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Information on EC 2.1.1.77 - protein-L-isoaspartate(D-aspartate) O-methyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q64J17
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EC Tree
2.1.1.77 protein-L-isoaspartate(D-aspartate) O-methyltransferaseIUBMB 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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Word Map
- 2.1.1.77
-
deamidation
- centrosome
-
isomerized
-
age-damaged
- s-adenosylhomocysteine
- adomet
-
pericentriolar
-
l-asparaginyl
-
methyl-accepting
-
adohcy
-
centriolar
- s-adenosyl-l-homocysteine
-
3h-methylated
- succinimide
-
s-adenosyl-l-methyl-3hmethionine
-
dauers
- pericentrin
- medicine
-
dynactin
- biotechnology
- molecular biology
- nutrition
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pcm-1, pcmt1, protein l-isoaspartyl methyltransferase, l-isoaspartyl methyltransferase, protein-l-isoaspartate (d-aspartate) o-methyltransferase, pimt1, protein isoaspartyl methyltransferase, protein l-isoaspartate (d-aspartate) o-methyltransferase, protein-l-isoaspartyl methyltransferase, protein l-isoaspartyl o-methyltransferase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-aspartyl/L-isoaspartyl methyltransferase
-
-
-
-
L-aspartyl/L-isoaspartyl protein methyltransferase
-
-
-
-
L-isoaspartyl/D-aspartyl protein carboxyl methyltransferase
-
-
-
-
methyltransferase, protein (D-aspartate)
-
-
-
-
PIMT1
protein (L-isoaspartate) O-methyltransferase
-
-
-
-
protein D-aspartate methyltransferase
-
-
-
-
protein L-isoaspartate methyltransferase
-
-
-
-
protein L-isoaspartyl methyltransferase
protein-beta-aspartate O-methyltransferase
-
-
-
-
protein-L-isoaspartate O-methyltransferase
-
-
-
-
protein L-isoaspartyl methyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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
105638-50-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
S-adenosyl-L-methionine + 60 S ribosomal protein L27
S-adenosyl-L-homocysteine +
-
-
-
-
?
S-adenosyl-L-methionine + ATHSP17.4 protein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + bovine serum albumin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + carboxyesterase 12
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + cinnamoyl-CoA reductase family protein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + early flowering 8 protein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + gamma-globulin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + KASA-L-isoAsp-LAKY
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + mitochondrial glycoprotein family protein/MAM33
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + oligocellula 2 protein
S-adenosyl-L-homocysteine +
-
-
-
-
?
S-adenosyl-L-methionine + ovalbumin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + ovalbumin L-isoaspartate
S-adenosyl-L-homocysteine + ovalbumin L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + PIRL8 protein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + plant RNA helicase 75 L-isoaspartate
S-adenosyl-L-homocysteine + plant RNA helicase 75 L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + PRH75 protein
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate beta-methyl ester
S-adenosyl-L-methionine + protein D-isoaspartate
S-adenosyl-L-homocysteine + protein D-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
S-adenosyl-L-methionine + UDP-xylose synthase 5
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + VYP-(L-iso-Asp)-HA
S-adenosyl-L-homocysteine + VYP-(L-iso-Asp-alpha-methyl ester)-HA
-
-
-
-
?
S-adenosyl-L-methionine + VYP-L-isoAsp-CA
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + VYP-L-isoAsp-GHG
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + VYP-L-isoAsp-HA
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + VYP-L-isoAsp-RR
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
the spontaneous and deleterious conversion of L-asparaginyl and L-aspartyl protein residues to L-iso-Asp or D-Asp occurs as a proteins age and is accelerated under stressful conditions. Arabidopsis thaliana contains two genes (At3g48330 and At5g50240) encoding protein-L-isoaspartate methyltransferase, an enzyme capable of correcting this damage
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
the spontaneous and deleterious conversion of L-asparaginyl and L-aspartyl protein residues to L-iso-Asp or D-Asp occurs as a proteins age and is accelerated under stressful conditions. Arabidopsis thaliana Heynh. contains two genes (At3g48330 and At5g50240) encoding protein-L-isoaspartate methyltransferase, an enzyme capable of correcting this damage
-
-
?
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate beta-methyl ester
-
-
-
?
S-adenosyl-L-methionine + protein D-aspartate
S-adenosyl-L-homocysteine + protein D-aspartate beta-methyl ester
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
repair enzyme, methylates abnormal L-isoaspartate residues in proteins which arise spontaneously as a result of aging
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + plant RNA helicase 75 L-isoaspartate
S-adenosyl-L-homocysteine + plant RNA helicase 75 L-isoaspartate alpha-methyl ester
-
-
-
-
?
S-adenosyl-L-methionine + protein D-isoaspartate
S-adenosyl-L-homocysteine + protein D-isoaspartate alpha-methyl ester
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
S-adenosyl-L-methionine + protein L-isoaspartate
S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
repair enzyme, methylates abnormal L-isoaspartate residues in proteins which arise spontaneously as a result of aging
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Urea
-
recombinant enzyme relative activity is greatest in liquid assays in 1 M urea
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7
9.4
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PIMT1 expression is more or less similar regardless of stress. PIMT2 transcript abundance increases due to abscisic acid, drought-stress or salt-stress
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoforms PIMT2 TISIalphapsi and PIMT2 TISIalphaomega are predominately present in the chloroplasts, isoform PIMT2 TISIbetapsi is not observed in the chloroplast
-
isoforms PIMT2 TISIbetapsi, PIMT2 TISIalphapsi, and PIMT2 TISIalphaomega are predominately present in small, motile bodies suspected of being mitochondria
-
the PIMT2 TISIIalphapsi and alphaomega isoforms are prominent in the nucleus
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
reduced PIMT1 accumulation leads to heightened sensitivity to aging treatments and loss of seed vigor under stressful germination conditions
physiological function
physiological function
-
PIMT1 improves longevity and vigor of seeds, PIMT1 overaccumulation reduces the accumulation of L-isoaspartyl residues in seed proteins and increases both seed longevity and germination vigor
physiological function
-
enzyme activity is important to reduce stress-induced iso-Asp accumulation which otherwise affects plant growth and development and survivability under stress conditions. The enzyme restricts reactive oxygen species accumulation and lipid peroxidation during heat and oxidative stresses, by protecting functionality of antioxidant enzymes, and improves stress tolerance. Transgenic plants expressing either isoform PIMT1 or PIMT2 show increased stress tolerance, and survive better than the wild type plants under heat (37°C) and oxidative stress (H2O2) conditions
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PIMT2_ARATH
309
0
33986
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA isolation, pcm gene cloned and expressed in Escherichia coli BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
heat and oxidative stress treatments strongly induce PIMT1 and PIMT2 transcript expression
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mudgett, M.B.; Clarke, S.
A distinctly regulated protein repair L-isoaspartylmethyltransferase from Arabidopsis thaliana
Plant Mol. Biol.
30
723-737
1996
Arabidopsis thaliana, Escherichia coli, Homo sapiens, Mus musculus, Triticum aestivum
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
Thapar, N.; Kim, A.K.; Clarke, S.
Distinct patterns of expression but similar biochemical properties of protein L-isoaspartyl methyltransferase in higher plants
Plant Physiol.
125
1023-1035
2001
Arabidopsis thaliana, Caenorhabditis elegans, Caenorhabditis elegans N2, Daucus carota, Escherichia coli, Homo sapiens, Oryza sativa, Oryza sativa M-101, Triticum aestivum, Zea mays
Thapar, N.; Griffith, S.C.; Yeates, T.O.; Clarke, S.
Protein repair methyltransferase from the hyperthermophilic archaeon Pyrococcus furiosus: unusual methyl-accepting affinity for D-aspartyl and N-succinyl-containing peptides
J. Biol. Chem.
277
1058-1065
2002
Arabidopsis thaliana, Caenorhabditis elegans, Escherichia coli, Homo sapiens, Mus musculus, Pyrococcus furiosus, Thermotoga maritima
Xu, Q.; Belcastro, M.P.; Villa, S.T.; Dinkins, R.D.; Clarke, S.G.; Downie, A.B.
A second protein L-isoaspartyl methyltransferase gene in Arabidopsis produces two transcripts whose products are sequestered in the nucleus
Plant Physiol.
136
2652-2664
2004
Arabidopsis thaliana (Q64J17), Arabidopsis thaliana Heynh. (Q64J17)
Oge, L.; Bourdais, G.; Bove, J.; Collet, B.; Godin, B.; Granier, F.; Boutin, J.P.; Job, D.; Jullien, M.; Grappin, P.
Protein repair L-isoaspartyl methyltransferase 1 is involved in both seed longevity and germination vigor in Arabidopsis
Plant Cell
20
3022-3037
2008
Arabidopsis thaliana
Dinkins, R.D.; Majee, S.M.; Nayak, N.R.; Martin, D.; Xu, Q.; Belcastro, M.P.; Houtz, R.L.; Beach, C.M.; Downie, A.B.
Changing transcriptional initiation sites and alternative 5'- and 3'-splice site selection of the first intron deploys Arabidopsis protein isoaspartyl methyltransferase2 variants to different subcellular compartments
Plant J.
55
1-13
2008
Arabidopsis thaliana
Chen, T.; Nayak, N.; Majee, S.M.; Lowenson, J.; Schaefermeyer, K.R.; Eliopoulos, A.C.; Lloyd, T.D.; Dinkins, R.; Perry, S.E.; Forsthoefel, N.R.; Clarke, S.G.; Vernon, D.M.; Zhou, Z.S.; Rejtar, T.; Downie, A.B.
Substrates of the Arabidopsis thaliana protein isoaspartyl methyltransferase 1 identified using phage display and biopanning
J. Biol. Chem.
285
37281-37292
2010
Arabidopsis thaliana
Nayak, N.R.; Putnam, A.A.; Addepalli, B.; Lowenson, J.D.; Chen, T.; Jankowsky, E.; Perry, S.E.; Dinkins, R.D.; Limbach, P.A.; Clarke, S.G.; Downie, A.B.
An Arabidopsis ATP-dependent, DEAD-box RNA helicase loses activity upon IsoAsp formation but is restored by protein isoaspartyl methyltransferase
Plant Cell
25
2573-2586
2013
Arabidopsis thaliana
Ghosh, S.; Kamble, N.U.; Verma, P.; Salvi, P.; Petla, B.P.; Roy, S.; Rao, V.; Hazra, A.; Varshney, V.; Kaur, H.; Majee, M.
Arabidopsis protein L-isoaspartyl methyltransferaserepairs isoaspartyl damage to antioxidant enzymes and increases heat and oxidative stress tolerance
J. Biol. Chem.
295
783-799
2019
Arabidopsis thaliana
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