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Information on EC 2.1.1.233 - [phosphatase 2A protein]-leucine-carboxy methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q04081

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IUBMB Comments
Methylates the C-terminal leucine of phosphatase 2A. A key regulator of protein phosphatase 2A. The methyl ester is hydrolysed by EC 3.1.1.89 (protein phosphatase methylesterase-1). Occurs mainly in the cytoplasm, Golgi region and late endosomes.
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Saccharomyces cerevisiae
UNIPROT: Q04081
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
+
[phosphatase 2A protein]-leucine
=
+
[phosphatase 2A protein]-leucine methyl ester
Synonyms
pme-1, lcmt-1, lcmt1, pp2a methyltransferase, leucine carboxyl methyltransferase, leucine carboxyl methyltransferase-1, leucine carboxyl methyltransferase 1, ppm1p, pp2a-specific methyltransferase, leucine carboxyl methyl transferase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
protein phosphatase methyltransferase 1
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phosphatase 2A protein methyltransferase
-
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Ppm1p
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major phosphatase 2A protein methyltransferase in Saccharomyces cerevisiae
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[phosphatase 2A protein]-leucine O-methyltransferase
Methylates the C-terminal leucine of phosphatase 2A. A key regulator of protein phosphatase 2A. The methyl ester is hydrolysed by EC 3.1.1.89 (protein phosphatase methylesterase-1). Occurs mainly in the cytoplasm, Golgi region and late endosomes.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine
S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine
S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester
show the reaction diagram
-
the enzyme catalyzes the methylation of the phosphatase 2A protein C subunit carboxyl-terminal leucine
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
dependent on
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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deletion of phosphatase 2A protein methyltransferase PPM1 greatly reduces Cdc55p, Tpd3p, and Rts1p binding and leads to nocodazole sensitivity
physiological function
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carboxymethylation of the PP2A catalytic subunit by phosphatase 2A protein methyltransferase PPM1 in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits Cdc55p and Rts1p
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native protein alone or in complexes with the S-adenosyl-L-methionine methyl donor and the S-adenosyl-L-homocysteine product and inhibitor, hanging drop vapor diffusion method, using 15% (w/v) PEG 8000 and 0.1 M potassium or sodium phosphate, pH 4.6, or 20% (w/v) PEG 8000, 0.1 M sodium acetate, and 0.1 M MES, pH 5.6, or 24% (w/v) PEG 4000, 0.2 M magnesium chloride, and 0.1 M Tris-HCl, pH 8.5
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity column chromatography and Superdex 75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli XL-10 Gold cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wei, H.; Ashby, D.; Moreno, C.; Ogris, E.; Yeong, F.; Corbett, A.; Pallas, D.
Carboxymethylation of the PP2A catalytic subunit in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits Cdc55p and Rts1p
J. Biol. Chem.
276
1570-1577
2001
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Leulliot, N.; Quevillon-Cheruel, S.; Sorel, I.; De La Sierra-Gallay, I.; Collinet, B.; Graille, M.; Blondeau, K.; Bettache, N.; Poupon, A.; Janin, J.; Van Tilbeurgh, H.
Structure of protein phosphatase methyltransferase 1 (PPM1), a leucine carboxyl methyltransferase involved in the regulation of protein phosphatase 2A activity
J. Biol. Chem.
279
8351-8358
2004
Saccharomyces cerevisiae (Q04081), Saccharomyces cerevisiae
Manually annotated by BRENDA team