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{{ | '''Protein-L-isoaspartate(D-aspartate) O-methyltransferase''' is an [[enzyme]] that in humans is encoded by the ''PCMT1'' [[gene]].<ref name="pmid1478665">{{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 | pmc = | doi =10.1016/S0888-7543(05)80104-1 }}</ref><ref name="pmid10343128">{{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 | pmc = | doi =10.1159/000015239 }}</ref><ref name="entrez"/> | ||
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| summary_text = 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]<ref name="entrez">{{cite web | title = Entrez Gene: PCMT1 protein-L-isoaspartate (D-aspartate) O-methyltransferase| url = | | summary_text = 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]<ref name="entrez">{{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| accessdate = }}</ref> | ||
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==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{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 | | *{{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 | | *{{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 |pmid= 2684970 |doi= }} | ||
*{{cite journal | | *{{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 | | *{{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 | *{{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 }} | ||
*{{cite journal | | *{{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 | | *{{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 }} | ||
*{{cite journal | | *{{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 }} | ||
*{{cite journal | *{{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 }} | ||
*{{cite journal | *{{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 | *{{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 }} | ||
*{{cite journal | *{{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 }} | ||
*{{cite journal | *{{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 | *{{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 | *{{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 | *{{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 }} | ||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=5110}} | |||
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Latest revision as of 17:46, 7 September 2017
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| Species | Human | Mouse | |||||
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| Location (UCSC) | n/a | n/a | |||||
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Protein-L-isoaspartate(D-aspartate) O-methyltransferase is an enzyme that in humans is encoded by the PCMT1 gene.[1][2][3] 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][3]
References
- ↑ MacLaren DC, O'Connor CM, Xia YR, Mehrabian M, Klisak I, Sparkes RS, Clarke S, Lusis AJ (Feb 1993). "The L-isoaspartyl/D-aspartyl protein methyltransferase gene (PCMT1) maps to human chromosome 6q22.3-6q24 and the syntenic region of mouse chromosome 10". Genomics. 14 (4): 852–6. doi:10.1016/S0888-7543(05)80104-1. PMID 1478665.
- ↑ DeVry CG, Clarke S (Jun 1999). "Assignment of the protein L-isoaspartate (D-aspartate) O-methyltransferase gene (PCMT1) to human chromosome bands 6q24→q25 with radiation hybrid mapping". Cytogenet Cell Genet. 84 (1–2): 130–1. doi:10.1159/000015239. PMID 10343128.
- ↑ 3.0 3.1 "Entrez Gene: PCMT1 protein-L-isoaspartate (D-aspartate) O-methyltransferase".
Further reading
- MacLaren DC, Kagan RM, Clarke S (1992). "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 (1): 277–83. doi:10.1016/S0006-291X(05)80987-8. PMID 1339271.
- Ingrosso D, Kagan RM, Clarke S (1991). "Distinct C-terminal sequences of isozymes I and II of the human erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase". Biochem. Biophys. Res. Commun. 175 (1): 351–8. doi:10.1016/S0006-291X(05)81242-2. PMID 1998518.
- Ingrosso D, Fowler AV, Bleibaum J, Clarke S (1989). "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 (33): 20131–9. PMID 2684970.
- Gilbert JM, Fowler A, Bleibaum J, Clarke S (1988). "Purification of homologous protein carboxyl methyltransferase isozymes from human and bovine erythrocytes". Biochemistry. 27 (14): 5227–33. doi:10.1021/bi00414a042. PMID 3167043.
- Ota IM, Gilbert JM, Clarke S (1988). "Two major isozymes of the protein D-aspartyl/L-isoaspartyl methyltransferase from human erythrocytes". Biochem. Biophys. Res. Commun. 151 (3): 1136–43. doi:10.1016/S0006-291X(88)80484-4. PMID 3355545.
- Takeda R, Mizobuchi M, Murao K, et al. (1995). "Characterization of three cDNAs encoding two isozymes of an isoaspartyl protein carboxyl methyltransferase from human erythroid leukemia cells". J. Biochem. 117 (4): 683–5. doi:10.1093/jb/117.2.267. PMID 7592526.
- Tsai W, Clarke S (1994). "Amino acid polymorphisms of the human L-isoaspartyl/D-aspartyl methyltransferase involved in protein repair". Biochem. Biophys. Res. Commun. 203 (1): 491–7. doi:10.1006/bbrc.1994.2209. PMID 8074695.
- DeVry CG, Tsai W, Clarke S (1997). "Structure of the human gene encoding the protein repair L-isoaspartyl (D-aspartyl) O-methyltransferase". Arch. Biochem. Biophys. 335 (2): 321–32. doi:10.1006/abbi.1996.0513. PMID 8914929.
- DeVry CG, Clarke S (1999). "Polymorphic forms of the protein L-isoaspartate (D-aspartate) O-methyltransferase involved in the repair of age-damaged proteins". J. Hum. Genet. 44 (5): 275–88. doi:10.1007/s100380050161. PMID 10496068.
- Ryttersgaard C, Griffith SC, Sawaya MR, et al. (2002). "Crystal structure of human L-isoaspartyl methyltransferase". J. Biol. Chem. 277 (12): 10642–6. doi:10.1074/jbc.M200229200. PMID 11792715.
- Smith CD, Carson M, Friedman AM, et al. (2002). "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". Protein Sci. 11 (3): 625–35. doi:10.1110/ps.37802. PMC 2373461. PMID 11847284.
- Misra P, Qi C, Yu S, et al. (2002). "Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation". J. Biol. Chem. 277 (22): 20011–9. doi:10.1074/jbc.M201739200. PMID 11912212.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Enünlü I, Pápai G, Cserpán I, et al. (2003). "Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus". Biochem. Biophys. Res. Commun. 309 (1): 44–51. doi:10.1016/S0006-291X(03)01514-6. PMID 12943661.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Zhu H, Yang W, Lu W, et al. (2006). "A known functional polymorphism (Ile120Val) of the human PCMT1 gene and risk of spina bifida". Mol. Genet. Metab. 87 (1): 66–70. doi:10.1016/j.ymgme.2005.09.008. PMC 2947858. PMID 16256389.
- Lanthier J, Desrosiers RR (2007). "Regulation of protein L-isoaspartyl methyltransferase by cell-matrix interactions: involvement of integrin alphavbeta3, PI 3-kinase, and the proteasome". Biochem. Cell Biol. 84 (5): 684–94. doi:10.1139/o06-055. PMID 17167531.
- Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
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