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Literature summary for 2.1.1.77 extracted from

  • Ota, I.M.; Ding, L.; Clarke, S.
    Methylation at specific altered aspartyl and asparaginyl residues in glucagon by the erythrocyte protein carboxyl methyltransferase (1987), J. Biol. Chem., 262, 8522-8531.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Homo sapiens 5829
-

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
-
human
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Homo sapiens
-
erythrocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
protein carboxyl methyltransferase type II
-
Homo sapiens