Protein L-Isoaspartate-O-Methyltransferase (PCMT1)

PIMT; L-isoaspartyl protein carboxyl methyltransferase; Protein L-isoaspartyl/D-aspartyl methyltransferase; Protein-beta-aspartate methyltransferase

SPN	M401
HGNC	8728
MGI	97502
PubMed	23918616
RGD	3268
UniProt	P22061
Wiki	PCMT1

Three classes of protein carboxyl methyltransferases, distinguished by their methyl-acceptor substrate specificity, have been found in prokaryotic and eukaryotic cells. The type II enzyme catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the free carboxyl groups of D-aspartyl and L-isoaspartyl residues.

These methyl-accepting residues result from the spontaneous deamidation, isomerization, and racemization of normal L-aspartyl and L-asparaginyl residues and represent sites of covalent damage to aging proteins PCMT1 (EC 2.1.1.77) is a protein repair enzyme that initiates the conversion of abnormal D-aspartyl and L-isoaspartyl residues to the normal L-aspartyl form.

Reference

"Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA, and small molecule S-adenosylmethionine-dependent methyltransferases."
J. Biol. Chem. 264:20131-20139(1989) [PubMed] [Europe PMC] [Abstract]

"Alternative splicing of the human isoaspartyl protein carboxyl methyltransferase RNA leads to the generation of a C-terminal -RDEL sequence in isozyme II."
Biochem. Biophys. Res. Commun. 185:277-283(1992) [PubMed] [Europe PMC] [Abstract]

"Characterization of three cDNAs encoding two isozymes of an isoaspartyl protein carboxyl methyltransferase from human erythroid leukemia cells."
J. Biochem. 117:683-685(1995) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and analysis of human chromosome 6."
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Structure of the human gene encoding the protein repair L-isoaspartyl (D-aspartyl) O-methyltransferase."
Arch. Biochem. Biophys. 335:321-332(1996) [PubMed] [Europe PMC] [Abstract]

"Purification of homologous protein carboxyl methyltransferase isozymes from human and bovine erythrocytes."
Biochemistry 27:5227-5233(1988) [PubMed] [Europe PMC] [Abstract]

, Submitted (DEC-2008) to UniProtKB

"Amino acid polymorphisms of the human L-isoaspartyl/D-aspartyl methyltransferase involved in protein repair."
Biochem. Biophys. Res. Commun. 203:491-497(1994) [PubMed] [Europe PMC] [Abstract]

"Distinct C-terminal sequences of isozymes I and II of the human erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase."
Biochem. Biophys. Res. Commun. 175:351-358(1991) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"Polymorphic forms of the protein L-isoaspartate (D-aspartate) O-methyltransferase involved in the repair of age-damaged proteins."
J. Hum. Genet. 44:275-288(1999) [PubMed] [Europe PMC] [Abstract]

"Crystal structure of human L-isoaspartyl methyltransferase."
J. Biol. Chem. 277:10642-10646(2002) [PubMed] [Europe PMC] [Abstract]

"Crystal structure of human L-isoaspartyl-O-methyl-transferase with S-adenosyl homocysteine at 1.6-A resolution and modeling of an isoaspartyl-containing peptide at the active site."
Protein Sci. 11:625-635(2002) [PubMed] [Europe PMC] [Abstract]

"Initial characterization of the human central proteome."
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]