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Literature summary extracted from

  • Powell, C.A.; Kopajtich, R.; DSouza, A.R.; Rorbach, J.; Kremer, L.S.; Husain, R.A.; Dallabona, C.; Donnini, C.; Alston, C.L.; Griffin, H.; Pyle, A.; Chinnery, P.F.; Strom, T.M.; Meitinger, T.; Rodenburg, R.J.; Schottmann, G.; Schuelke, M.; Romain, N.; Haller, R.G.; Ferrero, I.; Haack, T.B.; Taylor, R.W.; Pr, P.r.o.
    TRMT5 mutations cause a defect in post-transcriptional modification of mitochondrial tRNA associated with multiple respiratory-chain deficiencies (2015), Am. J. Hum. Genet., 97, 319-328.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.228 gene TRMT5, genetic structure and genotyping Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.228 M386V naturally occuring TRMT5 mutation, the mutant shows diminished G37 modification of a mitochondrial tRNA and a pathogenic phenotype Homo sapiens
2.1.1.228 additional information identification of TRMT5 enzyme mutants in patients, the loss of m1G37 does not appear to impact tRNA stability, phenotype, overview Homo sapiens
2.1.1.228 R291H naturally occuring TRMT5 mutation, the mutant shows diminished G37 modification of a mitochondrial tRNA and a pathogenic phenotype Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.1.228 mitochondrion
-
Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNA Homo sapiens
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.228 Homo sapiens
-
gene TRMT5
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.228 S-adenosyl-L-methionine + guanine37 in tRNA
-
Homo sapiens S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA
-
?

Subunits

EC Number Subunits Comment Organism
2.1.1.228 More three-dimensional enzyme model, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.1.1.228 Trm5p
-
Homo sapiens
2.1.1.228 tRNA methyltransferase 5
-
Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.228 S-adenosyl-L-methionine
-
Homo sapiens

General Information

EC Number General Information Comment Organism
2.1.1.228 evolution the enzyme shows strong homology to members of the class I-like methyltransferase superfamily Homo sapiens
2.1.1.228 malfunction mutations in TRMT5 are associated with the hypomodification of a guanosine residue at position 37 (G37) of mitochondrial tRNA, this hypomodification is particularly prominent in skeletal muscle. The patients show lactic acidosis and evidence of multiple mitochondrial respiratory-chain-complex deficiencies in skeletal muscle Homo sapiens
2.1.1.228 additional information three-dimensional enzyme model, overview Homo sapiens
2.1.1.228 physiological function methylation of G37 to form m1G acts to sterically block Watson-Crick base pairing and thereby both maintain an open loop conformation, by blocking base pairing with nucleotides elsewhere in the anticodon loop, and protect against frame shifting by preventing its interaction with the mRNA Homo sapiens