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Literature summary for 2.1.1.77 extracted from

  • Kharbanda, K.K.; Mailliard, M.E.; Baldwin, C.R.; Sorrell, M.F.; Tuma, D.J.
    Accumulation of proteins bearing atypical isoaspartyl residues in livers of alcohol-fed rats is prevented by betaine administration: effects on protein-L-isoaspartyl methyltransferase activity (2007), J. Hepatol., 46, 1119-1125.
    View publication on PubMed

Application

Application Comment Organism
molecular biology betaine administration of rats prevents the ethanol-induced accumulation of isoaspartyl-containing proteins in the liver by restoring the PIMT-catalyzed protein repair reaction through normalizing the hepatocellular SAM:SAH ratios Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information livers of male Wistar rats, fed the Lieber DeCarli control, ethanol or 1% betaine-supplemented diets for 4 weeks, are processed for PIMT-related analyses. A significant increase in the accumulation of modified proteins bearing isoaspartyl residues (substrates for PIMT), in homogenate samples and various subcellular fractions of livers from ethanol-fed rats are observed. Betaine supplementation prevents this accumulation of damaged proteins. Ethanol exposure induces no changes in the PIMT enzyme activity levels as compared to controls. The accumulation of damaged proteins negatively correlates with hepatic S-adenosylmethionine to S-adenosylhomocysteine ratios Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Synonyms

Synonyms Comment Organism
PIMT
-
Rattus norvegicus
protein L-isoaspartyl methyltransferase
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Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Rattus norvegicus