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Information on EC 2.7.1.82 - ethanolamine kinase
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2.7.1.82 ethanolamine kinaseSpecify your search results
Word Map
- 2.7.1.82
- choline
- phosphatidylethanolamine
- phosphoethanolamine
- cdp-ethanolamine
- phosphocholine
-
kennedy
-
ptdetn
- cdp-choline
-
setbp1
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ethanolamine kinase, etnk1, etnk2, etn kinase, ethanolamine kinase 1, ethanolamine kinase 2, treki1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EKI
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-
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EKI1
ethanolamine phosphokinase
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-
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Etn kinase
EtnK
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-
-
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kinase, ethanolamine (phosphorylating)
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-
-
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Treki1
additional information
EKI1
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-
-
-
additional information
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choline kinase and ethanolamine kinase activities are mediated by 2 distinct active sites, possibly on a single protein
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
choline kinase and ethanolamine kinase may not have a common active site in a single enzyme protein
additional information
-
ethanolamine kinase II and choline kinase do not use a common active site
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + ethanolamine = ADP + O-phosphoethanolamine
-
-
-
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ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase are 2 distinct enzymes
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ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
ethanolamine kinase II and choline kinase do not use a common active site
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ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase may not have a common active site in a single enzyme protein
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
choline kinase and ethanolamine kinase activities are mediated by 2 distinct active sites, possibly on a single protein
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ATP + ethanolamine = ADP + O-phosphoethanolamine
major part of choline kinase and ethanolamine kinase activities are catalyzed by the same enzyme
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP:ethanolamine O-phosphotransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9075-78-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 4-aminobutan-1-ol
ADP + 4-aminobutyl 1-phosphate
60% of the activity with choline
-
-
?
choline + ATP
ADP + O-phosphocholine
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ethanolamine kinase II, not ethanolamine kinase I
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-
?
GTP + ethanolamine
GDP + O-phosphoethanolamine
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13% of the activity with ATP
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-
?
ITP + ethanolamine
IDP + O-phosphoethanolamine
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45% of the activity with ATP
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-
?
ATP + (R)-1-aminopropan-2-ol
ADP + (R)-1-aminopropyl 2-phosphate
52.4% of the activity with ethanolamine
-
-
?
ATP + (R)-1-aminopropan-2-ol
ADP + (R)-1-aminopropyl 2-phosphate
7.2% of the activity with choline
-
-
?
ATP + (R)-2-aminobutan-1-ol
ADP + (R)-2-aminobutyl phosphate
102% of the activity with ethanolamine
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-
?
ATP + (R)-2-aminobutan-1-ol
ADP + (R)-2-aminobutyl phosphate
130% of the activity with choline
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-
?
ATP + (R)-2-aminopropan-1-ol
ADP + (R)-2-aminopropyl phosphate
108% of the activity with ethanolamine
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-
?
ATP + (R)-2-aminopropan-1-ol
ADP + (R)-2-aminopropyl phosphate
110% of the activity with choline
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-
?
ATP + (S)-1-aminopropan-2-ol
ADP + (S)-1-aminopropyl 2-phosphate
1.4% of the activity with choline
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-
?
ATP + (S)-1-aminopropan-2-ol
ADP + (S)-1-aminopropyl 2-phosphate
6.1% of the activity with ethanolamine
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-
?
ATP + (S)-2-aminobutan-1-ol
ADP + (S)-2-aminobutyl phosphate
114% of the activity with ethanolamine
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-
?
ATP + (S)-2-aminobutan-1-ol
ADP + (S)-2-aminobutyl phosphate
41% of the activity with choline
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-
?
ATP + (S)-2-aminopropan-1-ol
ADP + (S)-2-aminopropyl phosphate
22.4% of the activity with choline
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?
ATP + (S)-2-aminopropan-1-ol
ADP + (S)-2-aminopropyl phosphate
94% of the activity with ethanolamine
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?
ATP + 2-amino-2-methylpropan-1-ol
ADP + 2-amino-2-methylpropan-1-ol phosphate
25.6% of the activity with ethanolamine
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-
?
ATP + 2-amino-2-methylpropan-1-ol
ADP + 2-amino-2-methylpropan-1-ol phosphate
46% of the activity with choline
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-
?
ATP + 3-aminopropan-1-ol
ADP + 3-aminopropyl 1-phosphate
37.5% of the activity with ethanolamine
-
-
?
ATP + 3-aminopropan-1-ol
ADP + 3-aminopropyl 1-phosphate
44.5% of the activity with choline
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-
?
ATP + diethanolamine
ADP + O2-[(2-hydroxyethyl)amino]ethyl phosphate
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139% of the activity with choline
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?
ATP + diethanolamine
ADP + O2-[(2-hydroxyethyl)amino]ethyl phosphate
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88% of the activity with ethanolamine
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?
ATP + DL-1-aminopropan-2-ol
ADP + DL-1-aminopropane 2-phosphate
Flavobacterium rhenanum
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-
-
-
?
ATP + DL-1-aminopropan-2-ol
ADP + DL-1-aminopropane 2-phosphate
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-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
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?
ATP + ethanolamine
ADP + O-phosphoethanolamine
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?
ATP + ethanolamine
ADP + O-phosphoethanolamine
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the enzyme and the phospholipid phosphatidylethanolamine biosynthesis are regulated by inositol, Kennedy pathway overview
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?
ATP + ethanolamine
ADP + O-phosphoethanolamine
33% of the activity with choline
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?
ATP + N,N-diethylethanolamine
ADP + N,N-diethyl-O-phosphoethanolamine
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156% of the activity with choline
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?
ATP + N,N-diethylethanolamine
ADP + N,N-diethyl-O-phosphoethanolamine
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47% of the activity with ethanolamine
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?
ATP + N,N-dimethylethanolamine
ADP + N,N-dimethyl-O-phosphoethanolamine
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153% of the activity with choline
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?
ATP + N,N-dimethylethanolamine
ADP + N,N-dimethyl-O-phosphoethanolamine
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76% of the activity with ethanolamine
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?
ATP + N-ethylethanolamine
ADP + N-ethyl-O-phosphoethanolamine
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150% of the activity with choline
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?
ATP + N-ethylethanolamine
ADP + N-ethyl-O-phosphoethanolamine
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97% of the activity with ethanolamine
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?
ATP + N-methylethanolamine
ADP + N-methyl-O-phosphoethanolamine
106% of the activity with ethanolamine
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?
ATP + N-methylethanolamine
ADP + N-methyl-O-phosphoethanolamine
135% of the activity with choline
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?
additional information
?
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bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function
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?
additional information
?
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enzyme CEK4 is a bifunctional choline/ethanolamine kinase
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?
additional information
?
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the enzyme controls neuroblast divisions in Drosophila melanogaster mushroom bodies
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?
additional information
?
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Flavobacterium rhenanum
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bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function
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?
additional information
?
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rate-controlling step in phosphatidylethanolamine biosynthesis
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?
additional information
?
-
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rate-controlling step in phosphatidylethanolamine biosynthesis
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?
additional information
?
-
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bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + ethanolamine
ADP + O-phosphoethanolamine
-
the enzyme and the phospholipid phosphatidylethanolamine biosynthesis are regulated by inositol, Kennedy pathway overview
-
-
?
additional information
?
-
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bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function
-
-
?
additional information
?
-
enzyme CEK4 is a bifunctional choline/ethanolamine kinase
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-
?
additional information
?
-
-
the enzyme controls neuroblast divisions in Drosophila melanogaster mushroom bodies
-
-
?
additional information
?
-
Flavobacterium rhenanum
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bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function
-
-
?
additional information
?
-
rate-controlling step in phosphatidylethanolamine biosynthesis
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?
additional information
?
-
-
rate-controlling step in phosphatidylethanolamine biosynthesis
-
-
?
additional information
?
-
-
bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
Zn2+
-
100% activity in the presence of 0.0015 mM Zn2+, depletion of zinc from the growth medium of wild type cells causes a 2fold increase in ethanolamine kinase activity when compared with cells grown in the presence of zinc
Mg2+
-
absolute requirement for Mg2+ and Mn2+, Mg2+ is the most active divalent cation at concentrations above 5 mM, optimum: 18 mM, Mn2+ has a greater stimulatory effect on the enzyme than Mg2+ at levels less than 5 mM, presence of Mn2+ at lower concentrations of Mg2+ has an additive effect, at higher concentrations of Mg2+, Mn2+ inhibits
Mg2+
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Km MgATP2-: 10 mM, in presence of equivalent amounts of ATP and Mg2+
Mg2+
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1.25-2.5 mM ATP: reaction requires free Mg2+ rather than an ATP-Mg2+ complex for maximal velocity
Mg2+
-
ethanolamine kinase I: uses MgATP2- as substrate but also has an additional requirement for Mg2+
Mg2+
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ethanolamine kinase II: requires MgATP2- as substrate, maximal activation with 10 mM of Mg2+ and ATP
Mg2+
-
requires equimolar concentrations of Mg2+ and ATP (30 mM) for optimal activation
Mn2+
-
absolute requirement for Mg2+ and Mn2+, Mg2+ is the most active divalent cation at concentrations above 5 mM, optimum: 18 mM, Mn2+ has a greater stimulatory effect on the enzyme than Mg2+ at levels less than 5 mM, presence of Mn2+ at lower concentrations of Mg2+ has an additive effect, at higher concentrations of Mg2+, Mn2+ inhibits
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,3'-dodecane-1,12-diylbis[5-(2-hydroxyethyl)-4-methyl-1,3-thiazol-3-ium]
SAR97276
Inositol
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decreases gene EKI1 expression, involving the transcription factors Ino2p, Ino4p, and Opi1p, the UASINO element of the EKI promotor is required for the repressive regulation, the inhibitory effect on the enzyme is correlated with a decrease of ethanolamine incorporation into CDP-ethanolamine pathway intermediates and into phosphatidylethanolamine and phosphatidylcholine
SAR97276
bis-thiazolium compound designed as a choline analogue, affects ethanolamine kinase and choline kinase activities similarly. Inhibition is competitive and correlates with the impairment of cellular phosphatidylcholine biosynthesis
2-amino-1-butanol
analogue of ethanolamine, selective inhibition