EC number:2.1.1.233

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.233
Description:[Phosphatase 2A protein]-leucine-carboxy methyltransferase.
Alternative Name: Leucine carboxy methyltransferase-1.
Cath: 3.40.50.150; 3.40.50.1820;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.233
BRENDA Enzyme Link: BRENDA 2.1.1.233
KEGG Enzyme Link: KEGG2.1.1.233
BioCyc Enzyme Link: BioCyc 2.1.1.233
ExPASy Enzyme Link: ExPASy2.1.1.233
EC2PDB Enzyme Link: EC2PDB 2.1.1.233
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.233
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.233
IntEnz Enzyme Link: IntEnz 2.1.1.233
MEDLINE Enzyme Link: MEDLINE 2.1.1.233

EC number:2.1.1.233

MSA:

2.1.1.233;
Phylogenetic Tree:

2.1.1.233;
Uniprot:
M-CSA:
RHEA:48544 [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A.Tsai ML, Cronin N, Djordjevic S2011 Jan21206058
Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue.De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J1999 Dec 1410600115