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Ligand ethanolamine

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

cardiolipin biosynthesis, phosphatidylethanolamine bioynthesis

KEGG

Glycerophospholipid metabolism, Retrograde endocannabinoid signaling

MetaCyc

achromobactin biosynthesis, anandamide degradation, cardiolipin and phosphatidylethanolamine biosynthesis (Xanthomonas), cardiolipin biosynthesis III, choline biosynthesis I, choline biosynthesis II, ethanolamine utilization, phosphatidylethanolamine biosynthesis II, phosphatidylethanolamine biosynthesis III, phosphatidylserine biosynthesis II, phospholipid remodeling (phosphatidylethanolamine, yeast), plasmalogen biosynthesis I (aerobic), plasmalogen degradation, superpathway of phospholipid biosynthesis II (plants) more

Show all BRENDA pathways known for ethanolamine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Natural Substrate (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.8

ethanolamine + H2O + O2 = glycolaldehyde + NH3 + H2O2

742141, 391966

-

2.7.1.32

ethanolamine + ATP = O-phosphoethanolamine + ADP

685011

-

2.7.1.82

ATP + ethanolamine = ADP + O-phosphoethanolamine

137599, 738268, 642052, 739083, 702145, 739295, 762164, 662250

-

4.3.1.7

ethanolamine = ?

34383

3abo, 3D-view

4.3.1.7

ethanolamine = ?

34383

3abs, 3D-view

4.3.1.7

ethanolamine = acetaldehyde + NH3

680355, 680364, 682751, 690960, 691337, 662046, 690905, 690280, 692739

3abo, 3D-view

4.3.1.7

ethanolamine = acetaldehyde + NH3

680355, 680364, 682751, 690960, 691337, 662046, 690905, 690280, 692739

3abs, 3D-view

4.3.1.7

4 entries

In Vivo Product in Enzyme-catalyzed Reactions (31 results)

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Show Natural Product (31 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.8.29

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

0

-

2.7.8.B11

a phosphatidylglycerol + a phosphatidylethanolamine = a cardiolipin + ethanolamine

0

-

3.1.3.75

O-phosphoethanolamine + H2O = ethanolamine + phosphate

0

-

3.1.3.75

phosphoethanolamine + H2O = ethanolamine + phosphate

0

-

3.1.3.75

2 entries

3.1.4.2

glycero-3-phosphoethanolamine + H2O = sn-glycerol-3-phosphate + ethanolamine

0

-

3.1.4.39

1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine

0

-

3.1.4.4

phosphatidylethanolamine + H2O = 1,2-diacylglycerophosphate + ethanolamine

0

-

3.1.4.4

phosphatidylethanolamine + H2O = ethanolamine + phosphatidic acid

0

-

3.1.4.46

glycerophosphoethanolamine + H2O = sn-glycerol 3-phosphate + ethanolamine

0

-

3.1.4.46

sn-glycero-3-phosphoethanolamine + H2O = ethanolamine + sn-glycerol 3-phosphate

0

-

3.1.4.4

2 entries

3.1.4.46

2 entries

3.5.1.4

anandamide + H2O = arachidonic acid + ethanolamine

0

-

3.5.1.60

N-alpha-linolenoylethanolamide + H2O = alpha-linoleate + ethanolamine

0

-

3.5.1.60

N-arachidonoylethanolamide + H2O = arachidonate + ethanolamine

0

-

3.5.1.60

N-arachidonoylethanolamine + H2O = arachidic acid + ethanolamine

0

-

3.5.1.60

N-eicosapentaenoylethanolamide + H2O = eicosapentanoate + ethanolamine

0

-

3.5.1.60

N-linoleoylethanolamide + H2O = linoleate + ethanolamine

0

-

3.5.1.60

N-oleoylethanolamide + H2O = oleate + ethanolamine

0

-

3.5.1.60

N-palmitoylethanolamide + H2O = palmitate + ethanolamine

0

-

3.5.1.60

N-stearoylethanolamide + H2O = stearate + ethanolamine

0

-

3.5.1.60

oleoylethanolamide + H2O = oleate + ethanolamine

0

-

3.5.1.60

oleoylethanolamide + H2O = oleic acid + ethanolamine

0

-

3.5.1.60

palmitoylethanolamide + H2O = palmitate + ethanolamine

0

-

3.5.1.60

palmitoylethanolamide + H2O = palmitic acid + ethanolamine

0

-

3.5.1.99

(9Z)-N-ethyloctadec-9-enamide + H2O = oleic acid + ethanolamine

0

-

3.5.1.99

anandamide + H2O = arachidonic acid + ethanolamine

0

-

3.5.1.99

anandamide + H2O = ethanolamine + arachidonic acid

0

-

3.5.1.99

N-arachidonoylethanolamine + H2O = arachidonic acid + ethanolamine

0

-

3.5.1.99

N-oleoylethanolamine + H2O = oleic acid + ethanolamine

0

-

3.5.1.99

N-palmitoyl ethanolamine + H2O = palmitic acid + ethanolamine

0

-

3.5.1.99

N-palmitoylethanolamine + H2O = palmitic acid + ethanolamine

0

-

3.5.1.99

palmitoylethanolamide + H2O = palmitic acid + ethanolamine

0

-

3.5.1.60

12 entries

3.5.1.99

8 entries

Substrate in Enzyme-catalyzed Reactions (26 results)

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Show Substrate (26 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

2-aminoethanol + NAD+ = ?

684620

-

1.1.2.8

ethanolamine + phenazine methosulfate = ? + reduced phenazine methosulfate

763417

-

1.1.3.17

monoethanolamine + O2 = aminoacetaldehyde + H2O2

389719

-

1.4.3.21

ethanolamine + H2O + O2 = glycolaldehyde + NH3 + H2O2

725733, 743457

-

1.4.3.4

ethanolamine + H2O + O2 = glycolaldehyde + NH3 + H2O2

724603

-

1.4.3.8

ethanolamine + H2O + O2 = glycolaldehyde + NH3 + H2O2

742141, 391965, 391966, 391967

-

2.1.1.21

ethanolamine + L-glutamate = ?

485236

-

2.1.1.21

N-methyl-L-glutamate + ethanolamine = ?

485236

-

2.1.1.21

2 entries

2.1.4.1

arginine + ethanolamine = 2-guanidinoethanol + ornithine

485972

-

2.7.1.32

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

641357

-

2.7.1.32

ATP + ethanolamine = ADP + ethanolamine phosphate

641381, 641377, 641375, 641385, 672361

-

2.7.1.32

ATP + ethanolamine = ADP + O-phosphoethanolamine

760908

-

2.7.1.32

ATP + ethanolamine = ADP + phosphoethanolamine

722754

-

2.7.1.32

ethanolamine + ATP = ADP + ethanolamine phosphate

641352, 641359, 641368, 641371, 641369

-

2.7.1.32

ethanolamine + ATP = O-phosphoethanolamine + ADP

685011

-

2.7.1.32

ethanolamine + ATP = phosphoethanolamine + ADP

706447

-

2.7.1.82

ATP + ethanolamine = ADP + O-phosphoethanolamine

641346, 642054, 642036, 642040, 641345, 641347, 641348, 641349, 642038, 642056, 641379, 642053, 662250, 674547, 641354, 642041, 642039, 137599, 641355, 738268, 641350, 642052, 739083, 685011, 702145, 674650, 739295, 762164

-

2.7.1.82

GTP + ethanolamine = GDP + O-phosphoethanolamine

641350

-

2.7.1.82

ITP + ethanolamine = IDP + O-phosphoethanolamine

641350

-

2.7.1.32

7 entries

2.7.1.82

3 entries

3.1.4.4

phosphatidylcholine + ethanolamine = phosphatidylethanolamine + choline

135441, 135451, 135449, 135438, 135427, 135428, 135426, 694606

-

4.3.1.2

mesaconate + 2-aminoethanol = ?

730442

-

4.3.1.7

ethanolamine = ?

34383

3abo, 3D-view

4.3.1.7

ethanolamine = ?

34383

3abs, 3D-view

4.3.1.7

ethanolamine = acetaldehyde + NH3

34373, 34383, 34384, 34385, 680355, 680364, 682751, 690960, 691337, 34371, 34377, 34379, 34382, 729253, 34378, 34370, 34372, 34374, 34375, 34376, 34380, 34381, 729228, 662046, 661191, 690905, 690280, 692739, 704362, 747568, 747124

3abo, 3D-view

4.3.1.7

ethanolamine = acetaldehyde + NH3

34373, 34383, 34384, 34385, 680355, 680364, 682751, 690960, 691337, 34371, 34377, 34379, 34382, 729253, 34378, 34370, 34372, 34374, 34375, 34376, 34380, 34381, 729228, 662046, 661191, 690905, 690280, 692739, 704362, 747568, 747124

3abs, 3D-view

4.3.1.7

4 entries

6.3.2.3

ATP + gamma-L-Glu-L-Cys + ethanolamine = ADP + phosphate + gamma-Glu-L-Cys-ethanolamine

661012

-

Product in Enzyme-catalyzed Reactions (77 results)

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Show Product (77 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.8.29

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

0

-

2.7.8.B11

1-(1-heptadecanoyl-2-((9Z)-tetradec-9-enoyl)-sn-glycero-3-phospho)-sn-glycerol + 1-dodecanoyl-2-tridecanoyl-sn-glycero-3-phosphoethanolamine = 1-(1-heptadecanoyl-2-((9Z)-tetradec-9-enoyl)-sn-glycero-3-phospho)-3-(1-dodecanoyl-2-tridecanoyl-sn-glycero-3-phospho)glycerol + ethanolamine

0

-

2.7.8.B11

a phosphatidylglycerol + a phosphatidylethanolamine = a cardiolipin + ethanolamine

0

-

2.7.8.B11

2 entries

3.1.3.1

phosphoethanolamine + H2O = phosphate + ethanolamine

0

-

3.1.3.2

O-phosphoethanolamine + H2O = ethanolamine + phosphate

0

-

3.1.3.2

phosphorylethanolamine + H2O = ethanolamine + phosphate

0

-

3.1.3.75

O-phosphoethanolamine + H2O = ethanolamine + phosphate

0

-

3.1.3.75

phosphoethanolamine + H2O = ethanolamine + phosphate

0

-

3.1.4.2

ethanolamine lysoplasmalogen + H2O = ethanolamine + 1-(1-alkenyl)-sn-glycero-3-phosphate

0

-

3.1.4.2

glycero-3-phosphoethanolamine + H2O = sn-glycerol-3-phosphate + ethanolamine

0

-

3.1.4.2

glycerophosphoethanolamine + H2O = glycerol 1,2-cyclic phosphate + ethanolamine

646468, 81114

-

3.1.4.2

sn-glycero 3-phosphorylethanolamine + H2O = sn-glycerol 3-phosphate + ethanolamine

95138, 95129, 95152, 81114, 95130, 95151

-

3.1.4.2

sn-glycero-3-phosphoethanolamine + H2O = sn-glycerol-3-phosphate + ethanolamine

0

-

3.1.4.39

1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycero-3-phosphate + ethanolamine

208396, 208402

-

3.1.4.39

1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine

0

-

3.1.4.39

1-O-alkyl-2-lyso-sn-glycero-3-phosphoethanolamine + H2O = 1-O-alkyl-2-lyso-sn-glycero-3-phosphate + ethanolamine

650814

-

3.1.4.39

1-O-hexadecyl-2-lyso-sn-glycero-3-phosphoethanolamine + H2O = 1-O-hexadecyl-2-lyso-sn-glycero-3-phosphate + ethanolamine

208397, 208398, 208399, 208402

-

3.1.4.39

lysophosphatidyl ethanolamine + H2O = lysophosphatidic acid + ethanolamine

0

-

3.1.4.4

(2R)-3-{[(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-({12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodecanoyl}oxy)propyl tetradecanoate + H2O = ethanolamine + (2R)-2-({12-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]dodecanoyl}oxy)-3-(phosphonooxy)propyl tetradecanoate

0

-

3.1.4.4

1-myristoyl-2-hydroxy-sn-glycero-3-phosphoethanolamine + H2O = [(4R)-2-hydroxy-2-oxido-1,3,2-dioxaphospholan-4-yl]methyl tetradecanoate + ethanolamine

0

-

3.1.4.4

1-oleoyl-2-stearoylphosphatidylethanolamine + H2O = ethanolamine + 1-oleoyl-2-stearoyl-sn-glycero-3-phosphatidic acid

0

-

3.1.4.4

dioleoylphosphatidylethanolamine + H2O = ethanolamine + 1,2-dioleoyl-sn-glycero-3-phosphatidic acid

0

-

3.1.4.4

N-lauroyl-D-erythrosphingosylphosphoethanolamine + H2O = N-[(4R,5S)-2-hydroxy-2-oxido-4-[(1E)-pentadec-1-en-1-yl]-1,3,2-dioxaphosphinan-5-yl]dodecanamide + ethanolamine

0

-

3.1.4.4

oleoyllysophosphatidylethanolamine + H2O = ethanolamine + 1,2-dioleoyl-sn-glycero-3-phosphatidic acid

0

-

3.1.4.4

phosphatidylethanolamine + H2O = 1,2-diacylglycerophosphate + ethanolamine

0

-

3.1.4.4

phosphatidylethanolamine + H2O = ethanolamine + phosphatidate

651126, 0

-

3.1.4.4

phosphatidylethanolamine + H2O = ethanolamine + phosphatidic acid

0

-

3.1.4.4

phosphatidylethanolamine + H2O = phosphatidate + ethanolamine

0

-

3.1.4.46

glycerophosphoethanolamine + H2O = ethanolamine + glycerol-3-phosphate

0

-

3.1.4.46

glycerophosphoethanolamine + H2O = sn-glycerol 3-phosphate + ethanolamine

646457, 0

-

3.1.4.46

sn-glycero-3-phosphoethanolamine + H2O = ethanolamine + sn-glycerol 3-phosphate

0

-

3.5.1.4

anandamide + H2O = arachidonic acid + ethanolamine

0

-

3.5.1.4

arachidonoyl-ethanolamine + H2O = arachidonic acid + ethanolamine

0

-

3.5.1.4

N-lauroylethanolamine + H2O = lauric acid + ethanolamine

0

-

3.5.1.4

N-oleoyl ethanolamine + H2O = oleic acid + ethanolamine

0

-

3.5.1.4

N-oleoylethanolamine + H2O = oleic acid + ethanolamine

0

-

3.5.1.4

N-palmitolyl ethanolamine + H2O = palmitic acid + ethanolamine

0

-

3.5.1.4

N-palmitoylethanolamine + H2O = palmitic acid + ethanolamine

0

-

3.5.1.4

palmitoylethanolamide + H2O = palmitic acid + ethanolamine

0

-

3.5.1.60

(10Z)-heptadecenoylethanolamide + H2O = (10Z)-heptadec-10-enoic acid + ethanolamine

0

-

3.5.1.60

heptadecenoylethanolamide + H2O = heptadecenoate + ethanolamine

0

-

3.5.1.60

N-alpha-linolenoylethanolamide + H2O = alpha-linoleate + ethanolamine

0

-

3.5.1.60

N-arachidonoylethanolamide + H2O = arachidonate + ethanolamine

0

-

3.5.1.60

N-arachidonoylethanolamine + H2O = arachidic acid + ethanolamine

0

-

3.5.1.60

N-dodecanoylethanolamine + H2O = dodecanoic acid + ethanolamine

209214

-

3.5.1.60

N-eicosapentaenoylethanolamide + H2O = eicosapentanoate + ethanolamine

0

-

3.5.1.60

N-hexadecanoylethanolamine + H2O = hexadecanoic acid + ethanolamine

209214

-

3.5.1.60

N-linoleoylethanolamide + H2O = linoleate + ethanolamine

0

-

3.5.1.60

N-octadecanoylethanolamine + H2O = octadecanoic acid + ethanolamine

209214

-

3.5.1.60

N-oleoylethanolamide + H2O = oleate + ethanolamine

0

-

3.5.1.60

N-oleoylethanolamine + H2O = oleic acid + ethanolamine

209214

-

3.5.1.60

N-palmitoylethanolamide + H2O = palmitate + ethanolamine

0

-

3.5.1.60

N-palmitoylethanolamine + H2O = palmitic acid + ethanolamine

0

-

3.5.1.60

N-stearoylethanolamide + H2O = stearate + ethanolamine

0

-

3.5.1.60

N-tetradecanoylethanolamine + H2O = tetradecanoic acid + ethanolamine

209214

-

3.5.1.60

oleoylethanolamide + H2O = oleate + ethanolamine

0

-

3.5.1.60

oleoylethanolamide + H2O = oleic acid + ethanolamine

0

-

3.5.1.60

palmitoylethanolamide + H2O = palmitate + ethanolamine

0

-

3.5.1.60

palmitoylethanolamide + H2O = palmitic acid + ethanolamine

0

-

3.5.1.99

(9Z)-N-ethyloctadec-9-enamide + H2O = oleic acid + ethanolamine

0

-

3.5.1.99

all-trans-anandamide + H2O = ethanolamine + arachidonic acid

0

-

3.5.1.99

anandamide + H2O = arachidonic acid + ethanolamine

0

-

3.5.1.99

anandamide + H2O = ethanolamine + arachidonic acid

0

-

3.5.1.99

arachidonoyl ethanolamide + H2O = arachidonic acid + ethanolamine

0

-

3.5.1.99

N-arachidonoylethanolamine + H2O = arachidonic acid + ethanolamine

0

-

3.5.1.99

N-oleoylethanolamine + H2O = oleic acid + ethanolamine

0

-

3.5.1.99

N-palmitoyl ethanolamine + H2O = palmitic acid + ethanolamine

0

-

3.5.1.99

N-palmitoylethanolamine + H2O = palmitic acid + ethanolamine

0

-

3.5.1.99

oleoyl ethanolamide + H2O = oleic acid + ethanolamine

0

-

3.5.1.99

oleoylethanolamide + H2O = oleic acid + ethanolamine

0

-

3.5.1.99

palmitoylethanolamide + H2O = palmitic acid + ethanolamine

0

-

3.1.3.2

2 entries

3.1.3.75

2 entries

3.1.4.2

5 entries

3.1.4.39

5 entries

3.1.4.4

10 entries

3.1.4.46

3 entries

3.5.1.4

8 entries

3.5.1.60

20 entries

3.5.1.99

12 entries

3.5.4.42

N-hydroxyethylammelide + H2O = cyanuric acid + 2-aminoethanol

651707

-

3.6.1.1

2-phosphorylethanolamine + H2O = ethanolamine + phosphate

0

-

3.8.1.8

2-hydroxy-4,6-di(N-hydroxyethylamino)-1,3,5-triazine + H2O = 6-[(2-hydroxyethyl)amino]-1,3,5-triazine-2,4-diol + 2-aminoethanol

0

-

4.3.1.7

acetaldehyde + NH3 = ethanolamine

0

3abo, 3D-view

4.3.1.7

acetaldehyde + NH3 = ethanolamine

0

3abs, 3D-view

4.3.1.7

2 entries

4.4.1.11

DL-2-amino-3-(N-hydroxyethylamino)-propionic acid = ethanolamine + NH3 + pyruvate

34516

-

Activator in Enzyme-catalyzed Reactions (7 results)

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Show Activating Compound (7 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.3

alphaH44A mutant, works as catalytic base

348600

-

2.1.3.2

activates

485860

-

2.7.13.3

induces a 15fold increase in the rate of autophosphorylation in vitro of the HK17 sensor histidine kinase

692882

-

3.1.1.3

234% activation of recombinant refolded enzyme at 30% v/v, 37% at 10% v/v

666825

-

3.1.8.2

-

751964

-

4.1.1.40

activates

4542

-

5.4.3.8

stimulates activity of mutant enzyme Lys265Arg

3432

-

Inhibitor in Enzyme-catalyzed Reactions (39 results)

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Show Inhibitors (39 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.13

1 mM, 70% inhibition

484911

-

1.1.99.1

-

389886

-

1.2.1.8

100 mM, 35% inhibition

390329

-

1.4.3.10

-

395447

-

1.4.3.10

competitive inhibitor

684634

-

1.4.3.10

2 entries

2.1.1.156

45% inhibition at 250 mM, with glycine

659286

-

2.3.1.13

about 37% inhibition at 100 mM

737197

-

2.3.1.37

-

486820, 486860

-

2.3.2.13

-

657887

-

2.3.2.5

-

671982

-

2.4.1.140

-

488584

-

2.7.1.32

-

641368, 641370

-

2.7.1.32

inhibition only at very high concentration, 100-150 mM

641369

-

2.7.1.32

no significant effect

641358

-

2.7.1.32

poor inhibitor

672361

-

2.7.1.32

weak

641372

-

2.7.1.32

weak competitive inhibitor

641345, 641347

-

2.7.1.81

-

642035

-

2.7.1.81

40 mM, weak inhibition

642034

-

2.7.1.32

6 entries

2.7.1.81

2 entries

3.1.4.2

-

95151

-

3.2.1.10

about 70% inhibition of isomaltase activity by 50 mM

136520

-

3.2.1.106

-

170961

-

3.2.1.23

-

171271

-

3.2.1.33

-

171379

-

3.2.1.37

-

707563

-

3.2.1.48

-

136520

-

3.2.1.51

strong inhibition

208730

-

3.4.21.112

supresses cleavage by dS1P

709081

-

3.4.24.75

inhibits enzyme binding to the cell surface, leading to low enzyme activity, despite retention of its secondary structure. At pH 10.5 (but not at pH 7.5), methanolamine strongly deactivates the enzyme in a concentration-dependent manner

752549

-

3.5.1.93

-

756424

-

4.2.1.27

-

644460

-

4.2.1.84

markedly lower activity

676087

-

4.3.1.15

-

6046

-

4.3.1.17

-

210775, 210794

-

4.3.1.7

10 mM

34379

3abo, 3D-view

4.3.1.7

10 mM

34379

3abs, 3D-view

4.3.1.7

2 entries

6.3.1.6

weak

958

-

6.3.2.11

10 mM, 17% loss of activity

988

-

6.3.4.19

-

704642

-

3D Structure of Enzyme-Ligand-Complex (PDB) (9 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (9 entries)

EC NUMBER

ENZYME 3D STRUCTURE

3.8.1.5

7o3o, 3D-view

4.3.1.7

3abo, 3D-view

4.3.1.7

3abs, 3D-view

4.3.1.7

3abo, 3D-view

4.3.1.7

3abs, 3D-view

4.3.1.7

3abo, 3D-view

4.3.1.7

3abs, 3D-view

4.3.1.7

3abo, 3D-view

4.3.1.7

3abs, 3D-view

4.3.1.7

8 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (28 results)

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Show Turnover Number (28 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.4.3.21

3.3

-

isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

2.7.1.82

0.00016

-

-

642040

2.7.1.82

6.56

-

pH 7.8

685011

2.7.1.82

12.9

-

pH 7.8

685011

4.3.1.7

0.036

-

run 1, pH 8, 37°C, mutant E287A

729253

4.3.1.7

0.038

-

run 2, pH 8, 37°C, mutant D362N

729253

4.3.1.7

0.051

-

run 2, pH 8, 37°C, mutant Q162K

729253

4.3.1.7

0.066

-

run 2, pH 8, 37°C, mutant E287H

729253

4.3.1.7

0.085

-

run 1, pH 8, 37°C, mutant D362A

729253

4.3.1.7

0.086

-

run 2, pH 8, 37°C, mutant E287Q

729253

4.3.1.7

0.67

-

run 2, pH 8, 37°C, mutant D362E

729253

4.3.1.7

1

-

run 1, pH 8, 37°C, mutant R160A

729253

4.3.1.7

1.3

-

run 1, pH 8, 37°C, mutant N193A

729253

4.3.1.7

2.1

-

run 2, pH 8, 37°C, mutant E287D

729253

4.3.1.7

3

6

run 2, pH 8, 37°C, mutant N193D

729253

4.3.1.7

6

-

run 2, pH 8, 37°C, mutant Q162H

729253

4.3.1.7

8.5

-

R160K EAL

690960

4.3.1.7

16.7

-

reconstituted EAL (from EutB and EutC subunits), pH 7.5, 25°C

729228

4.3.1.7

20

-

run 1, pH 8, 37°C, mutant Q162A

729253

4.3.1.7

22

-

at 0°C

692739

4.3.1.7

22.7

-

purified EAL, pH 7.5, 25°C

729228

4.3.1.7

30

-

-

680355

4.3.1.7

52.2

-

wild-type

690960

4.3.1.7

55

-

at 22 °C

692739

4.3.1.7

79

-

run 2, pH 8, 37°C, mutant R160K

729253

4.3.1.7

110

-

run 2, pH 8, 37°C, mutant Q162E

729253

4.3.1.7

440

-

run 2, pH 8, 37°C, wild-type

729253

4.3.1.7

770

-

run 1, pH 8, 37°C, wild-type

729253

2.7.1.82

3 entries

4.3.1.7

24 entries

K_M Value (51 results)

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Show KM Value (51 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.3.21

2.05

-

isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

1.4.3.4

2

-

at pH 7.0 and 37°C

724603

1.4.3.8

0.16

-

-

391967

1.4.3.8

5

-

-

391965, 391966

2.1.4.1

163

-

-

485972

2.1.4.1

171

-

beta-transamidinase

485972

2.1.4.1

174

-

alpha-transamidinase

485972

2.1.4.1

450

-

beta-transamidinase

485972

2.7.1.32

-999

-

above 500 mM

702145

2.7.1.32

0.787

-

30°C

641371

2.7.1.32

0.787

-

30°C, pH 8.0

641359

2.7.1.32

1.2

-

30°C

641371

2.7.1.32

1.2

-

30°C, pH 8.0

641359

2.7.1.32

1.2

-

pH 8.5, 37°C

641370

2.7.1.32

2.01

-

-

706447

2.7.1.32

2.56

-

-

685011

2.7.1.32

5

-

in 100 mM Tris/HCl, 6 mM MgCl2, 5 mM ATP, pH 8.8, at 37°C

672361

2.7.1.32

8.1

-

pH 9.0

641352

2.7.1.32

12.01

-

-

706447

2.7.1.32

75

-

at pH 9.0 and 37°C

760908

2.7.1.82

0.008

-

pH 8.5

642039

2.7.1.82

0.0184

-

pH 7.8

685011

2.7.1.82

0.041

-

30°C, pH 9.0

642056

2.7.1.82

0.042

-

-

642041

2.7.1.82

0.1

-

37°C, pH 8.5

642038

2.7.1.82

0.171

-

30°C, pH 8.5

642053

2.7.1.82

0.25

-

37°C, pH 8.5

642040

2.7.1.82

0.458

-

pH 8.0, 37°C

702145

2.7.1.82

0.4757

-

-

702145

2.7.1.82

0.53

-

-

137599

2.7.1.82

2.56

-

pH 7.8

685011

2.7.1.82

7.7

-

-

641347

2.7.1.82

10

-

-

641379

4.3.1.7

-999

-

truncated enzymes, value between 0.0059 and 0.0076

704362

4.3.1.7

0.0019

-

-

680355

4.3.1.7

0.0033

-

run 2, pH 8, 37°C, wild-type

729253

4.3.1.7

0.0082

-

wild-type enzyme

704362

4.3.1.7

0.0136

-

wild-type

690960

4.3.1.7

0.022

-

-

34370, 34375

4.3.1.7

0.022

-

reconstituted EAL (from EutB and EutC subunits), pH 7.5, 25°C

729228

4.3.1.7

0.029

-

-

34376

4.3.1.7

0.03

-

pH 7

34382

4.3.1.7

0.0316

-

purified EAL, pH 7.5, 25°C

729228

4.3.1.7

0.2

-

-

34371, 34379

4.3.1.7

0.21

-

run 2, pH 8, 37°C, mutant N193D

729253

4.3.1.7

0.21

-

run 2, pH 8, 37°C, mutant R160K

729253

4.3.1.7

0.22

-

run 2, pH 8, 37°C, mutant Q162H

729253

4.3.1.7

0.3

-

pH 5.8

34382

4.3.1.7

0.41

-

R160K EAL shows a 30fold increase relative to wild-type enzyme

690960

4.3.1.7

0.73

-

run 2, pH 8, 37°C, mutant Q162E

729253

4.3.1.7

1

2

-

34379

1.4.3.8

2 entries

2.1.4.1

4 entries

2.7.1.32

12 entries

2.7.1.82

13 entries

4.3.1.7

18 entries

K_i Value (9 results)

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Show KI Value (9 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.8

78

-

-

390329

1.4.3.10

0.0018

-

wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C

684634

1.4.3.10

3

-

-

395447

1.4.3.10

2 entries

2.3.2.13

2.2

9

pH 8.0, 37°C

657887

2.3.2.5

19.3

-

-

671982

2.7.1.32

2

-

pH 8.5, 37°C

641370

2.7.1.32

5.5

-

in 100 mM Tris/HCl, 6 mM MgCl2, 5 mM ATP, pH 8.8, at 37°C

672361

3.2.1.37

0.7

-

substrate 4-nitrophenyl-beta-D-xylopyranoside, 25°C, pH 7.0

707563

3.2.1.37

0.92

-

substrate 4-nitrophenyl-alpha-L-arabinofuranoside, 25°C, pH 7.0

707563

2.7.1.32

2 entries

3.2.1.37

2 entries

IC₅₀ Value (1 result)

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Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

6.3.4.19

1.77

-

pH 8.5, 21°C

704642

References & Links

Literature References (154)

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Show Reference (154 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

958

-

Some properties of the theanine synthesizing enzyme in tea seedlings

1965

Sasaoka, K.; Kito, M.; Onishi, Y.

Agric. Biol. Chem.

29

984-988

988

-

Inhibition of carnosine synthetase by spermidine

1982

Seely, J.E.; Marshall, F.D.

Pept. Antibiot. Biosynth. Funct. (Kleinkauf H. et al. eds. )

-

347-352

3432

1643048

Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R

1992

Ilag, L.L.; Jahn, D.

Biochemistry

31

7143-7151

4542

14186730

Nonoxidative decarboxylation of hydroxypyruvate in mammalian systems

1964

Hedrick, J.L.; Sallach, H.J.

Arch. Biochem. Biophys.

105

261-269

6046

3275662

Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification and characterization of the crystalline enzyme and sequence determination of the pyridoxal 5'-phosphate binding peptide

1988

Nagasawa, T.; Tanizawa, K.; Satoda, T.; Yamada, H.

J. Biol. Chem.

263

958-964

34370

-

Ethanolamine deaminase (Clostridium sp.)

1971

Kaplan, B.H.; Stadtman, E.R.

Methods Enzymol.

17B

818-824

34371

784902

Microbial metabolism of amino alcohols. Ethanolamine catabolism mediated by coenzyme B12-dependent ethanolamine ammonia-lyase in Escherichia coli and Klebsiella aerogenes

1976

Scarlett, F.A.; Turner, J.M.

J. Gen. Microbiol.

95

173-176

34372

7341225

The substrate-dependent steric course of the ethanolamine ammonia-lyase reaction

1980

Diziol, P.; Haas, H.; Retey, J.; Graves, S.W.; Babior, B.M.

Eur. J. Biochem.

106

211-224

34373

9250987

Use of magnetic field effects to study coenzyme B12-dependent reactions

1997

Grissom, C.B.; Natarajan, E.

Methods Enzymol.

281

235-247

34374

3905806

The mechanism of action of ethanolamine ammonia-lyase, an adenosylcobalamin-dependent enzyme. Evidence that the hydrogen transfer mechanism involves a second intermediate hydrogen carrier in addition to the cofactor

1985

O'Brien, R.J.; Fox, J.A.; Kopczynski, M.G.; Babior, B.M.

J. Biol. Chem.

260

16131-16136

34375

4297225

Ethanolamine deaminase, a cobamide coenzyme-dependent enzyme. I. Purification, assay, and properties of the enzyme

1968

Kaplan, B.H.; Stadtman, E.R.

J. Biol. Chem.

243

1787-1793

34376

5846988

The clostridial fermentations of choline and ethanolamine. II. Requirement for a cobamide coenzyme by an ethanolamine deaminase

1965

Bradbeer, C.

J. Biol. Chem.

240

4675-4681

34377

-

The adenosylcobalamin-dependent ethanolamine ammonia-lyase of Escherichia coli

1981

Pennington, S.J.; Jones, P.W.; Turner, J.M.

Biochem. Soc. Trans.

9

447

34378

8069783

Sequence of Rhodococcus gene cluster encoding the subunits of ethanolamine ammonia-lyase and an APC-like permease

1994

De Mot, R.; Nagy, I.; Schoofs, G.; Vanderleyden, J.

Can. J. Microbiol.

40

403-407

34379

793895

Ethanolamine catabolism by bacteria, including Escherichia coli

1976

Blackwell, C.M.; Scarlett, F.A.; Turner, J.M.

Biochem. Soc. Trans.

4

495-497

34380

186123

Coenzyme B-12-dependent reactions. Part IV. Observations on the purification of ethanolamine ammonia-lyase

1976

Joblin, K.N.; Johnson, A.W.; Lappert, M.F.; Wallis, O.C.

Biochim. Biophys. Acta

452

262-270

34381

761617

Studies on the subunit structure of the adenosylcobalamin-dependent enzyme ethanolamine ammonia-lyase

1979

Wallis, O.C.; Johnson, A.W.; Lappert, M.F.

FEBS Lett.

97

196-199

34382

33657

Microbial metabolism of amino alcohols. Purification and properties of coenzyme B12-dependent ethanolamine ammonia-lyase of Escherichia coli

1978

Blackwell, C.M.; Turner, J.M.

Biochem. J.

175

555-563

34383

3045078

Ethanolamine utilization in Salmonella typhimurium

1988

Roof, D.M.; Roth, J.R.

J. Bacteriol.

170

3855-3863

34384

1550360

Overexpression, purification, and some properties of the AdoCbl-dependent ethanolamine ammonia-lyase from Salmonella typhimurium

1992

Faust, L.P.; Babior, B.M.

Arch. Biochem. Biophys.

294

50-54

34385

2197274

Cloning, sequencing, and expression of the genes encoding the adenosylcobalamin-dependent ethanolamine ammonia-lyase of Salmonella typhimurium

1990

Faust, L.R.; Connor, J.A.; Roof, D.M.; Hoch, J.A.; Babior, B.M.

J. Biol. Chem.

265

12462-12466

34516

-

The C3-N bond cleavage of 2-amino-3-(N-substituted-amino)-propionic acids catalyzed by L-mehtionine gamma-lyase

1988

Takada, H.; Esaki, N.; Tanaka, H.; Soda, K.

Agric. Biol. Chem.

52

2897-2901

81114

182119

Enzymic formation of glycerol 1:2-cyclic phosphate

1976

Clarke, N.; Dawson, R.M.C.

Biochem. J.

153

745-747

95129

8614297

Multiple forms of the enzyme glycerophosphodiesterase are present in human brain

1995

Ross, B.M.; Sherwin, A.L.; Kish, S.J.

Lipids

30

1075-1081

95130

8529026

Evolutionary comparison of enzyme activities of phosphatidylcholine metabolism in the nervous system of an invertebrate (Loligo pealei), lower vertebrate (Mustelus canis) and the rat

1995

Anfuso, C.D.; Sipione S.; Lupo, G.; Alberghina, M.

Comp. Biochem. Physiol. B

112

493-501

95138

2829735

Purification and characterization of glpQ-encoded glycerophosphodiester phosphodiesterase from Escherichia coli K-12

1988

Larson, T.J.; van Loo-Bhattacharya, A.T.

Arch. Biochem. Biophys.

260

577-584

95151

4305487

Rat kidney glycerylphosphorylcholine diesterase

1968

Baldwin, J.J.; Cornatzer, W.E.

Biochim. Biophys. Acta

164

195-204

95152

13143024

Metabolism of phospholipides by bacterial enzymes

1954

Hayaishi, O.; Kornberg, A.

J. Biol. Chem.

206

647-663

135426

-

Phospholipase D from savoy cabbage

1969

Yang, S.F.

Methods Enzymol.

14

208-210

135427

3688883

Purification of phospholipase D from citrus callus tissue

1987

Witt, W.; Yelenosky, G.; Mayer, R.T.

Arch. Biochem. Biophys.

259

164-170

135428

-

Purification and properties of phospholipase D from Actinomadura sp.strain no.362

1987

Kokusho, Y.; Kato, S.; Machida, H.; Iwasaki, S.

Agric. Biol. Chem.

51

2515-2524

135438

4642213

Purification of phospholipase D from peanuts

1972

Tzur, R.; Shapiro, B.

Biochim. Biophys. Acta

280

290-296

135441

7548180

Characterization and partial purification of phospholipase D from human placenta

1995

Vinggaard, A.M.; Hansen, H.S.

Biochim. Biophys. Acta

1258

169-176

135449

7983063

Purification and characterization of phosphatidylcholine phospholipase D from pig lung

1994

Okamura, S.; Yamashita, S.

J. Biol. Chem.

269

31207-31213

135451

9346296

Characteristics of protein-kinase-C- and ADP-ribosylation-factor-stimulated phospholipase D activities in human embryonic kidney cells

1997

Rumenapp, U.; Schmidt, M.; Wahn, F.; Tapp, E.; Grannass, A.; Jakobs, K.H.

Eur. J. Biochem.

248

407-414

136520

8924896

Inhibition of purified human sucrase and isomaltase by ethanolamine derivatives

1996

Kano, T.; Usami, Y.; Adachi, T.; Tatematsu, M.; Hirano, K.

Biol. Pharm. Bull.

19

341-344

137599

-

Phosphorylation of ethanolamine in catabolism. Biodegradative adenosine triphosphate-ethanolamine phosphotransferase and related enzymes in bacteria

1974

Faulkner, A.; Turner, J.M.

Biochem. Soc. Trans.

2

133-136

170961

3521492

Purification and properties of glucosidase I from mung bean seedlings

1986

Szumilo, T.; Kaushal, G.P.; Elbein, A.D.

Arch. Biochem. Biophys.

247

261-271

171271

-

beta-Galactosidase

1972

Wallenfels, K.; Weil, R.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

7

617-663

171379

5805288

Purification and properties of rabbit muscle amylo-1,6-glucosidase-oligo-1,4->1,4-transferase

1969

Nelson, T.E.; Kolb, E.; Larner, J.

Biochemistry

8

1419-1428

208396

3632787

Involvement of lysophospholipase D in the production of lysophosphatidic acid in rat plasma

1986

Tokumura, A.; Harada, K.; Fukazawa, K.; Tsukatani, H.

Biochim. Biophys. Acta

875

31-38

208397

7417469

Specificity of lysophospholipase D

1980

Wykle, R.L.; Kraemer, W.F.; Schremmer, J.M.

Biochim. Biophys. Acta

619

58-67

208398

597368

Studies of lysophospholipase D of rat liver and other tissues

1977

Wykle, R.L.; Kraemer, W.F.; Schremmer, J.M.

Arch. Biochem. Biophys.

184

149-155

208399

4855486

A lysophospholipase D pathway in the metabolism of ether-linked lipids in brain microsomes

1974

Wykle, R.L.; Schremmer, J.M.

J. Biol. Chem.

249

1742-1746

208402

1646942

Lysophospholipase D

1991

Wykle, L.; Strum, J.C.

Methods Enzymol.

197

583-590

208730

96860

The purification, properties and characterization of three forms of alpha-L-fucosidase from monkey brain

1978

Alam, T.; Balasubramanian, A.S.

Biochim. Biophys. Acta

524

373-384

209214

4055775

Properties of rat liver N-acylethanolamine amidohydrolase

1985

Schmid, P.C.; Zuzarte-Augustin, M.L.; Schmid, H.H.O.

J. Biol. Chem.

260

14145-14149

210775

7011505

In vitro studies on L-serine deaminase activity of Escherichia coli K12

1980

Newman, E.B.; Kapoor, V.

Can. J. Biochem.

58

1292-1297

210794

2065681

Purification and properties of an iron-sulfur containing and pyridoxal-phosphate-independent L-serine dehydratase from Peptostreptococcus asaccharolyticus

1991

Grabowski, R.; Buckel, W.

Eur. J. Biochem.

199

89-94

348600

9402752

Identification and Characterization of a catalytic base in bacterial luciferase by chemical rescue of a dark mutant

1997

Huang, S.; Tu, S.C.

Biochemistry

36

14609-14615

389719

-

Properties of choline oxidase of cylindrocarpon didymum M-1

1979

Yamada, H.; Mori, N.; Tani, Y.

Agric. Biol. Chem.

43

2173-2177

389886

6996732

A novel purification and some properties of rat liver mitochondrial choline dehydrogenase

1980

Tsuge, H.; Nakano, Y.; Onishi, H.; Futamura, Y.; Ohashi, K.

Biochim. Biophys. Acta

614

274-284

390329

2194570

Purification and characterization of osmoregulatory betaine aldehyde dehydrogenase of Escherichia coli

1990

Falkenberg, P.; Strom, A.R.

Biochim. Biophys. Acta

1034

253-259

391965

-

Ethanolamine oxidase

1966

Narrod, S.A.; Jakoby, W.B.

Methods Enzymol.

8

354-357

391966

14209947

Metabolism of ethanolamine, an ethanoloxidase

1964

Narrod, S.A.; Jakoby, W.B.

J. Biol. Chem.

239

2189-2193

391967

4709585

Ethanolamine oxidase from the blowfly, Phormia regina (Diptera: Insecta)

1973

Kulkarni, A.P.; Hodgson, E.

Comp. Biochem. Physiol. B

44

407-422

395447

1260033

Mechanism of action of putrescine oxidase. Binding characteristics of the active site of putrescine oxidase from Micrococcus rubens

1976

Swain, W.F.; Desa, R.J.

Biochim. Biophys. Acta

429

331-341

484911

7030206

Microbial oxidation of methanol: properties of crystallized alcohol oxidase from a yeast, Pichia sp

1981

Patel, R.N.; Hou, C.T.; Laskin, A.I.; Derelanko, P.

Arch. Biochem. Biophys.

210

481-488

485236

3911004

N-Methyl-L-glutamate synthase

1985

Hersh, L.B.

Methods Enzymol.

113

36-42

485860

4204271

Aspartate transcarbamylase from Streptococcus faecalis. Purification, properties, and nature of an allosteric activator site

1974

Chang, T.Y.; Jones, M.E.

Biochemistry

13

629-638

485972

8035648

Synthesis of neuroactive guanidino compounds by rat kidney L-arginine:glycine amidinotransferase

1994

Watanabe, Y.; Van Pilsum, J.F.; Yokoi, I.; Mori, A.

Life Sci.

55

351-358

486820

-

delta-Aminolevulinic acid synthetase

1972

Jordan, P.M.; Shemin, D.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

7

339-356

486860

12119044

Involvement of delta-aminolevulinate synthase encoded by the parasite gene in de novo heme synthesis by Plasmodium falciparum

2002

Varadharajan, S.; Dhanasekaran, S.; Bonday, Z.Q.; Rangarajan, P.N.; Padmanaban, G.

Biochem. J.

367

321-327

488584

7060056

Isolation and partial characterization of an extracellular glucansucrase from Leuconostoc mesenteroides NRRL B-1355 that synthesizes an alternating (1-6),(1-3)-alpha-D-glucan

1982

Cote, G.L.; Robyt, J.F.

Carbohydr. Res.

101

57-74

641345

2992596

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