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Information on EC 2.1.1.77 - protein-L-isoaspartate(D-aspartate) O-methyltransferase and Organism(s) Drosophila melanogaster and UniProt Accession Q27869

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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.
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This record set is specific for:
Drosophila melanogaster
UNIPROT: Q27869
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Word Map
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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-
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protein-beta-aspartate O-methyltransferase
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protein-L-isoaspartate O-methyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
105638-50-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + KASA(iso-D)LAKY
S-adenosyl-L-homocysteine + KASA(isoaspartate alpha-methyl ester)LAKY
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + KASA(iso-D)LAKY
S-adenosyl-L-homocysteine + KASA(L-isoaspartate alpha-methyl ester)LAKY
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + ovalbumin L-isoaspartate
S-adenosyl-L-homocysteine + ovalbumin L-isoaspartate alpha-methyl ester
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
show the reaction diagram
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
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + VYP(iso-D)HA
S-adenosyl-L-homocysteine + VYP(L-isoaspartate alpha-methyl ester)HA
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
show the reaction diagram
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
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0145 - 0.0286
KASA(iso-D)LAKY
0.0423 - 0.159
ovalbumin L-isoaspartate
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PIMT_DROME
226
0
24590
Swiss-Prot
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method, resolution of 2.2 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in transgenic flies extends the normal life span, suggesting that protein damage can be a limiting factor in longevity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team