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Information on EC 2.1.1.71 - phosphatidyl-N-methylethanolamine N-methyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SAH5

for references in articles please use BRENDA:EC2.1.1.71
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IUBMB Comments
The enzyme also catalyses the transfer of a further methyl group, producing phosphatidylcholine.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9SAH5
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
phospholipid methyltransferase, methyltransferase ii, pemt-l, pemt-s, phosphatidyl-n-methylethanolamine methyltransferase, phosphatidylmonomethylethanolamine methyltransferase, phosphatidylethanolamine methyltransferase i, phosphatidyl-n-methylethanolamine n-methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospholipid N-methyltransferase
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methyltransferase II
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phosphatidyl-N-methylethanolamine methyltransferase
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phosphatidyl-N-monomethylethanolamine methyltransferase
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phosphatidylethanolamine methyltransferase I
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phosphatidylmonomethylethanolamine methyltransferase
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phospholipid methyltransferase
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PLMT
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:phosphatidyl-N-methylethanolamine N-methyltransferase
The enzyme also catalyses the transfer of a further methyl group, producing phosphatidylcholine.
CAS REGISTRY NUMBER
COMMENTARY hide
67167-73-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + phosphatidyl-N-monomethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
show the reaction diagram
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?
S-adenosyl-L-methionine + phosphatidyl-N,N-dimethylethanolamine
S-adenosyl-L-homocysteine + phosphatidylcholine
show the reaction diagram
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?
additional information
?
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cannot utilize phosphatidyl-N-ethanolamine as a substrate
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
although the accumulation of the PLMT substrates phosphatidyl-N-monomethylethanolamine and phosphatidyl-N,N-dimethylethanolamine is considerably elevated in the plmt knock-out line, phosphatidylcholine levels remain normal, and no obvious differences are observed in plant morphology or development under standard growth conditions
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLMT_ARATH
164
3
18819
Swiss-Prot
Secretory Pathway (Reliability: 5)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Keogh, M.R.; Courtney, P.D.; Kinney, A.J.; Dewey, R.E.
Functional characterization of phospholipid N-methyltransferases from Arabidopsis and soybean
J. Biol. Chem.
284
15439-15447
2009
Arabidopsis thaliana (Q9SAH5), Glycine max (C3VD33)
Manually annotated by BRENDA team