Information on EC 2.7.8.4 - serine-phosphoethanolamine synthase

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The expected taxonomic range for this enzyme is: Gallus gallus

EC NUMBER
COMMENTARY hide
2.7.8.4
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RECOMMENDED NAME
GeneOntology No.
serine-phosphoethanolamine synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CDP-ethanolamine + L-serine = CMP + L-serine-phosphoethanolamine
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
substituted phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycerophospholipid metabolism
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SYSTEMATIC NAME
IUBMB Comments
CDP-ethanolamine:L-serine ethanolamine phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-23-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
chicken
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CDP-2-amino-2-methylpropanol + L-serine
?
show the reaction diagram
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-
-
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?
CDP-ethanolamine + DL-alpha-methylserine
?
show the reaction diagram
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-
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?
CDP-ethanolamine + L-serine
CMP + L-serine-ethanolamine phosphate
show the reaction diagram
CMP-aminoethylphosphonate + L-serine
?
show the reaction diagram
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-
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?
additional information
?
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CDP-choline and CDP-serine cannot replace CDP-ethanolamine, N-acetyl-L-serine, L-homoserine, 4-hydroxy-L-proline, 5-hydroxy-DL-lysine, 3-hydroxy-DL-glutamic acid, L-threonine, ethanolamine or 3-hydroxypropionic acid cannot replace serine
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CDP-ethanolamine + L-serine
CMP + L-serine-ethanolamine phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CDP
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strong inhibition
CETAB
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cationic detergent, strong inhibition
CMP
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competitive inhibition to CDPethanolamine, non-competitive inhibition to L-serine
Duponal
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strong inhibition
iodoacetamide
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; 1 mM, 6% remaining activity
iodoacetate
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1 mM, 42% remaining activity
L-alanine
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27-34% inhibition of the reaction
L-homoserine
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27-34% inhibition of the reaction
L-threonine
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27-34% inhibition of the reaction
Methylmercuric bromide
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0.1 mM, 6% remaining activity
Methylmercuric iodide
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0.1 mM, 3% remaining activity
N-Acetylimidazole
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; 10 mM, 8% remaining activity
N-ethylmaleimide
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0.2 mM, 25% remaining activity
p-hydroxymercuribenzoate
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0.1 mM, 2% remaining activity
phenylmercuric acetate
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0.1 mM, 2% remaining activity
Shell Nonidet P-40
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strong inhibition
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Sulfanilic acid
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diazotized, 0.2 mM, 36% remaining activity
additional information
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iodoacetate is less effective as inhibitor, DFP is no inhibitor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.085
CDP-ethanolamine
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pH 7.0, 37C
0.011
CMP-aminoethylphosphonate
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pH 7.0, 37C
1
L-serine
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pH 7.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0034
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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Manually annotated by BRENDA team
additional information
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no activity in liver, spleen, brain, oviduct, blood, and heart
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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stable for 60 min
55
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heat-labile, inactivated after 15 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to freezing, aggregates on thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, stable to freezing
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4C, enzyme preparartion remains active
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
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