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Ligand phosphatidylethanolamine

Basic Ligand Information

Molecular Structure

Related pathways

Pathway Source

Pathways

BRENDA

cardiolipin biosynthesis, phosphatidylethanolamine bioynthesis

KEGG

Autophagy - animal, Autophagy - other, Autophagy - yeast, Biosynthesis of secondary metabolites, Glycerophospholipid metabolism, Glycosylphosphatidylinositol (GPI)-anchor biosynthesis, Kaposi sarcoma-associated herpesvirus infection, Pathogenic Escherichia coli infection, Retrograde endocannabinoid signaling more

MetaCyc

(Kdo)2-lipid A modification (H. pylori), anandamide biosynthesis I, cardiolipin and phosphatidylethanolamine biosynthesis (Xanthomonas), cardiolipin biosynthesis III, lipid A-core biosynthesis (P. gingivalis), palmitoyl ethanolamide biosynthesis, phosphatidylcholine biosynthesis V, phosphatidylethanolamine biosynthesis II, phosphatidylethanolamine biosynthesis III, phosphatidylserine and phosphatidylethanolamine biosynthesis I, phosphatidylserine biosynthesis II, plasmalogen biosynthesis II (anaerobic), superpathway of phospholipid biosynthesis II (plants) more

Show all BRENDA pathways known for phosphatidylethanolamine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (15 results)

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Show Natural Substrate (15 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.17

3 S-adenosyl-L-methionine + phosphatidylethanolamine = 3 S-adenosyl-L-homocysteine + phosphatidylcholine + 2 H+

675185

-

2.1.1.17

S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine

485195, 485181, 485176, 485175, 485183, 485186, 485192, 485187, 485184, 485190, 485189, 776371, 776664, 776733, 777750, 777783, 778594, 779269

-

2.1.1.17

2 entries

2.3.1.269

phosphatidylethanolamine + [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine = 1-lyso-phosphatidylethanolamine + [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine

756949

8B0M, 3D-view

2.7.8.29

L-1-phosphatidylethanolamine + L-serine = L-1-phosphatidylserine + ethanolamine

741056, 722906

-

2.7.8.B11

a phosphatidylglycerol + a phosphatidylethanolamine = a cardiolipin + ethanolamine

739625

-

3.1.4.12

phosphatidylethanolamine + H2O = diacylglycerol + ethanolamine phosphate

649984

-

3.1.4.3

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

749482

-

3.1.4.3

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

730853, 752075

-

3.1.4.4

phosphatidylethanolamine + H2O = 1,2-diacylglycerophosphate + ethanolamine

666219

-

3.1.4.4

phosphatidylethanolamine + H2O = ethanolamine + phosphatidic acid

708211, 708212, 710281, 709835

-

3.1.4.62

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

771119, 772964, 772740, 774692, 768414, 769326, 769295, 770924, 770991

-

3.1.4.62

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

769327, 771091

-

7.6.2.1

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

688899, 712395

-

7.6.2.1

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

670656, 669094, 668247

-

7.6.2.1

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

748744, 767536, 767618, 767605

-

3.1.4.3

2 entries

3.1.4.4

2 entries

3.1.4.62

2 entries

7.6.2.1

3 entries

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

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Show Natural Product (8 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.8.1

CDP-ethanolamine + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylethanolamine

-

-

2.7.8.1

CDP-ethanolamine + 1,2-diacylglycerol = CMP + a phosphatidylethanolamine

-

-

2.7.8.1

CDP-ethanolamine + diacylglycerol = phosphatidylethanolamine + CMP

-

-

2.7.8.1

3 entries

2.7.8.2

CDP-ethanolamine + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylethanolamine

-

-

4.1.1.65

Phosphatidyl-L-serine = Phosphatidylethanolamine + CO2

-

-

7.6.2.1

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

-

-

7.6.2.1

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

-

-

7.6.2.1

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

-

-

7.6.2.1

3 entries

Substrate in Enzyme-catalyzed Reactions (47 results)

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Show Substrate (47 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.15.3

phosphatidylethanolamine + NADH + H+ + O2 = ?

285363

-

2.1.1.15

S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine

485161

-

2.1.1.16

S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + ?

485163

-

2.1.1.17

3 S-adenosyl-L-methionine + phosphatidylethanolamine = 3 S-adenosyl-L-homocysteine + phosphatidylcholine + 2 H+

675185

-

2.1.1.17

S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine

485165, 485185, 485187, 485182, 485190, 485167, 485168, 485169, 485170, 485171, 485174, 485179, 485180, 485181, 485183, 485184, 485186, 485188, 485189, 485191, 485192, 485195, 485193, 485194, 485175, 485176, 485178, 485164, 485177, 485172, 485173, 485166, 757524, 776371, 776664, 776733, 777750, 777783, 778594, 779269, 777484

-

2.1.1.17

2 entries

2.1.1.71

S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-monomethylethanolamine

485193, 485554

-

2.1.1.79

S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + ?

485631, 485625

-

2.3.1.158

phosphatidylethanolamine + 1,2-diacylglycerol = 2-lysophosphatidylethanolamine + triacylglycerol

684576

-

2.3.1.269

phosphatidylethanolamine + [apolipoprotein FSL-1]-S-1,2-diacyl-sn-glyceryl-L-cysteine = 1-lyso-phosphatidylethanolamine + [lipoprotein FSL-1]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine

748746

8B0M, 3D-view

2.3.1.269

phosphatidylethanolamine + [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine = 1-lyso-phosphatidylethanolamine + [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine

756949, 758353

8B0M, 3D-view

2.3.1.269

2 entries

2.3.1.43

phosphatidylethanolamine + cholesterol = cholesteryl ester + lysophosphatidylethanolamine

703346

-

2.3.1.78

acetyl-CoA + phosphatidylethanolamine = CoA + N-acetylphosphatidylethanolamine

661443

-

2.7.8.29

L-1-phosphatidylethanolamine + L-serine = L-1-phosphatidylserine + ethanolamine

717768, 717208, 717210, 722906, 741056

-

2.7.8.B11

a phosphatidylglycerol + a phosphatidylethanolamine = a cardiolipin + ethanolamine

739625

-

3.1.1.26

phosphatidylethanolamine + H2O = ?

94294, 94292, 94293, 94291

-

3.1.1.3

phosphatidylethanolamine + H2O = ?

653521, 80843, 729664

-

3.1.1.32

diacyl-sn-glycero-3-phosphorylethanolamine + H2O = fatty acid + lysophosphatidylethanolamine

94322

-

3.1.1.32

phosphatidylethanolamine + H2O = 2-acylglycerophosphoethanolamine + a carboxylate

652226, 664591, 664829, 709425, 749593

-

3.1.1.32

phosphatidylethanolamine + H2O = ?

94303, 94340, 94324, 94315, 94335, 94320, 133898, 94311, 94326, 94332, 678433, 774463

-

3.1.1.32

phosphatidylethanolamine + H2O = lysophosphatidylethanolamine + a carboxylate

680300, 749810

-

3.1.1.32

phosphatidylethanolamine + H2O = lysophosphatidylethanolamine + a fatty acid anion

692411, 690664

-

3.1.1.4

phosphatidylethanolamine + arachidonic acid = arachidonoyl phosphatidylethanolamine

133888

-

3.1.1.4

phosphatidylethanolamine + H2O = 1-acylglycerophosphatidylethanolamine + fatty acid

774471

-

3.1.1.4

phosphatidylethanolamine + H2O = 1-acylglycerophosphorylethanolamine + fatty acid

133914, 133881, 133918, 133877, 133920, 133928, 133931, 133908, 133898, 133909, 133906, 133921, 663759

-

3.1.1.4

phosphatidylethanolamine + linoleic acid = lineoyl phosphatidylethanolamine + fatty acid

133888

-

3.1.1.5

phosphatidylethanolamine + H2O = lysophosphatidylethanolamine + glycerophosphorylethanolamine + a carboxylate

94373, 94386, 94378

-

3.1.1.5

phosphatidylethanolamine + H2O = lysophosphatidylethanolamine + glycerophosphorylethanolamine + a fatty acid

678790

-

3.1.4.12

phosphatidylethanolamine + H2O = diacylglycerol + ethanolamine phosphate

649984

-

3.1.4.12

phosphatidylethanolamine + H2O = diacylglycerol + phosphorylethanolamine

135149

-

3.1.4.3

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

715836, 716770

-

3.1.4.3

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

749482, 770209

-

3.1.4.3

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

730853, 752075, 750568

-

3.1.4.3

phosphatidylethanolamine + H2O = phosphorylethanolamine + 1,2-diacylglycerol

662895, 691450

-

3.1.4.3

phosphatidylethanolamine + H2O = phosphorylethanolamine + diacylglycerol

135301, 135289, 135286, 133931, 135299, 135304, 135308, 135298, 135292, 135305, 135306, 135307, 135311

-

3.1.4.4

phosphatidylethanolamine + H2O = 1,2-diacylglycerophosphate + ethanolamine

135456, 135429, 135448, 135458, 135426, 135457, 135428, 135435, 135455, 666219, 135433

-

3.1.4.4

phosphatidylethanolamine + H2O = ethanolamine + phosphatidate

651126, 716035, 751819, 751163

-

3.1.4.4

phosphatidylethanolamine + H2O = ethanolamine + phosphatidic acid

708211, 708212, 710281, 709835, 707106

-

3.1.4.4

phosphatidylethanolamine + H2O = phosphatidate + ethanolamine

694606

-

3.1.1.32

5 entries

3.1.1.4

4 entries

3.1.1.5

2 entries

3.1.4.12

2 entries

3.1.4.3

5 entries

3.1.4.4

4 entries

3.1.4.41

phosphatidylethanolamine + H2O = ?

135485

-

3.1.4.62

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

771119, 772964, 772740, 774692, 768414, 769326, 769295, 770924, 770991

-

3.1.4.62

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

769327, 771091, 772870

-

3.1.4.62

2 entries

7.5.2.6

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

766510

-

7.6.2.1

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

688899, 712395, 718993, 749842, 734287, 735189, 734249

-

7.6.2.1

phosphatidylethanolamine/in = phosphatidylethanolemine/out

667578

-

7.6.2.1

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

670656, 669094, 668247, 697213, 700100

-

7.6.2.1

phosphatidylethanolamine/out = phosphatidylethanolamine/in

668454, 667175

-

7.6.2.1

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

748744, 749049, 749181, 749361, 747035, 747611, 747894, 767536, 767618, 767605, 767233, 767789, 767899, 767105, 766240, 767111

-

7.6.2.1

5 entries

Product in Enzyme-catalyzed Reactions (17 results)

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Show Product (17 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.148

lyso-Phosphatidylethanolamine + phospholipid = Phosphatidylethanolamine + lyso-phospholipid

-

-

2.3.1.148

Phosphatidylcholine + lyso-phosphatidylethanolamine = lyso-Phosphatidylcholine + phosphatidylethanolamine

-

-

2.3.1.148

2 entries

2.3.1.40

acyl-(acyl-carrier protein) + O-(2-acyl-sn-glycero-3-phospho) ethanolamine = (acyl-carrier protein) + O-(1,2-diacyl-sn-glycero-3-phospho) ethanolamine

486910

-

2.7.8.1

CDP-ethanolamine + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylethanolamine

-

-

2.7.8.1

CDP-ethanolamine + 1,2-diacylglycerol = CMP + a phosphatidylethanolamine

644346, 644359, 644323, 644345, 644356, 644357, 644358, 644360, 644362, 644363, 644365, 644406, 644407, 644409, 644410, 644411, 644343, 644349, 644355, 644401, 644347, 644353, 644344, 644414, 644350, 644408, 644413, 644351, 644348, 644412, 644354, 644352, 644385, 644361, -

-

2.7.8.1

CDP-ethanolamine + diacylglycerol = phosphatidylethanolamine + CMP

-

-

2.7.8.2

CDP-ethanolamine + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylethanolamine

-

-

2.7.8.2

CDP-choline + bacterial 1,2-diacyl-sn-glycerol = CMP + phosphatidylethanolamine

-

-

2.7.8.2

CDP-ethanolamine + 1,2-diacylglycerol = CMP + phosphatidylethanolamine

-

-

2.7.8.1

3 entries

2.7.8.2

3 entries

3.1.4.4

phosphatidylcholine + ethanolamine = phosphatidylethanolamine + choline

-

-

4.1.1.65

Phosphatidyl-L-serine = Phosphatidylethanolamine + CO2

4762, 4768, 4782, 4785, 4783, 4765, 4777, 4764, 4767, 4769, 4770, 4773, 4774, 4775, 4780, 4786, 4789, 4790, 4761, 4763, 4771, 4776, 4787, 4788, 4791, 649308, 652981, 4779, 4784, 652561, 4778, 4781, 653276, 4772, 4766, -

-

7.5.2.6

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

-

-

7.6.2.1

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

-

-

7.6.2.1

phosphatidylethanolamine/out = phosphatidylethanolamine/in

-

-

7.6.2.1

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

-

-

7.6.2.1

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

-

-

7.6.2.1

phosphatidylethanolamine/in = phosphatidylethanolemine/out

-

-

7.6.2.1

5 entries

Activator in Enzyme-catalyzed Reactions (84 results)

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Show Activating Compound (84 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.12.24

144% activity at 0.1 mg per g wet weight of cells

733523

-

1.2.3.3

enzyme is specifically activated by phosphotidylethanolamine (16:0-18:1). The C-terminal sequence is important for activation

762867

-

1.3.3.3

3.9fold activation at 0.5 mg/ml

390964

-

1.8.4.2

activates at low concentration

394810, 394817, 394812

-

2.3.1.15

activation of microsomal enzyme

486348

-

2.3.1.15

activation of reconstituted mitochondrial acyl transferase

486378

-

2.3.1.15

inefficient, pH-dependent

486372

-

2.3.1.15

seems to be required for optimal activity

486367

-

2.3.1.15

4 entries

2.3.1.23

incorporation in membrane elevates acyltransferase activity

486641

-

2.3.1.26

weak stimulatory effect on activity

486682

-

2.3.1.269

-

747801

8B0M, 3D-view

2.4.1.132

activation

636753, 636754

-

2.4.1.132

and mixtures with other phospholipids forming non-bilayer phospholipid phases e.g. hexagonal phases

636754

-

2.4.1.132

enzyme-phospholipid-complex formation

636754

-

2.4.1.132

from various eukaryotic and prokaryotic sources

636754

-

2.4.1.132

in the absence of detergent

636754

-

2.4.1.132

no activation by phosphatidylcholine, phosphatidylinositol, phosphatidylglycerol, sphingomyelin, lysophosphocholine or lysophosphoethanolamine

636754

-

2.4.1.132

phosphoethanolamine containing unsaturated acylchains

636754

-

2.4.1.132

7 entries

2.4.1.16

stimulates

488645

-

2.4.1.173

increases 125% of activity

637775

-

2.4.1.179

activation, less efficient than Triton CF-54

638380

-

2.4.1.38

activation

489511

-

2.4.1.46

mild activity-enhancing effect (60%, at 40 mol percent concentration)

735136

-

2.4.1.47

optimum phospholipid requirement of phosphatidylethanolamine: phosphatidylcholine of 5:1 with 2.5fold stimulation, Na cholate prevents stimulation

489219

-

2.4.1.47

stimulates

489216

-

2.4.1.47

2 entries

2.4.1.54

activates

489288

-

2.4.1.58

requirement, most effective phospholipid, phosphatidylethanolamine containing unsaturated or cyclopropane acyl groups is more effective than that containing saturated acyl groups

489212

-

2.4.1.83

increases activity 2.3fold at the optimal concentration

489447

-

2.4.1.83

relative activity: 125%

692257

-

2.4.1.83

2 entries

2.4.1.88

activation

489482

-

2.4.1.90

activation

489511

-

2.5.1.39

-

637001

-

2.7.1.107

activates only in presence of Triton X-100

640361

-

2.7.1.107

activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin

640370

-

2.7.1.107

DGKalpha can be activated in vitro in a Ca2+-independent manner by lipids such as phosphatidylethanolamine

701582

-

2.7.1.107

plus cardiolipin, activates

640362

-

2.7.1.107

4 entries

2.7.1.108

stimulated by after dialysis

640396

-

2.7.1.174

-

687738

-

2.7.1.197

-

736548

-

2.7.11.17

activation

490759

-

2.7.8.14

stimulates 5fold 0.36 mM

645346

-

2.7.8.15

stimulates activity of enzyme in endoplasmic membrane vesicles

645355

-

2.7.8.2

activates

644335

-

2.7.8.5

stimulates, no stimulation by other diacylglycerophosphatides or lysophosphatides

644293

-

2.7.8.8

slightly activates. The enzyme is completely desensitized by treatment for 5 min at 40°C against the effect of phosphatidylethanolamine without loss of activity

643784

-

3.1.1.1

activates

171023

-

3.1.1.13

slightly activating

133829

-

3.1.1.2

stimulates

646527

-

3.1.1.2

stimulation

646509

-

3.1.1.2

2 entries

3.1.1.79

0.075 mM, approx. 6fold activation upon incorporation into cholestryl oleate liquid crystals

133829

-

3.1.2.2

-

171023

-

3.1.2.20

-

171023

-

3.1.3.1

1fold stimulation of hydrophilic enzyme form

94623

-

3.1.3.4

stimulation

134894

-

3.1.3.51

0.1 mM, slight stimulation

134920

-

3.1.3.51

activates

134915

-

3.1.4.11

activates the hydrolysis. Human platelet phosphatidylinositol phosphodiesterase

285214

-

3.1.4.11

enhances hyrolysis of phosphatidylinositol 4,5-diphosphate, membrane bound enzyme and cytosolic enzyme

135123

-

3.1.4.11

slightly increases rate of hydrolysis

285223

-

3.1.4.11

stimulation in presence of 1 mM Ca2+

135141

-

3.1.4.12

-

135183

-

3.1.4.12

0.2 mM, 2.9fold activation

652090

-

3.1.4.12

sphingomyelinase is enhanced by cholesterol and by lipids with an intrinsic negative curvature, e.g. phosphatidylethanolamine

714335

-

3.1.3.51

2 entries

3.1.4.11

4 entries

3.1.4.12

3 entries

3.1.4.3

phospholipase C is enhanced by cholesterol and by lipids with an intrinsic negative curvature, e.g. phosphatidylethanolamine

714335

-

3.1.4.4

activates PLD activity, leading to increased matrix metalloproteinase 9, MMP-9, activity

707273

-

3.1.4.4

required for maximal activity of the beta and gamma-enzymes

135446

-

3.1.4.4

2 entries

3.1.4.50

activation

646486

-

3.1.4.54

activates

708110

-

3.1.4.54

activates 5.91fold at 1 mM

708110

-

3.1.4.54

2 entries

3.1.8.1

stimulation

646509

-

3.2.1.113

activation, in the presence of 3.5 mM Triton X-100

646572

-

3.2.1.24

8fold stimulation at 0.002%

136002

-

3.4.21.89

is required to maintain activity of the membrane-incorporated signal-peptidase (full-length signal peptidase I incoporated into phospholipid vesicles). Maximal activity is achieved at about 55% phosphatidylethanolamine

667597

-

3.4.21.B1

enhances autofragmentation and serine protease activity at 0.001 mg/ml and 0.00001 mg/ml

650490

-

3.5.1.138

phosphatidylethanolamine from bovine brain activates the enzyme activity 2.1fold at an optimum phospholipid concentration of 5 mg/ml

771008

-

3.6.1.42

20-25% stimulation

768653

-

3.6.1.75

-

680601

-

4.1.99.5

requirement, phosphatidylcholine is preferred, phopshatidylserine and phopshatidylethanolamine substitute less effectively

648395

-

5.3.99.5

-

727320

-

6.2.1.3

slight stimulation, acyl-CoA synthetase II

759

-

7.1.1.9

more than 3fold activation

396090

-

7.6.2.1

activates to a lesser degree

712395

-

7.6.2.1

slight activation

685075

-

7.6.2.1

2 entries

7.6.2.9

non-bilayer lipid essential for high activity of OpuA

655328

-

Inhibitor in Enzyme-catalyzed Reactions (27 results)

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Show Inhibitors (27 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.101

-

285690

-

1.14.15.6

-

285415

-

2.3.1.15

1,2-unsaturated species

486363

-

2.3.1.20

-

735573

-

2.3.1.42

above 1.5 mM

486953

-

2.4.1.121

-

488523

-

2.4.1.38

-

489513

-

2.4.1.90

-

489513

-

2.7.1.67

-

641804

-

2.7.1.67

0.1 mM, 24% inhibition

641791

-

2.7.1.67

0.6 mM, 67% inhibition

641799

-

2.7.1.67

3 entries

2.7.1.94

inhibition alone, synergistic activation with the protein peak eluted from hydroxylapatite by 25 mM phosphate

642127

-

2.7.7.41

2 mM, 16% inhibition

643311

-

2.7.8.1

-

644406

-

2.7.8.15

-

645354

-

3.1.1.13

-

133829

-

3.1.3.27

3 mM, 70% inhibition. competitive

751064

-

3.1.3.51

-

134917

-

3.1.3.51

1 mM

134920

-

3.1.3.51

2 entries

3.1.4.11

25% inhibition, in presence of 0.001 mM Ca2+

135141

-

3.1.4.3

-

135291

-

3.1.4.4

-

135449

-

3.2.1.104

-

208429

-

3.4.21.39

-

29374

-

3.5.1.138

phosphatidylethanolamine at concentrations higher than 5 mg/ml is slightly inhibitory

771008

-

3.6.1.43

-

134917

-

4.6.1.6

-

648788

-

3D Structure of Enzyme-Ligand-Complex (PDB) (133 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (133 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.10.3.9

7PI0, 3D-view

1.10.3.9

7PIN, 3D-view

1.10.3.9

7PIW, 3D-view

1.10.3.9

7PNK, 3D-view

1.10.3.9

7PI0, 3D-view

1.10.3.9

7PIN, 3D-view

1.10.3.9

7PIW, 3D-view

1.10.3.9

7PNK, 3D-view

1.10.3.9

8 entries

1.13.11.1

5TD3, 3D-view

1.9.3.1

6YMX, 3D-view

1.9.3.1

6YMY, 3D-view

1.9.3.1

6YMX, 3D-view

1.9.3.1

6YMY, 3D-view

1.97.1.12

6SL5, 3D-view

1.97.1.12

6ZZX, 3D-view

1.97.1.12

6ZZY, 3D-view

1.97.1.12

7A4P, 3D-view

1.97.1.12

7BLZ, 3D-view

1.97.1.12

6SL5, 3D-view

1.97.1.12

6ZZX, 3D-view

1.97.1.12

6ZZY, 3D-view

1.97.1.12

7A4P, 3D-view

1.97.1.12

7BLZ, 3D-view

1.9.3.1

4 entries

1.97.1.12

10 entries

2.3.1.269

8B0M, 3D-view

2.4.1.267

6SNI, 3D-view

2.4.99.18

6EZN, 3D-view

2.4.99.18

8AGB, 3D-view

2.4.99.18

8AGC, 3D-view

2.4.99.18

8AGE, 3D-view

2.4.99.18

6EZN, 3D-view

2.4.99.18

8AGB, 3D-view

2.4.99.18

8AGC, 3D-view

2.4.99.18

8AGE, 3D-view

2.4.99.18

8 entries

3.4.21.69

3JTC, 3D-view

3.4.24.64

8BPX, 3D-view

3.6.3.8

2AGV, 3D-view

3.6.3.8

2DQS, 3D-view

3.6.3.8

2EAU, 3D-view

3.6.3.8

3AR3, 3D-view

3.6.3.8

3AR4, 3D-view

3.6.3.8

3AR5, 3D-view

3.6.3.8

3AR6, 3D-view

3.6.3.8

3AR7, 3D-view

3.6.3.8

3NAM, 3D-view

3.6.3.8

3NAN, 3D-view

3.6.3.8

4J2T, 3D-view

3.6.3.8

4YCM, 3D-view

3.6.3.8

4YCN, 3D-view

3.6.3.8

5ZMV, 3D-view

3.6.3.8

2AGV, 3D-view

3.6.3.8

2DQS, 3D-view

3.6.3.8

2EAU, 3D-view

3.6.3.8

3AR3, 3D-view

3.6.3.8

3AR4, 3D-view

3.6.3.8

3AR5, 3D-view

3.6.3.8

3AR6, 3D-view

3.6.3.8

3AR7, 3D-view

3.6.3.8

3NAM, 3D-view

3.6.3.8

3NAN, 3D-view

3.6.3.8

4J2T, 3D-view

3.6.3.8

4YCM, 3D-view

3.6.3.8

4YCN, 3D-view

3.6.3.8

5ZMV, 3D-view

7.1.1.2

7AQQ, 3D-view

7.1.1.2

7AQW, 3D-view

7.1.1.2

7AR7, 3D-view

7.1.1.2

7AR8, 3D-view

7.1.1.2

7ARB, 3D-view

7.1.1.2

8BEF, 3D-view

7.1.1.2

8BEH, 3D-view

7.1.1.2

8BPX, 3D-view

7.1.1.2

7AQQ, 3D-view

7.1.1.2

7AQW, 3D-view

7.1.1.2

7AR7, 3D-view

7.1.1.2

7AR8, 3D-view

7.1.1.2

7ARB, 3D-view

7.1.1.2

8BEF, 3D-view

7.1.1.2

8BEH, 3D-view

7.1.1.2

8BPX, 3D-view

7.1.1.8

6YMX, 3D-view

7.1.1.8

8AB6, 3D-view

7.1.1.8

8AB7, 3D-view

7.1.1.8

8AB8, 3D-view

7.1.1.8

8AB9, 3D-view

7.1.1.8

8ABA, 3D-view

7.1.1.8

8ABB, 3D-view

7.1.1.8

8ABE, 3D-view

7.1.1.8

8ABF, 3D-view

7.1.1.8

8ABG, 3D-view

7.1.1.8

8ABH, 3D-view

7.1.1.8

8ABI, 3D-view

7.1.1.8

8ABJ, 3D-view

7.1.1.8

8ABK, 3D-view

7.1.1.8

8ABL, 3D-view

7.1.1.8

8ABM, 3D-view

7.1.1.8

8AC3, 3D-view

7.1.1.8

8AC4, 3D-view

7.1.1.8

8AC5, 3D-view

7.1.1.8

8BEL, 3D-view

7.1.1.8

8BPX, 3D-view

7.1.1.8

6YMX, 3D-view

7.1.1.8

8AB6, 3D-view

7.1.1.8

8AB7, 3D-view

7.1.1.8

8AB8, 3D-view

7.1.1.8

8AB9, 3D-view

7.1.1.8

8ABA, 3D-view

7.1.1.8

8ABB, 3D-view

7.1.1.8

8ABE, 3D-view

7.1.1.8

8ABF, 3D-view

7.1.1.8

8ABG, 3D-view

7.1.1.8

8ABH, 3D-view

7.1.1.8

8ABI, 3D-view

7.1.1.8

8ABJ, 3D-view

7.1.1.8

8ABK, 3D-view

7.1.1.8

8ABL, 3D-view

7.1.1.8

8ABM, 3D-view

7.1.1.8

8AC3, 3D-view

7.1.1.8

8AC4, 3D-view

7.1.1.8

8AC5, 3D-view

7.1.1.8

8BEL, 3D-view

7.1.1.8

8BPX, 3D-view

7.1.2.2

6WM2, 3D-view

7.1.2.2

9BRD, 3D-view

7.1.2.2

6WM2, 3D-view

7.1.2.2

9BRD, 3D-view

7.2.2.2

8SQ0, 3D-view

7.2.2.2

8SQL, 3D-view

7.2.2.2

8SQ0, 3D-view

7.2.2.2

8SQL, 3D-view

7.6.2.3

8SQ0, 3D-view

7.6.2.3

8SQL, 3D-view

7.6.2.3

8SQ0, 3D-view

7.6.2.3

8SQL, 3D-view

3.6.3.8

28 entries

7.1.1.2

16 entries

7.1.1.8

42 entries

7.1.2.2

4 entries

7.2.2.2

4 entries

7.6.2.3

4 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (1 result)

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Show Turnover Number (1 entry)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.1.1.4

26.9

-

pH 9, 45°C

774471

K_M Value (12 results)

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Show KM Value (12 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.1.1.17

0.0336

-

-

485175, 485176

2.1.1.17

0.057

-

-

485166

2.1.1.17

5

-

-

485171

2.1.1.17

3 entries

2.1.1.79

0.53

-

-

485625

3.1.1.32

0.92

-

-

94322

3.1.1.4

0.02

-

recombinant PLA2

133881

3.1.1.4

0.024

-

natural PLA2

133881

3.1.1.4

0.067

-

active enzyme

133914

3.1.1.4

0.167

-

inactivated enzyme

133914

3.1.1.4

10.5

-

pH 9, 45°C

774471

3.1.4.4

0.91

-

-

135429, 135433

3.1.4.4

4

-

-

135435

3.1.1.4

5 entries

3.1.4.4

2 entries

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.1.3.27

2.7

-

pH 7.5, 23°C

751064

References & Links

Literature References (375)

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Show Reference (375 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

759

-

Long-chain acyl-CoA synthetase I and II from Candida lipolytica

1981

Hosaka, K.; Mishina, M.; Kamiryo, T.; Numa, S.

Methods Enzymol.

71

325-333

4761

1495416

Phosphatidylserine decarboxylase from rat liver

1992

Volker, D.R.; Golden, E.B.

Methods Enzymol.

209

360-365

4762

5002558

Enzymes of phospholipid metabolism: localization in the cytoplasmic and outer membrane of the cell envelope of Escherichia coli and Salmonella typhimurium

1971

Bell, R.M.; Mavis, R.D.; Osborn, M.J.; Vagelos, P.R.

Biochim. Biophys. Acta

249

628-635

4763

4512836

Effect of phosphatidyl serine decarboxylase on neural excitation

1972

Cook, A.M.; Low, E.; Ishijimi, M.

Nature New Biol.

239

150-151

4764

4598120

Purification and properties of phosphatidylserine decarboxylase from Escherichia coli

1974

Dowhan, W.; Wickner, W.T.; Kennedy, E.P.

J. Biol. Chem.

249

3079-3084

4765

-

Studies on decarboxylation of phosphatidylserine

1974

Suda, T.; Matsuda, M.

Biochim. Biophys. Acta

369

331-337

4766

235903

Phosphatidylserine decarboxylase: analysis of its action towards unsaturated and saturated phosphatidylserine and the effect of Triton X-100 on activity

1975

Warner, T.G.; Dennis, E.A.

Arch. Biochem. Biophys.

167

761-768

4767

1100627

Action of the highly purified, membrane-bound enzyme phosphatidylserine decarboxylase Escherichia coli toward phosphatidylserine in mixed micelles and erythrocyte ghosts in the presence of surfactant

1975

Warner, T.G.; Dennis, E.A.

J. Biol. Chem.

250

8004-8009

4768

199573

Intracellular distribution of enzymes of phospholipid metabolism in several gram-negative bacteria

1977

Dutt, A.; Dowhan, W.

J. Bacteriol.

132

159-165

4769

338609

Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli

1978

Satre, M.; Kennedy, E.P.

J. Biol. Chem.

253

479-483

4770

368058

Increased synthesis of phosphatidylserine decarboxylase in a strain of Escherichia coli bearing a hybrid plasmid

1979

Tyhach, R.J.; Hawrot, E.; Satre, M.; Kennedy, P.

J. Biol. Chem.

254

627-633

4771

490039

Phosphatidylserine biosynthesis in mitochondria from the Morris 7777 hepatoma

1979

Hostetler, K.Y.; Zenner, B.D.; Morris, H.P.

J. Lipid Res.

20

607-613

4772

7493929

A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody

1995

Igarashi, K.; Kaneda, M.; Yamaji, A.; Saido, T.C.; Kikkawa, U.; Ono, Y.; Inoue, K.; Umeda, M.

J. Biol. Chem.

270

29075-29078

4773

7011377

Kinetics and protein subunit interactions of Escherichia coli phosphatidylserine decarboxylase in detergent solution

1981

Rizzolo, L.J.

Biochemistry

20

868-873

4774

6263870

Phospholipid biosynthesis in some anaerobic bacteria

1981

Silber, P.; Borie, R.P.; Mikowski, E.J.; Goldfine, H.

J. Bacteriol.

147

57-61

4775

7024734

Phosphatidylserine decarboxylase from Escherichia coli

1981

Hawrot, E.

Methods Enzymol.

71

571-576

4776

6859873

Characterization of brain phosphatidylserine decarboxylase: localization in the mitochondrial inner membrane

1983

Percy, A.K.; Moore, J.F.; Carson, M.A.; Waechter, C.J.

Arch. Biochem. Biophys.

223

484-494

4777

6862014

Phosphatidylserine decarboxylase is located on the external side of the inner mitochondrial membrane

1983

Zborowski, J.; Dygas, A.; Wojtczak, L.

FEBS Lett.

157

179-182

4778

6319391

Localization of phospholipid biosynthetic enzyme activities in cell-free fractions derived from Rhodopseudomonas sphaeroides

1984

Cain, B.D.; Donohue, T.J.; Shepherd, W.D.; Kaplan, S.

J. Biol. Chem.

259

942-948

4779

3005242

Subcellular and submitochondrial localization of phospholipid-synthesizing enzymes in Saccharomyces cerevisiae

1986

Kuchler, K.; Daum, G.; Paltauf, F.

J. Bacteriol.

165

901-910

4780

-

Steric course of the reaction catalyzed by phosphatidylserine decarboxylase from Escherichia coli

1988

No, Z.; Sanders, C.R.; Dowhan, W.; Tsai, M.D.

Bioorg. Chem.

16

184-188

4781

4020299

Phosphatidylserine decarboxylase from Clostridium butyricum

1985

Verma, J.N.; Goldfine, H.

J. Lipid Res.

26

610-616

4782

8870646

Post-translational processing of the phosphatidylserine decarboxylase gene product in Chinese hamster ovary cells

1996

Kuge, O.; Saito, K.; Kojima, M.; Akamatsu, Y.; Nishijima, M.

Biochem. J.

319

33-38

4783

9370338

Phosphatidylserine decarboxylase

1997

Voelker, D.R.

Biochim. Biophys. Acta

1348

236-244

4784

1929418

Regulation of phosphatidylserine decarboxylase in Saccharomyces cerevisiae by inositol and choline: kinetics of repression and derepression

1991

Overmeyer, J.H.; Waechter, C.J.

Arch. Biochem. Biophys.

290

511-516

4785

9211308

Phosphatidylserine decarboxylases: pyruvoyl-dependent enzymes from bacteria to mammals

1997

Dowhan, W.

Methods Enzymol.

280

81-88

4786

1495415

Phosphatidylserine decarboxylase from Escherichia coli

1992

Dowhan, W.; Li, Q.X.

Methods Enzymol.

209

348-359

4787

8132055

Purification of plasma membrane rat liver phosphatidylserine decarboxylase

1993

Auchi, L.; Tsvetnitsky, V.; Yeboah, F.A.; Gibbons, W.A.

Biochem. Soc. Trans.

21

488S

4788

2618245

Effect of Triton X-100 on the activity and solubilization of rat liver mitochondrial phosphatidylserine decarboxylase

1989

Dygas, A.; Zborowski, J.

Acta Biochim. Pol.

36

131-141

4789

2406271

Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli

1990

Li, Q.X.; Dowhan, W.

J. Biol. Chem.

265

4111-4115

4790

3042771

Structural characterization of Escherichia coli phosphatidylserine decarboxylase

1988

Li, Q.X.; Dowhan, W.

J. Biol. Chem.

263

11516-11522

4791

1512221

On the mechanism of the mitochondrial decarboxylation of phosphatidylserine

1992

Hovius, R.; Faber, B.; Brigot, B.; Nicolay, K.; de Kruijff, B.

J. Biol. Chem.

267

16790-16795

29374

3890754

Chymotrypsin- and trypsin-type serine proteases in rat mast cells: properties and functions

1985

Kido, H.; Fukusen, N.; Katunuma, N.

Arch. Biochem. Biophys.

239

436-443

80843

2051929

Purification and substrate specificity of rat hepatic lipase

1991

Waite, M.; Thuren, T.Y.; Wilcox, R.W.; Sisson, P.J.; Kucera, G.L.

Methods Enzymol.

197

331-339

94291

-

Purification of a lipolytic acyl-hydrolase from Phaseolus vulgaris leaves by affinity chromatography on palmitolyated gauze and its properties

1979

Matsuda, H.; Tanaka, G.; Morita, K.; Hirayama, O.

Agric. Biol. Chem.

43

563-570

94292

-

Enzymatic properties of a galactolipase from rice bran

1979

Matsuda, H.; Hirayama, O.

Agric. Biol. Chem.

43

697-703

94293

454635

Purification and properties of a lipolytic acyl-hydrolase from potato leaves

1979

Matsuda, H.; Hirayama, O.

Biochim. Biophys. Acta

573

155-165

94294

236765

Purification and properties of a lipid acyl-hydrolase from potato tubers

1975

Hirayama, O.; Matsuda, H.; Takeda, H.; Maenaka, K.; Takatsuka, H.

Biochim. Biophys. Acta

384

127-137

94303

6692000

Substrate specificity of two cationic lipases with high phospholipase A1 activity purified from guinea pig pancreas. II. Studies on glycerophospholipids

1984

Fauvel, J.; Chap, H.; Roques, V.; Douste-Blazy, L.

Biochim. Biophys. Acta

792

72-78

94311

6833259

A phospholipase A1 from the hemolymph of the tobacco hornworm, Manduca sexta

1983

Nieder, M.; Law, J.H.

J. Biol. Chem.

258

4304-4310

94315

7278676

Phospholipases A1 from lysosomes and plasma membranes of rat liver

1981

Waite, M.; Rao, R.H.; Griffin, H.; Franson, R.; Miller, C.; Sisson, P.; Frye, J.

Methods Enzymol.

71

674-689

94320

4415399

Purification and properties of a membrane-bound phospholipase A1 from Mycobacterium phlei

1974

Nishijima, M.; Akamatsu, Y.; Nojima, S.

J. Biol. Chem.

249

5658-5667

94322

4807791

Subcellular distribution and kinetic properties of rat brain phospholipases A1 and A2

1973

Woelk, H.; Porcellati, G.

Hoppe-Seyler's Z. Physiol. Chem.

354

90-100

94324

4946924

A membrane-bound phospholipase A1 purified from Escherichia coli

1971

Scandella, C.J.; Kornberg, A.

Biochemistry

10

4447-4456

94326

8422930

Role of a serum phospholipase A1 in the phosphati dylserine-induced T cell inhibition

1993

Bellini, F.; Bruni, A.

FEBS Lett.

316

1-4

94332

8216258

The presence of Ca2+-independent phospholipase A1 highly specific for phosphatidylinositol in bovine brain

1993

Ueda, H.; Kobayashi, T.; Kishimoto, M.; Tsusumi, T.; Watanabe, S.; Okuyama, H.

Biochem. Biophys. Res. Commun.

195

1272-1279

94335

7786901

Phospholipid interactions affect substrate hydrolysis by bovine brain phospholipase A1

1995

Pete, M.J.; Exton, J.H.

Biochim. Biophys. Acta

1256

367-373

94340

10348899

Characterization of heparin low-affinity phospholipase A1 present in brain and testicular tissue

1999

Uchiyama, S.I.; Miyazaki, Y.; Amakasu, Y.; Kuwata, H.; Nakatani, Y.; Atsumi, G.I.; Murakami, M.; Kudo, I.

J. Biochem.

125

1001-1010

94373

-

Purification and some properties of soluble phospholipase B from baker's yeast (Saccharomyces cerevisiae)

1985

Ichimasa, M.; Shiobara, M.

Agric. Biol. Chem.

49

1083-1089

94378

7278668

Lysophospholipase-transacylase from rat lung

1981

Van den Bosch, H.; Vianen, G.M.; van Heusden, G.P.H.

Methods Enzymol.

71

513-521

94386

8816850

Kashiwabara, Y.: Purification and properties of a membrane-bound phospholipase B from Mycobacterium lepraemurium

1996

Maeda, S

Biochim. Biophys. Acta

1303

31-38

94623

1815949

Properties of amphiphilic and hydrophilic forms of alkaline phosphatase from human liver

1991

Kihn, L.; Rutkowski, D.; Nakatsui, T.; Stinson, R.A.

Enzyme

45

155-164

133829

8468334

Hydrolysis of cholesteryl oleate liquid crystals by hormon-sensitive lipase

1993

Tsujita,T.; Okuda, H.

J. Biochem.

113

264-269

133877

8925928

Purification and characterization of nuclear alkaline phospholipase A2 in rat ascites hepatoma cells

1996

Oishi, T.; Tamiya-Koizumi, K.; Kudo, I.; Iino, S.; Takagi, K.; Yoshida, Y.

FEBS Lett.

394

55-60

133881

-

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