http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-6528295-B2

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classificationCPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K38-00
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classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-18
classificationIPCAdditional http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K38-00
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-18
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21
filingDate 2001-04-20-04:00^^<http://www.w3.org/2001/XMLSchema#date>
grantDate 2003-03-04-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_a1ac633cee523619e424b56c098f8157
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_41e57b36406348fd4474d9c8a159161c
publicationDate 2003-03-04-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber US-6528295-B2
titleOfInvention Protein phosphatase methylesterase
abstract Carboxymethylation of proteins is a highly conserved means of regulation in eukaryotic cells. The protein phosphatase 2A (PP2A) catalytic (C) subunit is reversibly methylated at its carboxy-terminus by specific methylesterase. Carboxymethylation affects PP2A activity and varies during the cell cycle. The present disclosure provides the coding sequence of a methylesterase, herein named Protein Phosphatase Methylesterase-1 (PME-1). PME-1 is highly conserved from yeast to human and contains a motif found in lipases, which motif has a catalytic triad-activated serine as the active site nucleophile. Recombinant PME-1 polypeptide produced in bacteria demethylates PP2A C subunit in vitro and okadaic acid, a known inhibitor of the PP2A methylesterase, inhibited this reaction. PME-1 represents the first mammalian protein phosphatase methylesterase cloned to date.
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priorityDate 1998-04-17-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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