Literature summary for 2.1.1.233 extracted from

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 (2001), J. Biol. Chem., 276, 1570-1577.

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Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine	the enzyme catalyzes the methylation of the phosphatase 2A protein C subunit carboxyl-terminal leucine	Saccharomyces cerevisiae	S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester	-	?

Synonyms

Synonyms	Comment	Organism
phosphatase 2A protein methyltransferase	-	Saccharomyces cerevisiae
Ppm1p	major phosphatase 2A protein methyltransferase in Saccharomyces cerevisiae	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
malfunction	deletion of phosphatase 2A protein methyltransferase PPM1 greatly reduces Cdc55p, Tpd3p, and Rts1p binding and leads to nocodazole sensitivity	Saccharomyces cerevisiae
physiological function	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	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)