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EC Tree
IUBMB Comments D-Aspartate (but not L-aspartate) residues in proteins can also act as acceptors. Previously also listed as EC 2.1.1.24.
The taxonomic range for the selected organisms is: Drosophila melanogaster The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pcm-1, pcmt1, protein l-isoaspartyl methyltransferase, l-isoaspartyl methyltransferase, pimt1, protein-l-isoaspartate (d-aspartate) o-methyltransferase, protein isoaspartyl methyltransferase, protein l-isoaspartate (d-aspartate) o-methyltransferase, protein-l-isoaspartyl methyltransferase, pimt2,
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protein L-isoaspartyl methyltransferase
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D-aspartyl/L-isoaspartyl methyltransferase
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L-aspartyl/L-isoaspartyl protein methyltransferase
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L-isoaspartyl/D-aspartyl protein carboxyl methyltransferase
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methyltransferase, protein (D-aspartate)
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protein (L-isoaspartate) O-methyltransferase
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protein D-aspartate methyltransferase
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protein L-isoaspartate methyltransferase
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protein L-isoaspartyl methyltransferase
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protein-beta-aspartate O-methyltransferase
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protein-L-isoaspartate O-methyltransferase
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methyl group transfer
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S-adenosyl-L-methionine:protein-L-isoaspartate O-methyltransferase
D-Aspartate (but not L-aspartate) residues in proteins can also act as acceptors. Previously also listed as EC 2.1.1.24.
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S-adenosyl-L-methionine + KASA(iso-D)LAKY
S-adenosyl-L-homocysteine + KASA(isoaspartate alpha-methyl ester)LAKY
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S-adenosyl-L-methionine + KASA(iso-D)LAKY
S-adenosyl-L-homocysteine + KASA(L-isoaspartate alpha-methyl ester)LAKY
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S-adenosyl-L-methionine + ovalbumin L-isoaspartate
S-adenosyl-L-homocysteine + ovalbumin L-isoaspartate alpha-methyl ester
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S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
the enzyme catalyzes the methylation of L-isoaspartyl residues that arise spontaneously in proteins with age, thereby initiating a repair process that restores the normal backbone configuration to the damaged polypeptide
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S-adenosyl-L-methionine + VYP(iso-D)HA
S-adenosyl-L-homocysteine + VYP(isoaspartate alpha-methyl ester)HA
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S-adenosyl-L-methionine + VYP(iso-D)HA
S-adenosyl-L-homocysteine + VYP(L-isoaspartate alpha-methyl ester)HA
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S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
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S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
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S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
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S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
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function in protein repair
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S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
the enzyme catalyzes the methylation of L-isoaspartyl residues that arise spontaneously in proteins with age, thereby initiating a repair process that restores the normal backbone configuration to the damaged polypeptide
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S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
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S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
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S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
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function in protein repair
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?
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0.0145 - 0.0286
KASA(iso-D)LAKY
0.0423 - 0.159
ovalbumin L-isoaspartate
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0.0145
KASA(iso-D)LAKY
wild-type enzyme
0.023
KASA(iso-D)LAKY
mutant enzyme S60Q
0.0286
KASA(iso-D)LAKY
mutant enzyme S60T
0.0423
ovalbumin L-isoaspartate
mutant enzyme S60Q
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0.121
ovalbumin L-isoaspartate
wild-type enzyme
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0.159
ovalbumin L-isoaspartate
mutant enzyme S60T
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Uniprot
brenda
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brenda
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PIMT_DROME
226
0
24590
Swiss-Prot
other Location (Reliability: 2 )
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sitting drop vapour diffusion method, resolution of 2.2 A
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S60A
inactive mutant protein
S60Q
the ratio of turnover number to KM-value for ovalbumin L-isoaspartate is 24.3fold lower than the wild-type value, the ratio of turnover-number to KM-value for KASA(iso-D)LAKY is 21fold lower than wild-type value
S60T
the ratio of turnover number to KM-value for ovalbumin L-isoaspartate is 6.2fold lower than the wild-type value, the ratio of turnover-number to KM-value for KASA(iso-D)LAKY is 2fold lower than the wild-type value
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overexpression in transgenic flies extends the normal life span, suggesting that protein damage can be a limiting factor in longevity
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Ingrosso, D.; Kagan, R.M.; Clarke, S.
Distinct C-terminal sequences of isozymes I and II of the human erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase [published erratum appears in Biochem Biophys Res Commun 1991 Apr 15;176(1):549]
Biochem. Biophys. Res. Commun.
175
351-358
1991
Bos taurus, Oryctolagus cuniculus, Drosophila melanogaster, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
David, C.L.; Pierce, V.A.; Aswad, D.W.; Gibbs, A.G.
The effect of urea exposure on isoaspartyl content and protein L-isoaspartate methyltransferase activity in Drosophila melanogaster
Comp. Biochem. Physiol. B
124B
423-427
1999
Drosophila melanogaster, Rattus norvegicus
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brenda
Thapar, N.; Clarke, S.
Expression, Purification, and Characterization of the Protein Repair L-Isoaspartyl Methyltransferase from Arabidopsis thaliana
Protein Expr. Purif.
20
237-251
2000
Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Escherichia coli, Homo sapiens, Oryza sativa, Rattus norvegicus, Solanum lycopersicum, Thermotoga maritima, Triticum aestivum, Xenopus laevis, Zea mays
brenda
Bennett, E.J.; Bjerregaard, J.; Knapp, J.E.; Chavous, D.A.; Friedman, A.M.; Royer, W.E., Jr.; O'Connor, C.M.
Catalytic implications from the Drosophila protein L-isoaspartyl methyltransferase structure and site-directed mutagenesis
Biochemistry
42
12844-12853
2003
Drosophila melanogaster (Q27869), Drosophila melanogaster
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