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Information on EC 4.2.3.2 - ethanolamine-phosphate phospho-lyase and Organism(s) Homo sapiens

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.2 ethanolamine-phosphate phospho-lyase
IUBMB Comments
A pyridoxal-phosphate protein. Also acts on D(or L)-1-aminopropan-2-ol O-phosphate.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
agxt2l1, etnppl, pea phospho-lyase, o-phosphoethanolamine phospho-lyase, ethanolamine-phosphate phospho-lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AGXT2L1
-
-
amino alcohol O-phosphate phospholyase
-
-
-
-
ETNPPL
-
-
O-phosphoethanolamine phospho-lyase
-
-
O-phosphoethanolamine-phospholyase
-
-
-
-
O-phosphorylethanol-amine phospho-lyase
-
-
-
-
PEA phospho-lyase
-
-
phospho-lyase, ethanolamine phosphate
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
ethanolamine-phosphate phosphate-lyase (deaminating; acetaldehyde-forming)
A pyridoxal-phosphate protein. Also acts on D(or L)-1-aminopropan-2-ol O-phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
37290-88-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ethanolamine phosphate + H2O
acetaldehyde + NH3 + phosphate
show the reaction diagram
-
-
-
-
ir
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ethanolamine phosphate + H2O
acetaldehyde + NH3 + phosphate
show the reaction diagram
-
-
-
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Aminopropylphosphonate
-
-
ethylsulfonate
-
-
methylsulfonate
-
-
phosphate
-
competitive inhibitor at pH values between 6.0 and 8.0
sulfate
-
competitive inhibitor at pH values between 6.0 and 8.0
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
Ethanolamine phosphate
-
at pH 7.4 and 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9 - 2.3
Ethanolamine phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
Ethanolamine phosphate
-
at pH 7.4 and 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 8
phosphate
1.5
sulfate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AT2L1_HUMAN
499
0
55671
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schiroli, D.; Ronda, L.; Peracchi, A.
Kinetic characterization of the human O-phosphoethanolamine phospho-lyase reveals unconventional features of this specialized pyridoxal phosphate-dependent lyase
FEBS J.
282
183-199
2015
Homo sapiens
Manually annotated by BRENDA team