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Literature summary for 2.1.1.228 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)

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

Protein Variants

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
gene TRMT5
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
Trm5p
-
Homo sapiens
tRNA methyltransferase 5
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
Homo sapiens

General Information

General Information Comment Organism
evolution the enzyme shows strong homology to members of the class I-like methyltransferase superfamily Homo sapiens
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
additional information three-dimensional enzyme model, overview Homo sapiens
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