Literature summary for 2.1.1.233 extracted from

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 (2004), J. Biol. Chem., 279, 8351-8358.

Search for more literature for 2.1.1.233

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli XL-10 Gold cells	Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	Q04081	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni2+ affinity column chromatography and Superdex 75 gel filtration	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine	-	Saccharomyces cerevisiae	S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester	-	?

Synonyms

Synonyms	Comment	Organism
PPM1	-	Saccharomyces cerevisiae
protein phosphatase methyltransferase 1	-	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	dependent on	Saccharomyces cerevisiae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)