EC number:3.1.1.89

Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.1 Carboxylic-ester hydrolases
ID:3.1.1.89
Description:Protein phosphatase methylesterase-1.
Cath: 3.40.50.150; 3.40.50.1820;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.1.89
BRENDA Enzyme Link: BRENDA 3.1.1.89
KEGG Enzyme Link: KEGG3.1.1.89
BioCyc Enzyme Link: BioCyc 3.1.1.89
ExPASy Enzyme Link: ExPASy3.1.1.89
EC2PDB Enzyme Link: EC2PDB 3.1.1.89
ExplorEnz Enzyme Link: ExplorEnz 3.1.1.89
PRIAM enzyme-specific profiles Link: PRIAM 3.1.1.89
IntEnz Enzyme Link: IntEnz 3.1.1.89
MEDLINE Enzyme Link: MEDLINE 3.1.1.89

EC number:3.1.1.89

MSA:

3.1.1.89;
Phylogenetic Tree:

3.1.1.89;
Uniprot:
M-CSA:
RHEA:48548 [phosphatase 2A protein]-C-terminal L-leucine methyl ester + H2O = [phosphatase 2A protein]-C-terminal L-leucine + H(+) + methanol
RULE(radius=1) [*:1]-[O;H0;+0:2]-[CH3;+0:3].[OH2;+0:4]>>[*:1]-[OH;+0:2].[CH3;+0:3]-[OH;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural mechanism of demethylation and inactivation of protein phosphatase 2A.Xing Y, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi Y2008 Apr 418394995
A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A.Ogris E, Du X, Nelson KC, Mak EK, Yu XX, Lane WS, Pallas DC1999 May 1410318862