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Literature summary for 2.1.1.77 extracted from

  • 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 (2008), Plant Cell, 20, 3022-3037.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3)RIL cells Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Arabidopsis thaliana 5829
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
 ecotype Wassilewskija
-

Purification (Commentary)

Purification (Comment) Organism
MagneHis protein purification system Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + ovalbumin L-isoaspartate
-
 Arabidopsis thaliana S-adenosyl-L-homocysteine + ovalbumin L-isoaspartate alpha-methyl ester
-
 ?

Synonyms

Synonyms Comment Organism
L-isoaspartyl (D-aspartyl) O-methyltransferase
-
 Arabidopsis thaliana
PIMT1
-
 Arabidopsis thaliana
protein repair L-isoaspartyl methyltransferase 1
-
 Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Arabidopsis thaliana

General Information

General Information Comment Organism
malfunction reduced PIMT1 accumulation leads to heightened sensitivity to aging treatments and loss of seed vigor under stressful germination conditions Arabidopsis thaliana
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 Arabidopsis thaliana