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Literature summary for 2.1.1.77 extracted from

  • Lyon, Y.A.; Sabbah, G.M.; Julian, R.R.
    Differences in alpha-crystallin isomerization reveal the activity of protein isoaspartyl methyltransferase (PIMT) in the nucleus and cortex of human lenses (2018), Exp. Eye Res., 171, 131-141 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.77

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + protein L-isoaspartate Homo sapiens
-
 S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
lens cortex the enzyme is more prevalent in the lens cortex than the nucleus Homo sapiens
-
lens nucleus
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + protein L-isoaspartate
-
 Homo sapiens S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
-
 ?

Synonyms

Synonyms Comment Organism
PIMT
-
 Homo sapiens
protein isoaspartyl methyltransferase
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function the enzyme plays a critical role in repairing isomerized Asp residues in the cortex of lenses Homo sapiens