EC Number   |
General Information |
Reference |
|---|
   2.1.1.221 | evolution |
aside from an active site aspartate residue, alignment of the available Trm10 protein structures and their primary sequences show no other obvious amino acid candidates in the active site that could account for the differences between m1G9-specific (Saccharomyces cerevisiae and Schizosaccharomyces pombe), m1A9-specific (Sulfolobus acidocaldarius) and m1A9/m1G9 dual-specific (human Trmt10C and Trm10 from Thermococcus kodakarensis) Trm10 MTases. It is possible that the purine specificity might simply be due to differences in surface charge around the active site and size and/or layout of the purine-binding pocket, which could allow different Trm10 family members to accommodate different purine substrates, rather than to specific residues for catalysis. The active site pocket is more open for the m1G9-specific Trmt10A and m1A9-specific Trm10, compared to the other Trm10 proteins. No obvious similarities are observed within the m1G9-specific group of proteins that are also clearly different from the m1A9-specific Trm10, and altered in the m1G9/m1A9 dual-specific protein |
-, 756160 |
| 2.1.1.221 | evolution |
N-1 methylation of the nearly invariant purine residue found at position 9 of tRNA is a nucleotide modification found in multiple tRNA species throughout Eukarya and Archaea |
737225 |
| 2.1.1.221 | evolution |
N-1 methylation of the nearly invariant purine residue found at position 9 of tRNA is a nucleotide modification found in multiple tRNA species throughout Eukarya and Archaea. The tRNA methyltransferase Trm10 is a highly conserved protein both necessary and sufficient to catalyze all known instances of m1G9 modification in yeast |
737225 |
| 2.1.1.221 | evolution |
the enzyme belongs to the tRNA m1R9 methyltransferase (Trm10) family, which is conserved throughout eukarya and archaea. Distinct substrate specificities of the human tRNA methyltransferases TRMT10A and TRMT10B. hTRMT10A and hTRMT10B are not biochemically redundant. hTRMT10A is the de facto methyltransferase responsible for all m1G9 formation on cytosolic tRNA, and hTRMT10B has a much more limited and specific role in tRNA processing in humans |
758328 |
| 2.1.1.221 | evolution |
the enzyme Trm10 belongs to the SPOUT superfamily. Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. The MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Trm10 from Schizosaccharomyces pombe demonstrates identical tRNA MTase activity as Trm10 from Saccharomyces cerevisiae |
-, 736903 |
| 2.1.1.221 | evolution |
tRNA m1G9 methyltransferase (Trm10) is a member of the SpoU-TrmD (SPOUT) superfamily of methyltransferases, and Trm10 homologs are widely conserved throughout eukarya and archaea. Despite possessing the trefoil knot characteristic of SPOUT enzymes, Trm10 does not share the same quaternary structure or key sequences with other members of the SPOUT family, suggesting a distinct mechanism of catalysis. Sequence comparison of human TRMT10A and yeast Trm10. Trm10 does not depend on a catalytic metal ion, further distinguishing it from the other known SPOUT m1G methyltransferase, TrmD |
-, 757847 |
| 2.1.1.221 | evolution |
tRNA m1G9 methyltransferase (Trm10) is a member of the SpoU-TrmD (SPOUT) superfamily of methyltransferases, and Trm10 homologs are widely conserved throughout eukarya and archaea. Despite possessing the trefoil knot characteristic of SPOUT enzymes, Trm10 does not share the same quaternary structure or key sequences with other members of the SPOUT family, suggesting a distinct mechanism of catalysis. Trm10 does not depend on a catalytic metal ion, further distinguishing it from the other known SPOUT m1G methyltransferase, TrmD |
757847 |
| 2.1.1.221 | malfunction |
guanine9 methylation activity is not detectable in trm10-DELTA/trm10-DELTA strain |
663384 |
| 2.1.1.221 | malfunction |
several disease states correlate with deficiency in the human homologue TRMT10A, mostly characterized by neurological and glucose metabolic defects, despite the presence of another cytoplasmic enzyme, TRMT10B |
758328 |
| 2.1.1.221 | malfunction |
TRMT10A silencing induces human beta-cell apoptosis.. TRMT10A deficiency negatively affects beta-cell mass and the pool of neurons in the developing brain. A nonsense mutation R127stop in the enzyme is involved in the syndrome of young onset diabetes, short stature and microcephaly (small brain size) with intellectual disability in a large consanguineous family, TRMT10A mRNA and protein are absent in cells from affected siblings, phenotype, overview. Patients are homozygous for a nonsense mutation in TRMT10A and lose TRMT10A expression |
737064 |
