Information on EC 2.7.1.82 - ethanolamine kinase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.7.1.82
-
RECOMMENDED NAME
GeneOntology No.
ethanolamine kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + ethanolamine = ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
show the reaction diagram
choline kinase and ethanolamine kinase may not have a common active site in a single enzyme protein
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
show the reaction diagram
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
show the reaction diagram
ethanolamine kinase II and choline kinase do not use a common active site
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
show the reaction diagram
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
show the reaction diagram
choline kinase and ethanolamine kinase activities are mediated by 2 distinct active sites, possibly on a single protein
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
show the reaction diagram
choline kinase and ethanolamine kinase are 2 distinct enzymes
-
ATP + ethanolamine = ADP + O-phosphoethanolamine
show the reaction diagram
major part of choline kinase and ethanolamine kinase activities are catalyzed by the same enzyme
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phopho group transfer
Q8IIB7
-
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
choline biosynthesis I
-
Glycerophospholipid metabolism
-
Metabolic pathways
-
phosphatidylethanolamine biosynthesis II
-
SYSTEMATIC NAME
IUBMB Comments
ATP:ethanolamine O-phosphotransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
EKI
-
-
-
-
EKI1
-
-
-
-
ethanolamine kinase
Q8IIB7
-
ethanolamine kinase 2
-
-
ethanolamine phosphokinase
-
-
-
-
EtnK
-
-
-
-
Etnk2
-
-
kinase, ethanolamine (phosphorylating)
-
-
-
-
additional information
-
cf. EC 2.7.1.32; choline kinase and ethanolamine kinase activities are mediated by 2 distinct active sites, possibly on a single protein
additional information
-
cf. EC 2.7.1.32; choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
cf. EC 2.7.1.32; choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
cf. EC 2.7.1.32; choline kinase and ethanolamine kinase are 2 distinct enzymes
additional information
-
cf. EC 2.7.1.32; choline kinase and ethanolamine kinase may not have a common active site in a single enzyme protein
additional information
-
cf. EC 2.7.1.32; ethanolamine kinase II and choline kinase do not use a common active site
CAS REGISTRY NUMBER
COMMENTARY
9075-78-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
NCIB 9205
-
-
Manually annotated by BRENDA team
pigeon
-
-
Manually annotated by BRENDA team
Culex pipiens fatigans
-
-
-
Manually annotated by BRENDA team
Flavobacterium rhenanum
NCIB 9157, enzyme formed only when amino alcohol serves as a substrate and when activated by ADP
-
-
Manually annotated by BRENDA team
chicken
-
-
Manually annotated by BRENDA team
Hemidactylus sp.
lizard
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
NCIB 8185, enzyme formed only when amino alcohol serves as a substrate and when activated by ADP
-
-
Manually annotated by BRENDA team
alpha isoform, liver, inducible by CCl4
-
-
Manually annotated by BRENDA team
Ehrlich ascites cells
-
-
Manually annotated by BRENDA team
isozyme alpha, exon 1; isozyme alpha, exon 2; isozyme alpha, exon 3; isozyme alpha, exons 4-8; isozyme alpha, exons 9-11
GenBank
Manually annotated by BRENDA team
isozyme alpha, exon 2'
GenBank
Manually annotated by BRENDA team
isozyme beta
SwissProt
Manually annotated by BRENDA team
isoform EK1
UniProt
Manually annotated by BRENDA team
isoform EK2, bifunctional choline kinase/ethanolamine kinase
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (R)-1-aminopropan-2-ol
ADP + (R)-1-aminopropyl 2-phosphate
show the reaction diagram
Q386V0, Q57W59, -
52.4% of the activity with ethanolamine
-
-
?
ATP + (R)-1-aminopropan-2-ol
ADP + (R)-1-aminopropyl 2-phosphate
show the reaction diagram
Q386V0, Q57W59, -
7.2% of the activity with choline
-
-
?
ATP + (R)-2-aminobutan-1-ol
ADP + (R)-2-aminobutyl phosphate
show the reaction diagram
Q386V0, Q57W59, -
102% of the activity with ethanolamine
-
-
?
ATP + (R)-2-aminobutan-1-ol
ADP + (R)-2-aminobutyl phosphate
show the reaction diagram
Q386V0, Q57W59, -
130% of the activity with choline
-
-
?
ATP + (R)-2-aminopropan-1-ol
ADP + (R)-2-aminopropyl phosphate
show the reaction diagram
Q386V0, Q57W59, -
108% of the activity with ethanolamine
-
-
?
ATP + (R)-2-aminopropan-1-ol
ADP + (R)-2-aminopropyl phosphate
show the reaction diagram
Q386V0, Q57W59, -
110% of the activity with choline
-
-
?
ATP + (S)-1-aminopropan-2-ol
ADP + (S)-1-aminopropyl 2-phosphate
show the reaction diagram
Q386V0, Q57W59, -
1.4% of the activity with choline
-
-
?
ATP + (S)-1-aminopropan-2-ol
ADP + (S)-1-aminopropyl 2-phosphate
show the reaction diagram
Q386V0, Q57W59, -
6.1% of the activity with ethanolamine
-
-
?
ATP + (S)-2-aminobutan-1-ol
ADP + (S)-2-aminobutyl phosphate
show the reaction diagram
Q386V0, Q57W59, -
114% of the activity with ethanolamine
-
-
?
ATP + (S)-2-aminobutan-1-ol
ADP + (S)-2-aminobutyl phosphate
show the reaction diagram
Q386V0, Q57W59, -
41% of the activity with choline
-
-
?
ATP + (S)-2-aminopropan-1-ol
ADP + (S)-2-aminopropyl phosphate
show the reaction diagram
Q386V0, Q57W59, -
22.4% of the activity with choline
-
-
?
ATP + (S)-2-aminopropan-1-ol
ADP + (S)-2-aminopropyl phosphate
show the reaction diagram
Q386V0, Q57W59, -
94% of the activity with ethanolamine
-
-
?
ATP + 2-amino-2-methylpropan-1-ol
ADP + 2-amino-2-methylpropan-1-ol phosphate
show the reaction diagram
Q386V0, Q57W59, -
25.6% of the activity with ethanolamine
-
-
?
ATP + 2-amino-2-methylpropan-1-ol
ADP + 2-amino-2-methylpropan-1-ol phosphate
show the reaction diagram
Q386V0, Q57W59, -
46% of the activity with choline
-
-
?
ATP + 3-aminopropan-1-ol
ADP + 3-aminopropyl 1-phosphate
show the reaction diagram
Q386V0, Q57W59, -
37.5% of the activity with ethanolamine
-
-
?
ATP + 3-aminopropan-1-ol
ADP + 3-aminopropyl 1-phosphate
show the reaction diagram
Q386V0, Q57W59, -
44.5% of the activity with choline
-
-
?
ATP + 4-aminobutan-1-ol
ADP + 4-aminobutyl 1-phosphate
show the reaction diagram
Q386V0, Q57W59, -
60% of the activity with choline
-
-
?
ATP + choline
ADP + ?
show the reaction diagram
-
-
-
-
-
ATP + choline
ADP + ?
show the reaction diagram
-
-
-
-
?
ATP + choline
ADP + ?
show the reaction diagram
-, Q9HBU6
very little activity
-
-
?
ATP + choline
ADP + choline phosphate
show the reaction diagram
Q386V0, Q57W59, -
-
-
-
?
ATP + diethanolamine
ADP + O2-[(2-hydroxyethyl)amino]ethyl phosphate
show the reaction diagram
Q386V0, Q57W59, -
-
139% of the activity with choline
-
?
ATP + diethanolamine
ADP + O2-[(2-hydroxyethyl)amino]ethyl phosphate
show the reaction diagram
Q386V0, Q57W59, -
-
88% of the activity with ethanolamine
-
?
ATP + DL-1-aminopropan-2-ol
ADP + DL-1-aminopropane 2-phosphate
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
A7MCT6
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
-
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
-
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
Flavobacterium rhenanum
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
Culex pipiens fatigans
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-, Q9HBU6
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
Q386V0, Q57W59, -
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
Q8IIB7
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-, Q8IIB7
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
the enzyme and the phospholipid phosphatidylethanolamine biosynthesis are regulated by inositol, Kennedy pathway overview
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
Q386V0, Q57W59, -
33% of the activity with choline
-
-
?
ATP + N,N-diethylethanolamine
ADP + N,N-diethyl-O-phosphoethanolamine
show the reaction diagram
Q386V0, Q57W59, -
-
156% of the activity with choline
-
?
ATP + N,N-diethylethanolamine
ADP + N,N-diethyl-O-phosphoethanolamine
show the reaction diagram
Q386V0, Q57W59, -
-
47% of the activity with ethanolamine
-
?
ATP + N,N-dimethylethanolamine
ADP + N,N-dimethyl-O-phosphoethanolamine
show the reaction diagram
Q386V0, Q57W59, -
-
153% of the activity with choline
-
?
ATP + N,N-dimethylethanolamine
ADP + N,N-dimethyl-O-phosphoethanolamine
show the reaction diagram
Q386V0, Q57W59, -
-
76% of the activity with ethanolamine
-
?
ATP + N-ethylethanolamine
ADP + N-ethyl-O-phosphoethanolamine
show the reaction diagram
Q386V0, Q57W59, -
-
150% of the activity with choline
-
?
ATP + N-ethylethanolamine
ADP + N-ethyl-O-phosphoethanolamine
show the reaction diagram
Q386V0, Q57W59, -
-
97% of the activity with ethanolamine
-
?
ATP + N-methylethanolamine
ADP + N-methyl-O-phosphoethanolamine
show the reaction diagram
Q386V0, Q57W59, -
106% of the activity with ethanolamine
-
-
?
ATP + N-methylethanolamine
ADP + N-methyl-O-phosphoethanolamine
show the reaction diagram
Q386V0, Q57W59, -
135% of the activity with choline
-
-
?
choline + ATP
ADP + O-phosphocholine
show the reaction diagram
-
not
-
-
-
choline + ATP
ADP + O-phosphocholine
show the reaction diagram
-
ethanolamine kinase II, not ethanolamine kinase I
-
-
?
GTP + ethanolamine
GDP + O-phosphoethanolamine
show the reaction diagram
Culex pipiens fatigans
-
13% of the activity with ATP
-
-
-
ITP + ethanolamine
IDP + O-phosphoethanolamine
show the reaction diagram
Culex pipiens fatigans
-
45% of the activity with ATP
-
-
-
additional information
?
-
-, Q9HBU6
rate-controlling step in phosphatidylethanolamine biosynthesis
-
-
-
additional information
?
-
-
bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function
-
-
-
additional information
?
-
-
the enzyme controls neuroblast divisions in Drosophila melanogaster mushroom bodies
-
-
-
additional information
?
-
Q386V0, Q57W59, -
no choline kinase activity
-
-
-
additional information
?
-
-, Q8IIB7
no substrate: choline
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-, Q9HBU6
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
Q8IIB7
-
-
-
?
ATP + ethanolamine
ADP + O-phosphoethanolamine
show the reaction diagram
-
the enzyme and the phospholipid phosphatidylethanolamine biosynthesis are regulated by inositol, Kennedy pathway overview
-
-
?
additional information
?
-
-, Q9HBU6
rate-controlling step in phosphatidylethanolamine biosynthesis
-
-
-
additional information
?
-
-
bacteria: enzyme functions in a biodegradative mode, higher organisms: biosynthetic function
-
-
-
additional information
?
-
-
the enzyme controls neuroblast divisions in Drosophila melanogaster mushroom bodies
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
Flavobacterium rhenanum
-
stimulates
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
can substitute for Mg2+
Ca2+
-
neither Ca2+ nor Mn2+ can substitute for Mg2+
Mg2+
-
1.25-2.5 mM ATP: reaction requires free Mg2+ rather than an ATP-Mg2+ complex for maximal velocity; 1.5 mM, in 1.5-fold higher concentration of Mg2+ than ATP; ATP concentration exceeding that of Mg2+: strong inhibition; Km MgATP2-: 10 mM, in presence of equivalent amounts of ATP and Mg2+
Mg2+
-
ethanolamine kinase II: requires MgATP2- as substrate, maximal activation with 10 mM of Mg2+ and ATP; ethanolamine kinase I: uses MgATP2- as substrate but also has an additional requirement for Mg2+; Km MgATP2-: 14 mM; maximal activation at 16 mM MgATP2-, inhibition above
Mg2+
-
requires equimolar concentrations of Mg2+ and ATP (30 mM) for optimal activation
Mg2+
Culex pipiens fatigans
-
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+
-
Mg2+ required
Mg2+
-
maximum concentration equal to that of ATP; Mg2+ required
Mg2+
-
Mg-ATP complex is the substrate
Mg2+
-
Mg-ATP complex is the substrate
Mg2+
-
Mg2+ required
Mg2+
-
free Mg2+ essential for maximal velocity; Km MgATP2-: 0.063 mM; Mg-ATP complex is the substrate
Mn2+
Culex pipiens fatigans
-
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
Mn2+
-
inhibition
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
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
2,3-Dimercaptopropanol
-
-
2-amino-1-butanol
-, Q8IIB7
analogue of ethanolamine, selective inhibition
2-amino-1-butanol
Q8IIB7
-
3,3'-dodecane-1,12-diylbis[5-(2-hydroxyethyl)-4-methyl-1,3-thiazol-3-ium]
Q8IIB7
SAR97276
Acetyl-beta-methylcholine chloride
-
-
Acetylcholine
-
-
adenosine
Culex pipiens fatigans
-
-
ADP
Culex pipiens fatigans
-
-
AMP
Culex pipiens fatigans
-
-
ATP
-
concentration exceeding that of Mg2+
ATP
Culex pipiens fatigans
-
above 8 mM
betaine
-
not
Butyrylcholine iodide
-
-
butyrylthiocholine iodide
-
-
Ca2+
Culex pipiens fatigans
-
inhibits activating effect of Mg2+
Ca2+
-
in presence of Mg2+
choline
-
very strong
choline
-
mixed type
choline
-
ethanolamine kinase I not inhibited, ethanolamine kinase II strongly inhibited
choline
Culex pipiens fatigans
-
not
choline
-
-
choline
-
not
choline phosphate
-
-
Cu2+
Culex pipiens fatigans
-
inhibits activating effect of Mg2+
EGTA
-
stimulation at 0.4-0.9 mM, inhibition at 1.8 mM
Ethanolaminephosphate
-
-
hemicholinium-3
-, Q8IIB7
-
Inositol
-
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
KCl
Culex pipiens fatigans
-
at 10 mM
Methane sulfonylcholine chloride
-
-
MgATP2-
-
substrate inhibition
Mn2+
Culex pipiens fatigans
-
presence of Mn2+ at lower concentrations of Mg2+ has an additive stimulating effect, at higher concentrations of Mg2+, Mn2+ inhibits
Mn2+
-
in presence of Mg2+
N,N-dimethylethanolamine
-
-
N,N-dimethylethanolamine
-
-
N-ethylmaleimide
Culex pipiens fatigans
-
-
N-Methyl-N-isopropylethanolamine
Culex pipiens fatigans
-
-
N-Methylethanolamine
-
-
Ni2+
Culex pipiens fatigans
-
inhibits activating effect of Mg2+
p-chloromercuribenzoate
Culex pipiens fatigans
-
-
p-chloromercuribenzoate
-
not
phosphorylcholine
Culex pipiens fatigans
-
not
phosphorylcholine
-
-
phosphorylcholine
-
not
Phosphorylethanolamine
Culex pipiens fatigans
-
-
Phosphorylethanolamine
-
-
Phosphorylethanolamine
-
not
Propionylcholine iodide
-
-
SAR97276
-, Q8IIB7
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
stearoyl-CoA
-
-
Succinylcholine chloride
-
-
monomethylethanolamine
-
-
additional information
-
not inhibitory: citrate
-
additional information
Culex pipiens fatigans
-
not inhibitory: N-ethyl-N,N-dibutylethanolamine; not inhibitory: N-methyl-N-butylethanolamine; not inhibitory: N-methyl-N,N-diisopropylethanolamine; not inhibitory: N,N-diisopropylethanolamine; not inhibitory: N,N,N-triethanolamine; not inhibitory: serine
-
additional information
-
criterion for an effective inhibitor is the presence of only one N-alkyl group (except dimethylethanol) and a distance of 2 carbon atoms between the N atom and the OH group
-
additional information
-
not inhibitory: sodium arsenite
-
additional information
-
not inhibitory: CDP-choline
-
additional information
-
enzyme expression is not affected by addition of choline
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
Culex pipiens fatigans
-
stimulates
cysteine
Culex pipiens fatigans
-
stimulates
EGTA
-
stimulation at 0.4-0.9 mM, inhibition at 1.8 mM
glutathione
Culex pipiens fatigans
-
stimulates
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0206
-
ATP
Q386V0, Q57W59, -
pH 7.8
0.219
-
ATP
Q386V0, Q57W59, -
pH 7.8
0.5
-
ATP
-
-
0.0314
-
choline
Q386V0, Q57W59, -
-
0.275
-
choline
-
30C, pH 8.5
0.36
-
DL-1-aminopropan-2-ol
Flavobacterium rhenanum
-
-
0.008
-
ethanolamine
-
pH 8.5
0.0184
-
ethanolamine
Q386V0, Q57W59, -
pH 7.8
0.041
-
ethanolamine
-
30C, pH 9.0
0.042
-
ethanolamine
-
-
0.1
-
ethanolamine
-
37C, pH 8.5
0.171
-
ethanolamine
-
30C, pH 8.5
0.25
-
ethanolamine
-
37C, pH 8.5
0.458
-
ethanolamine
-, Q8IIB7
pH 8.0, 37C
0.4757
-
ethanolamine
Q8IIB7
-
0.53
-
ethanolamine
Flavobacterium rhenanum
-
-
2.56
-
ethanolamine
Q386V0, Q57W59, -
pH 7.8
7.7
-
ethanolamine
-
-
10
-
ethanolamine
-
-
1.5
-
MgATP2-
-
with 1.5-fold higher concentration of Mg2+ than ATP, pH 8.5
10
-
MgATP2-
-
in presence of equivalent amounts of ATP and Mg2+, pH 8.5
additional information
-
additional information
-
-
-
additional information
-
additional information
Culex pipiens fatigans
-
-
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00016
-
ethanolamine
-
-
6.56
-
ethanolamine
Q386V0, Q57W59, -
pH 7.8
12.9
-
ethanolamine
Q386V0, Q57W59, -
pH 7.8
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.73
-
3,3'-dodecane-1,12-diylbis[5-(2-hydroxyethyl)-4-methyl-1,3-thiazol-3-ium]
Q8IIB7
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.46
-
2-amino-1-butanol
Q8IIB7
Plasmodium falciparum-endogenous ethanolamine kinase
1.36
-
2-amino-1-butanol
-, Q8IIB7
pH 8.0, 37C
1.36
-
2-amino-1-butanol
Q8IIB7
recombinant protein
0.61
-
3,3'-dodecane-1,12-diylbis[5-(2-hydroxyethyl)-4-methyl-1,3-thiazol-3-ium]
Q8IIB7
recombinant protein
0.79
-
3,3'-dodecane-1,12-diylbis[5-(2-hydroxyethyl)-4-methyl-1,3-thiazol-3-ium]
Q8IIB7
Plasmodium falciparum-endogenous ethanolamine kinase
0.46
-
hemicholinium-3
-, Q8IIB7
pH 8.0, 37C
0.79
-
SAR97276
-, Q8IIB7
pH 8.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.3
-
-, Q8IIB7
pH 8.0, 37C
1.398
-
-
pH 8.5
10.73
-
-
pH 8.5
additional information
-
Culex pipiens fatigans
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
8.5
-
ethanolamine kinase I
8
9.5
-
ethanolamine kinase II
8
-
-
-
8
-
Flavobacterium rhenanum
-
-
8
-
Q8IIB7
activity assay
8.5
10.5
-
-
8.5
-
-
-
8.5
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
9
-
80% of maximum activity at pH 8.0 and pH 9.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
37
-
Culex pipiens fatigans
-
-
37
-
-
assay at
37
-
Q8IIB7
activity assay
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
nerve endings from forebrain
Manually annotated by BRENDA team
Culex pipiens fatigans
-
-
Manually annotated by BRENDA team
-
alpha isozyme
Manually annotated by BRENDA team
-
in the livers of laying geese compared with prelaying geese, genes encoding ethanolamine kinase, vitellogenin I, apoVLDL-II, G-protein gamma-5 subunit, and leucyl-tRNA synthase are highly expressed
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
-
high expression of isoform Eki2 at the time of sex-differentiation
Manually annotated by BRENDA team
-
alpha isozyme
Manually annotated by BRENDA team
additional information
-
beta isozyme, almost equal distribution in all tissues examined
Manually annotated by BRENDA team
additional information
-
high enzyme expression levels in almost all cancer cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-, Q8IIB7
of Plasmodium falciparum
Manually annotated by BRENDA team
additional information
-
a small percentage is membrane associated
-
Manually annotated by BRENDA team
additional information
-
high speed supernatant; supernatant fraction
-
Manually annotated by BRENDA team
additional information
-
supernatant fraction
-
Manually annotated by BRENDA team
additional information
-
supernatant fraction
-
Manually annotated by BRENDA team
additional information
-, Q8IIB7
protein expression levels increase during erythrocytic development
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17000
19000
-
gel filtration, monomeric form
36000
37000
-
dimeric form, gel filtration
36000
-
-
ethanolamine kinase I, gel filtration
44000
-
Culex pipiens fatigans
-
gel filtration
48000
-
Q8IIB7
determined by SDS-PAGE and Western Blot analysis
87000
-
-
gel filtration
90000
-
-
gel filtration
100000
-
Q386V0, Q57W59, -
gel filtration
109000
-
Q8IIB7
determined by gel filtration
110000
-
-
gel filtration
140000
-
Q386V0, Q57W59, -
gel filtration
160000
-
-
ethanolamine kinase II, gel filtration
190000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 42000, SDS-PAGE
dimer
-
2 * 17000-19000, SDS-PAGE, enzyme exists in monomeric and dimeric form
dimer
-
2 * 44000, SDS-PAGE
dimer
-
2 * 86000, SDS-PAGE
dimer
Q386V0, Q57W59, -
2 * 49100, calculated, 2 * 51655, MALDI-TOF; 2 * 70140, calculated, 2 * 72614, MALDI-TOF
homodimer
Q8IIB7
-
monomer
-
1 * 17000-19000, SDS-PAGE, gel filtration, enzyme exists in monomeric and dimeric form
oligomer
-
x * 47000, or x-y * 47000 + y * 43000, or x * 43000, active form consitsts of oligomers of alpha/beta isoforms, with relatively small parts of alpha/alpha or beta/beta homo-oligomers, SDS-PAGE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
Culex pipiens fatigans
-
20 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
inactivation by repeated freezing and thawing
Culex pipiens fatigans
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 10 days, stable
Culex pipiens fatigans
-
-20C or 0-4C, crude cell extract, appreciable loss of activity
-
-20C, 0.02 M phosphate buffer, pH 7.0, 2.9 mM DTT, protein concentration 1.0 mg/ml, ethanolamine kinase I, 2 days, 40% loss of activity
-
4C, 1 week, ethanolamine kinase I, 50% loss of activity
-
0-4C or -20C, partially purified enzyme, 10-14 days, 50% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
using a HisTrap chelating and a gel filtration column
Q8IIB7
copurification of choline kinase and ethanolamine kinase
-
ethanolamine kinase I and II
-
recombinant protein; recombinant protein
Q386V0, Q57W59, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression as GST-fusion protein in Escherichia coli strain BL21
-
-
Q9HBU6
overview
-
-
O54804, Q54AG5, Q9D4V0
expressed in 293T cells
A7MCT6
expression in Escherichia coli
-, Q8IIB7
into the vector pET24b for expression in Escherichia coli BL21DE3-pRIL cells
Q8IIB7
expressed in Escherichia coli strain strain DH5alpha
-
expression of the enzyme fused to the lacZ reporter gene in several yeast strains and in Escherichia coli strain DH5alpha, expression analysis in presence of inositol and choline in correlation to wild-type and mutated promotor
-
expression in Escherichia coli; expression in Escherichia coli
Q386V0, Q57W59, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression levels increases during erythrocytic development
Q8IIB7
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
easily shocked mutation, significantly reduced levels of O-phosphoethanolamine and phosphatidylserine
additional information
-
targeted disruption of Eki2 gene. No abnormalities in deficient mice with regard to embryonic and adult testis morphology, differentiation, function or fertility, and no significant differences in litter size, pup mortality rates or distribution of the sexes among the offspring compared with wild-type
additional information
-
eki1Delta, main enzyme responsible for phosphoethanolamine synthesis eki1Delta cki1Delta, no residual enzymic activity
additional information
-
down-regulation of the expression of ethanolamine kinase and ethanolamine-phosphate cytidylyltransferase by RNAi results in inhibition of phosphatidylethanolamine synthesis in procyclic forms and, concomitantly, in a block in glycosylphosphatidylinositol attachment to procyclins and ethanolamine-phosphoglycerol modification of eukaryotic elongation factor 1A
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
Q8IIB7
ethanolamine kinase could be a target for antimalerial therapy
medicine
-
galactosemic cataractogenesis changes substrate specificity of enzyme