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PCMT1

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{{Short description|Protein-coding gene in the species Homo sapiens}}

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Protein-L-isoaspartate(D-aspartate) O-methyltransferase is an enzyme that in humans is encoded by the PCMT1 gene.{{cite journal | vauthors = MacLaren DC, O'Connor CM, Xia YR, Mehrabian M, Klisak I, Sparkes RS, Clarke S, Lusis AJ | title = The L-isoaspartyl/D-aspartyl protein methyltransferase gene (PCMT1) maps to human chromosome 6q22.3-6q24 and the syntenic region of mouse chromosome 10 | journal = Genomics | volume = 14 | issue = 4 | pages = 852–6 |date=Feb 1993 | pmid = 1478665 | doi =10.1016/S0888-7543(05)80104-1 }}{{cite journal | vauthors = DeVry CG, Clarke S | title = Assignment of the protein L-isoaspartate (D-aspartate) O-methyltransferase gene (PCMT1) to human chromosome bands 6q24→q25 with radiation hybrid mapping | journal = Cytogenet Cell Genet | volume = 84 | issue = 1–2 | pages = 130–1 |date=Jun 1999 | pmid = 10343128 | doi =10.1159/000015239 | s2cid = 38976877 }}

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.[supplied by OMIM]{{cite web | title = Entrez Gene: PCMT1 protein-L-isoaspartate (D-aspartate) O-methyltransferase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5110}}

References

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Further reading

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  • {{cite journal | vauthors=MacLaren DC, Kagan RM, Clarke S |title=Alternative splicing of the human isoaspartyl protein carboxyl methyltransferase RNA leads to the generation of a C-terminal -RDEL sequence in isozyme II |journal=Biochem. Biophys. Res. Commun. |volume=185 |issue= 1 |pages= 277–83 |year= 1992 |pmid= 1339271 |doi=10.1016/S0006-291X(05)80987-8 }}
  • {{cite journal | vauthors=Ingrosso D, Kagan RM, Clarke S |title=Distinct C-terminal sequences of isozymes I and II of the human erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase |journal=Biochem. Biophys. Res. Commun. |volume=175 |issue= 1 |pages= 351–8 |year= 1991 |pmid= 1998518 |doi=10.1016/S0006-291X(05)81242-2 }}
  • {{cite journal | vauthors=Ingrosso D, Fowler AV, Bleibaum J, Clarke S |title=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 |journal=J. Biol. Chem. |volume=264 |issue= 33 |pages= 20131–9 |year= 1989 |doi=10.1016/S0021-9258(19)47228-1 |pmid= 2684970 |doi-access=free }}
  • {{cite journal | vauthors=Gilbert JM, Fowler A, Bleibaum J, Clarke S |title=Purification of homologous protein carboxyl methyltransferase isozymes from human and bovine erythrocytes |journal=Biochemistry |volume=27 |issue= 14 |pages= 5227–33 |year= 1988 |pmid= 3167043 |doi=10.1021/bi00414a042 }}
  • {{cite journal | vauthors=Ota IM, Gilbert JM, Clarke S |title=Two major isozymes of the protein D-aspartyl/L-isoaspartyl methyltransferase from human erythrocytes |journal=Biochem. Biophys. Res. Commun. |volume=151 |issue= 3 |pages= 1136–43 |year= 1988 |pmid= 3355545 |doi=10.1016/S0006-291X(88)80484-4 }}
  • {{cite journal |vauthors=Takeda R, Mizobuchi M, Murao K, etal |title=Characterization of three cDNAs encoding two isozymes of an isoaspartyl protein carboxyl methyltransferase from human erythroid leukemia cells |journal=J. Biochem. |volume=117 |issue= 4 |pages= 683–5 |year= 1995 |pmid= 7592526 |doi=10.1093/jb/117.2.267 |doi-access=free }}
  • {{cite journal | vauthors=Tsai W, Clarke S |title=Amino acid polymorphisms of the human L-isoaspartyl/D-aspartyl methyltransferase involved in protein repair |journal=Biochem. Biophys. Res. Commun. |volume=203 |issue= 1 |pages= 491–7 |year= 1994 |pmid= 8074695 |doi= 10.1006/bbrc.1994.2209 }}
  • {{cite journal | vauthors=DeVry CG, Tsai W, Clarke S |title=Structure of the human gene encoding the protein repair L-isoaspartyl (D-aspartyl) O-methyltransferase |journal=Arch. Biochem. Biophys. |volume=335 |issue= 2 |pages= 321–32 |year= 1997 |pmid= 8914929 |doi= 10.1006/abbi.1996.0513 |citeseerx=10.1.1.630.8527 }}
  • {{cite journal | vauthors=DeVry CG, Clarke S |title=Polymorphic forms of the protein L-isoaspartate (D-aspartate) O-methyltransferase involved in the repair of age-damaged proteins |journal=J. Hum. Genet. |volume=44 |issue= 5 |pages= 275–88 |year= 1999 |pmid= 10496068 |doi=10.1007/s100380050161 |doi-access=free }}
  • {{cite journal |vauthors=Ryttersgaard C, Griffith SC, Sawaya MR, etal |title=Crystal structure of human L-isoaspartyl methyltransferase |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10642–6 |year= 2002 |pmid= 11792715 |doi= 10.1074/jbc.M200229200 |doi-access= free }}
  • {{cite journal |vauthors=Smith CD, Carson M, Friedman AM, etal |title=Crystal structure of human L-isoaspartyl-O-methyl-transferase with S-adenosyl homocysteine at 1.6-Å resolution and modeling of an isoaspartyl-containing peptide at the active site |journal=Protein Sci. |volume=11 |issue= 3 |pages= 625–35 |year= 2002 |pmid= 11847284 |doi=10.1110/ps.37802 | pmc=2373461 }}
  • {{cite journal |vauthors=Misra P, Qi C, Yu S, etal |title=Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 20011–9 |year= 2002 |pmid= 11912212 |doi= 10.1074/jbc.M201739200 |doi-access= free}}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
  • {{cite journal |vauthors=Enünlü I, Pápai G, Cserpán I, etal |title=Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus |journal=Biochem. Biophys. Res. Commun. |volume=309 |issue= 1 |pages= 44–51 |year= 2003 |pmid= 12943661 |doi=10.1016/S0006-291X(03)01514-6 }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
  • {{cite journal |vauthors=Zhu H, Yang W, Lu W, etal |title=A known functional polymorphism (Ile120Val) of the human PCMT1 gene and risk of spina bifida |journal=Mol. Genet. Metab. |volume=87 |issue= 1 |pages= 66–70 |year= 2006 |pmid= 16256389 | pmc=2947858 |doi= 10.1016/j.ymgme.2005.09.008 }}
  • {{cite journal | vauthors=Lanthier J, Desrosiers RR |title=Regulation of protein L-isoaspartyl methyltransferase by cell-matrix interactions: involvement of integrin alphavbeta3, PI 3-kinase, and the proteasome |journal=Biochem. Cell Biol. |volume=84 |issue= 5 |pages= 684–94 |year= 2007 |pmid= 17167531 |doi= 10.1139/o06-055 }}
  • {{cite journal |vauthors=Ewing RM, Chu P, Elisma F, etal |title=Large-scale mapping of human protein–protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue= 1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 }}

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