2.1.1.103: phosphoethanolamine N-methyltransferase
This is an abbreviated version!
For detailed information about phosphoethanolamine N-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.103
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2.1.1.103
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phosphatidylcholine
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phosphocholine
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choline
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phospholipid
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plasmodium
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falciparum
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malaria
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betaine
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s-adenosylhomocysteine
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plant-like
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osmoprotectant
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cdp-choline
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s-adenosylmethionine-dependent
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transmethylation
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medicine
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halophyte
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s-adenosyl-l-methionine-dependent
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nematicide
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amodiaquine
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drug development
- 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
Reaction
Synonyms
AtNMT1, DPR2, More, NMT1, NMT2, PEAMT, PEAMT1, Pfpmt, phosphodimethylethanolamine methyltransferase, phosphoethanolamine methyltransferase, phosphoethanolamine N-methyltransferase, phosphoethanolamine-N-methyltransferases, phosphomethylethanolamine N-methyltransferase, PMEAMT, PMT, PMT-1, PMT1, PMT2, PVX_083045, S-adenosyl-L-methionine:phosphoethanolamine N-methyltransferase, SoPEAMT
ECTree
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General Information
General Information on EC 2.1.1.103 - phosphoethanolamine N-methyltransferase
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malfunction
metabolism
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the enzyme has a central role in phosphatidylcholine biosynthesis via the methylation pathway and plays a role in cell division and inflorescence meristem
physiological function
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knock-out of the PMT gene encoding the phosphoethanolamine methyltransferase enzyme completely abrogates the biosynthesis of phosphatidylcholine via the serine-decarboxylase-phosphoethanolamine-methyltransferase pathway, loss of PMT results in significant defects in parasite growth, multiplication, and viability, suggesting that this gene plays an important role in the pathogenesis of intraerythrocytic Plasmodium parasites
malfunction
Arabidopsis pmeamt T-DNA mutant (atpmeamt) lacks transcripts associated with PMEAMT but has no overt phenotype. The leaf membrane phospholipid profiles show a greater content of PtdMEA as the 34:3 lipid molecular species in atpmeamt plants relative to wild type
malfunction
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disruption of enzyme activity results in severe defects in important cellular processes such as development, replication, survival and sexual maturation and differentiation
malfunction
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inhibition of enzyme biosynthesis leads to necrotic lesions in leaves, multiple inflorescences, sterility in the flower, and early flowering in short day conditions
malfunction
parasites lacking the enzyme are incapable of producing mature gametocytes and are not transmitted to mosquitoes
enzyme can rescue a choline auxotroph of yeast
physiological function
the enzyme is essential for normal growth and development
physiological function
the enzyme is required for gametocyte development, maturation, and transmission to mosquitoes
physiological function
isoform NMT1 is essential for normal growth and salt tolerance. The NMT1 mutant displays a short root phenotype under normal growth conditions and hypersensitivity, as determined by root length, under salt-stress conditions
physiological function
loss of function of DPR2/PEAMT1 affects root stem cell niche, division zone, elongation and differentiation zone. PIN-FORMED (PIN) protein abundance, PIN2 polar distribution and general endocytosis are impaired in the root tip of the mutant. Excess hydrogen peroxide and auxin accumulate in the elongation and differentiation zone, leading to root apical meristem consumption by accelerating cell differentiation
physiological function
the isoforms NMT1/NMT3 double knock-out mutant is viable. This is enabled by residual phosphoethanolamine N-methyltransferase activity through isoform NMT2. The triple NMT1/NMT2/NMT3 knock-out mutant cannot synthesize phosphatidylcholine from phosphoethanolamine and is lethal. Through alternative use of its promoter, NMT2 encodes two phosphoethanolamine N-methyltransferase variants, which greatly differ in their ability to perform the initial phosphobase methylation of phosphoethanolamine