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Literature summary for 2.3.2.8 extracted from

  • Ribeiro, P.A.; Ribeiro, J.P.; Minozzo, F.C.; Pavlov, I.; Leu, N.A.; Kurosaka, S.; Kashina, A.; Rassier, D.E.
    Contractility of myofibrils from the heart and diaphragm muscles measured with atomic force cantilevers: effects of heart-specific deletion of arginyl-tRNA-protein transferase (2013), Int. J. Cardiol., 168, 3564-3571.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
myofibril
-
Mus musculus 30016
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arginyl-tRNAArg + protein Mus musculus
-
tRNAArg + L-arginyl-[protein]
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginyl-tRNAArg + protein
-
Mus musculus tRNAArg + L-arginyl-[protein]
-
?

Synonyms

Synonyms Comment Organism
arginyl-tRNA-protein transferase
-
Mus musculus
Ate1
-
Mus musculus

General Information

General Information Comment Organism
malfunction diaphragm myofibrils from enzyme-knockout mice produce an increased force compared to myofibrils from wild type Mus musculus