2004

Pessi, G.; Kociubinski, G.; Mamoun, C.B.

Proc. Natl. Acad. Sci. USA

101

6206-6211

664211

16054448

Probing the substrate specificities of human PHOSPHO1 and PHOSPHO2

2005

Roberts, S.J.; Stewart, A.J.; Schmid, R.; Blindauer, C.A.; Bond, S.R.; Sadler, P.J.; Farquharson, C.

Biochim. Biophys. Acta

1752

73-82

664697

15886911

Identification, cloning, and expression of Pseudomonas aeruginosa phosphorylcholine phosphatase gene

2005

Massimelli, M.J.; Beassoni, P.R.; Forrellad, M.A.; Barra, J.L.; Garrido, M.N.; Domenech, C.E.; Lisa, A.T.

Curr. Microbiol.

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2116592

Identification of the Pseudomonas aeruginosa acid phosphatase as an phosphorylcholine phosphatase activity

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Mol. Cell. Biochem.

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17612623

Metabolic and molecular aspects of ethanolamine phospholipid biosynthesis: the role of CTP:phosphoethanolamine cytidylyltransferase (Pcyt2)

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Bakovic, M.; Fullerton, M.D.; Michel, V.

Biochem. Cell Biol.

85

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671898

17313371

Phosphoethanolamine N-methyltransferase (PMT-1) catalyzes the first reaction of a new pathway for phosphocholine biosynthesis in Caenorhabditis elegans

2007

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The CbiB protein of Salmonella enterica is an integral membrane protein involved in the last step of the de novo corrin ring biosynthetic pathway

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Zayas, C.L.; Claas, K.; Escalante-Semerena, J.C.

J. Bacteriol.

189

7697-7708

674611

16704982

Localization of the phosphoethanolamine methyltransferase of the human malaria parasite Plasmodium falciparum to the Golgi apparatus

2006

Witola, W.H.; Pessi, G.; El Bissati, K.; Reynolds, J.M.; Mamoun, C.B.

J. Biol. Chem.

281

21305-21311

675978

17325045

Developmental and metabolic effects of disruption of the mouse CTP:phosphoethanolamine cytidylyltransferase gene (Pcyt2)

2007

Fullerton, M.D.; Hakimuddin, F.; Bakovic, M.

Mol. Cell. Biol.

27

3327-3336

676425

17189343

Defects in CTP:phosphorylethanolamine cytidylyltransferase affect embryonic and postembryonic development in Arabidopsis

2006

Mizoi, J.; Nakamura, M.; Nishida, I.

Plant Cell

18

3370-3385

680993

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Functional involvement of PHOSPHO1 in matrix vesicle-mediated skeletal mineralization

2007

Roberts, S.; Narisawa, S.; Harmey, D.; Millan, J.L.; Farquharson, C.

J. Bone Miner. Res.

22

617-627

685132

17269657

ATP-dependent transport of phosphatidylserine analogues in human erythrocytes

2007

Smriti, T.; Nemergut, E.C.; Daleke, D.L.

Biochemistry

46

2249-2259

693090

18499667

Phosphatidylethanolamine is the precursor of the ethanolamine phosphoglycerol moiety bound to eukaryotic elongation factor 1A

2008

Signorell, A.; Jelk, J.; Rauch, M.; Buetikofer, P.

J. Biol. Chem.

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2007

Tie, A.; Bakovic, M.

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Stimulation of the human CTP:phosphoethanolamine cytidylyltransferase gene by early growth response protein 1

2008

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Choline induces transcriptional repression and proteasomal degradation of the malarial phosphoethanolamine methyltransferase

2007

Witola, W.H.; Ben Mamoun, C.

Eukaryot. Cell

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698812

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Disruption of the Plasmodium falciparum PfPMT gene results in a complete loss of phosphatidylcholine biosynthesis via the SDPM pathway and severe growth and survival defects

2008

Witola, W.H.; El Bissati, K.; Pessi, G.; Xie, C.; Roepe, P.D.; Ben Mamoun, C.

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283

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Biochemical and genetic analysis of the phosphoethanolamine methyltransferase of the human malaria parasite Plasmodium falciparum

2008

Reynolds, J.M.; Takebe, S.; Choi, J.Y.; El Bissati, K.; Witola, W.H.; Bobenchik, A.M.; Hoch, J.C.; Voelker, D.R.; Mamoun, C.B.

J. Biol. Chem.

283

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Cloning, characterization, and transformation of the phosphoethanolamine N-methyltransferase gene (ZmPEAMT1) in maize (Zea mays L.)

2007

Wu, S.; Yu, Z.; Wang, F.; Li, W.; Ye, C.; Li, J.; Tang, J.; Ding, J.; Zhao, J.; Wang, B.

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Low-density lipoprotein and oxysterols suppress the transcription of CTP:Phosphoethanolamine cytidylyltransferase in vitro

2010

Ando, H.; Horibata, Y.; Yamashita, S.; Oyama, T.; Sugimoto, H.

Biochim. Biophys. Acta

1801

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Regulation of the mouse CTP: phosphoethanolamine cytidylyltransferase gene Pcyt2 during myogenesis

2009

Zhu, L.; Michel, V.; Bakovic, M.

Gene

447

51-59

704542

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Elimination of the CDP-ethanolamine pathway disrupts hepatic lipid homeostasis

2009

Leonardi, R.; Frank, M.W.; Jackson, P.D.; Rock, C.O.; Jackowski, S.

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The ethanolamine branch of the Kennedy pathway is essential in the bloodstream form of Trypanosoma brucei

2009

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Mol. Microbiol.

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Site-directed mutations and kinetic studies show key residues involved in alkylammonium interactions and reveal two sites for phosphorylcholine in Pseudomonas aeruginosa phosphorylcholine phosphatase

2011

Beassoni, P.R.; Otero, L.H.; Boetsch, C.; Domenech, C.E.; Gonzalez-Nilo, F.D.; Lisa, A.T.

Biochim. Biophys. Acta

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Arabidopsis thaliana PECP1 - Enzymatic characterization and structural organization of the first plant phosphoethanolamine/phosphocholine phosphatase

2012

May, A.; Spinka, M.; Koeck, M.

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2011

Domenech, C.E.; Otero, L.H.; Beassoni, P.R.; Lisa, A.T.

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561841

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Loss of skeletal mineralization by the simultaneous ablation of PHOSPHO1 and alkaline phosphatase function: A unified model of the mechanisms of initiation of skeletal calcification

2011

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The Arabidopsis thaliana phosphate starvation responsive gene AtPPsPase1 encodes a novel type of inorganic pyrophosphatase

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Biochim. Biophys. Acta

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1H, 13C, and 15N chemical shift assignments for PfPMT, a phosphoethanolamine methyltransferase from Plasmodium falciparum

2013

Bezsonova, I.; Rujan, I.; Bobenchik, A.M.; Gorbatyuk, V.; Maciejewski, M.W.; Gorbatyuk, O.; Hao, B.; Arthanari, H.; Mamoun, C.B.; Hoch, J.C.

Biomol. NMR Assign.

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719167

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Identification of inhibitors of Plasmodium falciparum phosphoethanolamine methyltransferase using an enzyme-coupled transmethylation assay

2010

Bobenchik, A.M.; Choi, J.Y.; Mishra, A.; Rujan, I.N.; Hao, B.; Voelker, D.R.; Hoch, J.C.; Mamoun, C.B.

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Thermodynamic evaluation of ligand binding in the plant-like phosphoethanolamine methyltransferases of the parasitic nematode Haemonchus contortus

2011

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Structure and reaction mechanism of phosphoethanolamine methyltransferase from the malaria parasite Plasmodium falciparum: an antiparasitic drug target

2012

Lee, S.G.; Kim, Y.; Alpert, T.D.; Nagata, A.; Jez, J.M.

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Biochemical characterization of Plasmodium falciparum CTP:phosphoethanolamine cytidylyltransferase shows that only one of the two cytidylyltransferase domains is active

2013

Maheshwari, S.; Lavigne, M.; Contet, A.; Alberge, B.; Pihan, E.; Kocken, C.; Wengelnik, K.; Douguet, D.; Vial, H.; Cerdan, R.

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Pavlovic, Z.; Bakovic, M.

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Crystal structure of phosphoethanolamine methyltransferase from Plasmodium falciparum in complex with amodiaquine

2012

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Transcriptome-wide analysis of SAMe superfamily to novelty phosphoethanolamine N-methyltransferase copy in Lonicera japonica

2015

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Saen-Oon, S.; Lee, S.G.; Jez, J.M.; Guallar, V.

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Plasmodium falciparum phosphoethanolamine methyltransferase is essential for malaria transmission

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Bobenchik, A.M.; Witola, W.H.; Augagneur, Y.; Nic Lochlainn, L.; Garg, A.; Pachikara, N.; Choi, J.Y.; Zhao, Y.O.; Usmani-Brown, S.; Lee, A.; Adjalley, S.H.; Samanta, S.; Fidock, D.A.; Voelker, D.R.; Fikrig, E.; Ben Mamoun, C.

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Structure, function and inhibition of the phosphoethanolamine methyltransferases of the human malaria parasites Plasmodium vivax and Plasmodium knowlesi

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Human CTP:phosphoethanolamine cytidylyltransferase: enzymatic properties and unequal catalytic roles of CTP-binding motifs in two cytidylyltransferase domains

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Tian, S.; Ohtsuka, J.; Wang, S.; Nagata, K.; Tanokura, M.; Ohta, A.; Horiuchi, H.; Fukuda, R.

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Kinetic characterization of the human O-phosphoethanolamine phospho-lyase reveals unconventional features of this specialized pyridoxal phosphate-dependent lyase

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Schiroli, D.; Ronda, L.; Peracchi, A.

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Kinetic characterization of the human O-phosphoethanolamine phospho-lyase reveals unconventional features of this specialized pyridoxal phosphate-dependent lyase

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FEBS J.

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The reconstituted Escherichia coli MsbA protein displays lipid flippase activity

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Eckford, P.D.; Sharom, F.J.

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The reconstituted Escherichia coli MsbA protein displays lipid flippase activity

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Pi starvation-dependent regulation of ethanolamine metabolism by phosphoethanolamine phosphatase PECP1 in Arabidopsis roots

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J. Exp. Bot.

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Pi starvation-dependent regulation of ethanolamine metabolism by phosphoethanolamine phosphatase PECP1 in Arabidopsis roots

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Characterization of phosphoethanolamine-N-methyltransferases in green algae

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Hirashima, T.; Toyoshima, M.; Moriyama, T.; Nakamura, Y.; Sato, N.

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Conformational changes in the di-domain structure of Arabidopsis phosphoethanolamine methyltransferase leads to active-site formation

2017

Lee, S.G.; Jez, J.M.

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Loss of phosphoethanolamine N-methyltransferases abolishes phosphatidylcholine synthesis and is lethal

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Chen, W.; Taylor, M.C.; Barrow, R.A.; Croyal, M.; Masle, J.

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Chen, W.; Taylor, M.C.; Barrow, R.A.; Croyal, M.; Masle, J.

Plant Physiol.

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124-142

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Knockdown of phosphoethanolamine transmethylation enzymes decreases viability of Haemonchus contortus

2016

Witola, W.H.; Cooks-Fagbodun, S.; Ordonez, A.R.; Matthews, K.; Abugri, D.A.; McHugh, M.

Vet. Parasitol.

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Manganese-induced substrate promiscuity in the reaction catalyzed by phosphoglutamine cytidylyltransferase from Campylobacter jejuni

2019

Taylor, Z.W.; Raushel, F.M.

Biochemistry

58

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Manganese-induced substrate promiscuity in the reaction catalyzed by phosphoglutamine cytidylyltransferase from Campylobacter jejuni

2019

Taylor, Z.W.; Raushel, F.M.

Biochemistry

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2144-2151

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768346

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Structural characterization of human O-phosphoethanolamine phospho-lyase

2020

Vettraino, C.; Peracchi, A.; Donini, S.; Parisini, E.

Acta Crystallogr. F Struct. Biol. Commun.

76

160-167

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Utilization of ethanolamine phosphate phospholyase as a unique astrocytic marker

2023

Tsujioka, H.; Yamashita, T.

Front. Cell. Neurosci.

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1097512

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The emerging roles of PHOSPHO1 and its regulated phospholipid homeostasis in metabolic disorders

2022

Liu, Y.; Wu, Y.; Jiang, M.

Front. Physiol.

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Substrate structure-activity relationship reveals a limited lipopolysaccharide chemotype range for intestinal alkaline phosphatase

2019

Komazin, G.; Maybin, M.; Woodard, R.W.; Scior, T.; Schwudke, D.; Schombel, U.; Gisch, N.; Mamat, U.; Meredith, T.C.

J. Biol. Chem.

294

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The role of ethanolamine phosphate phospholyase in regulation of astrocyte lipid homeostasis

2021

White, C.J.; Ellis, J.M.; Wolfgang, M.J.

J. Biol. Chem.

297

100830

775114

34098589

At4g29530 is a phosphoethanolamine phosphatase homologous to PECP1 with a role in flowering time regulation

2021

Tannert, M.; Balcke, G.U.; Tissier, A.; Koeck, M.

Plant J.

107

1072-1083

775143

31302410

Expression and functional characterization of sugar beet phosphoethanolamine/phosphocholine phosphatase under salt stress

2019

Sahashi, K.; Yamada-Kato, N.; Maeda, T.; Kito, K.; Cha-Um, S.; Rai, V.; Tanaka, Y.; Takabe, T.

Plant Physiol. Biochem.

142

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776433

37212658

Broad-spectrum inhibitors for conserved unique phosphoethanolamine methyltransferases in parasitic nematodes possess anthelmintic efficacy

2023

Zhang, X.; Sicalo Gianechini, L.; Li, K.; Kaplan, R.M.; Witola, W.H.

Antimicrob. Agents Chemother.

67

e0000823

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34386021

Cloning and functional identification of phosphoethanolamine methyltransferase in soybean (Glycine max)

2021

Ji, X.; Wu, X.; Chen, W.; Yuan, Q.; Shen, Y.; Chi, Y.

Front. Plant Sci.

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612158

778445

36710008

Functional analysis of phosphoethanolamine N-methyltransferase in plants and parasites essential S-adenosylmethionine-dependent methyltransferase in choline and phospholipid metabolism

2023

Bare, A.; Thomas, J.; Etoroma, D.; Lee, S.G.

Methods Enzymol.

680

101-137

778514

32479776

Structural and biochemical analysis of phosphoethanolamine methyltransferase from the pine wilt nematode Bursaphelenchus xylophilus

2020

Lee, S.G.; Chung, M.S.; DeMarsilis, A.J.; Holland, C.K.; Jaswaney, R.V.; Jiang, C.; Kroboth, J.H.P.; Kulshrestha, K.; Marcelo, R.Z.W.; Meyyappa, V.M.; Nelson, G.B.; Patel, J.K.; Petronio, A.J.; Powers, S.K.; Qin, P.R.; Ramachandran, M.; Rayapati, D.; Rincon, J.A.; Rocha, A.; Ferreira, J.G.R.N.; Steinbrecher, M.K.; Kaisen, Y.; Zhang, E.J.; Zou, AJ.; Gang, M.; Sparks, M.; Cascella, B.; Cruz, W.; Jez, J.M.

Mol. Biochem. Parasitol.

238

111291

Links to other databases for O-phosphoethanolamine

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