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Literature summary for 2.1.1.221 extracted from

  • Howell, N.; Jora, M.; Jepson, B.; Limbach, P.; Jackman, J.
    Distinct substrate specificities of the human tRNA methyltransferases TRMT10A and TRMT10B (2019), RNA, 25, 1366-1376 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.221

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information single-turnover kinetic analysis of the enzyme with representative tRNA substrates, tRNAArg, tRNATrp, and tRNAAsp Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Homo sapiens 5737
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + guanine9 in tRNA Homo sapiens
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
S-adenosyl-L-methionine + guanine9 in tRNAArg Homo sapiens
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAArg
-
 ?
S-adenosyl-L-methionine + guanine9 in tRNAAsp Homo sapiens
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAAsp
-
 ?
S-adenosyl-L-methionine + guanine9 in tRNATrp Homo sapiens
-
 S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNATrp
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8TBZ6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate specificity analysis and comparison of hTRMT10A and hTRMT10B enzymes, overview. hTRMT10A and hTRMT10B catalyze methylation of different tRNA substrates. hTRMT10A displays robust activity on every tested G9-containing tRNA from either humans or Saccharomyces cerevisiae, similar to Saccharomyces cerevisiae ScTrm10. hTRMT10B, and not hTRMT10A, is indeed capable of catalyzing m1A9 methylation on tRNAAsp in vitro, while hTRMT10B has the sole responsibility for generating the m1A9 modification. hTRMT10A displays higher in vitro catalytic rates than hTRMT10B Homo sapiens ?
-
-
S-adenosyl-L-methionine + guanine9 in tRNA
-
 Homo sapiens S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
 ?
S-adenosyl-L-methionine + guanine9 in tRNAArg
-
 Homo sapiens S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAArg
-
 ?
S-adenosyl-L-methionine + guanine9 in tRNAAsp
-
 Homo sapiens S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAAsp
-
 ?
S-adenosyl-L-methionine + guanine9 in tRNATrp
-
 Homo sapiens S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNATrp
-
 ?

Synonyms

Synonyms Comment Organism
hTRMT10A
-
 Homo sapiens
TRMT10A
-
 Homo sapiens
tRNA m1G9 methyltransferase
-
 Homo sapiens
tRNA m1R9 methyltransferase
-
 Homo sapiens

Cofactor

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

General Information

General Information Comment Organism
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 Homo sapiens
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 Homo sapiens
physiological function robust activity for hTRMT10A as a tRNAAsp-specific m1A9 methyltransferase, it is the relevant enzyme responsible for the m1A9 modification in humans. Inability of hTRMT10A to catalyze any detectable m1A9 modification Homo sapiens