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Information on EC 2.1.1.103 - phosphoethanolamine N-methyltransferase and Organism(s) Spinacia oleracea and UniProt Accession Q9M571
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2.1.1.103 phosphoethanolamine N-methyltransferaseIUBMB Comments
The enzyme may catalyse the transfer of two further methyl groups to the product.
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Word Map
- 2.1.1.103
- phosphatidylcholine
- phosphocholine
- choline
- phospholipid
- plasmodium
- falciparum
- malaria
- betaine
- s-adenosylhomocysteine
-
plant-like
-
osmoprotectant
- cdp-choline
-
s-adenosylmethionine-dependent
-
transmethylation
- medicine
-
halophyte
-
s-adenosyl-l-methionine-dependent
-
nematicide
- amodiaquine
- drug development
The taxonomic range for the selected organisms is: Spinacia oleracea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
pfpmt, peamt, phosphoethanolamine n-methyltransferase, phosphoethanolamine methyltransferase, pmt-1, atnmt1, pmeamt, s-adenosyl-l-methionine:phosphoethanolamine n-methyltransferase, peamt1, phosphomethylethanolamine n-methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
phosphodimethylethanolamine methyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:ethanolamine-phosphate N-methyltransferase
The enzyme may catalyse the transfer of two further methyl groups to the product.
CAS REGISTRY NUMBER
COMMENTARY
145539-90-8
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171040-79-2
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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
S-adenosyl-L-methionine + 2-(methylamino)ethyl phosphate
S-adenosyl-L-homocysteine + 2-(dimethylamino)ethyl phosphate
-
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
S-adenosyl-L-methionine + phosphodimethylethanolamine
S-adenosyl-L-homocysteine + phosphocholine
-
-
?
S-adenosyl-L-methionine + 2-(methylamino)ethyl phosphate
S-adenosyl-L-homocysteine + 2-(dimethylamino)ethyl phosphate
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
S-adenosyl-L-methionine + phosphodimethylethanolamine
S-adenosyl-L-homocysteine + phosphocholine
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
involved in synthesis of phosphocholine and phosphatidylcholine
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
involved in production of free choline
-
?
S-adenosyl-L-methionine + 2-(methylamino)ethyl phosphate
S-adenosyl-L-homocysteine + 2-(dimethylamino)ethyl phosphate
-
-
-
?
S-adenosyl-L-methionine + 2-(methylamino)ethyl phosphate
S-adenosyl-L-homocysteine + 2-(dimethylamino)ethyl phosphate
-
-
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
-
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
-
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
-
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
involved in synthesis of phosphocholine and phosphatidylcholine
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
involved in synthesis of phosphocholine and phosphatidylcholine
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
involved in synthesis of phosphocholine and phosphatidylcholine
-
?
S-adenosyl-L-methionine + phosphodimethylethanolamine
S-adenosyl-L-homocysteine + phosphocholine
-
-
-
?
S-adenosyl-L-methionine + phosphodimethylethanolamine
S-adenosyl-L-homocysteine + phosphocholine
-
poor substrate
-
?
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
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
involved in synthesis of phosphocholine and phosphatidylcholine
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
involved in production of free choline
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
involved in synthesis of phosphocholine and phosphatidylcholine
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
involved in synthesis of phosphocholine and phosphatidylcholine
-
?
S-adenosyl-L-methionine + ethanolamine phosphate
S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
-
involved in synthesis of phosphocholine and phosphatidylcholine
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the protein and transcript level for SoPEAMT are lower in the roots grown with 10 mM choline chloride than in the roots grown either with or without 10 mM NaCl
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PEAMT_SPIOL
494
0
56361
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
deleting the C-terminal domain does not abolish ethanolamine phosphate reactivity, C-terminal domain catalyzes reactions with methylated ethanolamine phosphate
additional information
-
deleting the C-terminal domain does not abolish ethanolamine phosphate reactivity, C-terminal domain catalyzes reactions with methylated ethanolamine phosphate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weretilnyk, E.A.; Smith, D.D.; Wilch, G.A.; Summers, P.S.
Enzymes of choline synthesis in spinach. Response of phospho-base N-methyltransferase activities to light and salinity
Plant Physiol.
109
1085-1091
1995
Spinacia oleracea
Nuccio, M.L.; Ziemak, M.J.; Henry, S.A.; Weretilnyk, E.A.; Hanson, A.D.
cDNA cloning of phosphoethanolamine N-methyltransferase from spinach by complementation in Schizosaccharomyces pombe and characterization of the recombinant enzyme
J. Biol. Chem.
275
14095-14101
2000
Spinacia oleracea (Q9M571), Spinacia oleracea
Lorenzin, D.; Webb, C.; Summers, P.S.; Weretilnyk, E.A.
Enzymes of choline synthesis in diverse plants: Variation in phospho-base N-methyltransferase activities
Can. J. Bot.
79
897-904
2001
Amaranthus caudatus, Beta vulgaris, Glycine max, Gossypium hirsutum, Limonium perezii, Pisum sativum, Spinacia oleracea
Smith, D.D.; Summers, P.S.; Weretilnyk, E.A.
Phosphocholine synthesis in spinach: characterization of phosphoethanolamine N-methyltransferase
Physiol. Plant.
108
286-294
2000
Spinacia oleracea
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