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Literature summary for 2.1.1.219 extracted from

  • Guelorget, A.; Roovers, M.; Guérineau, V.; Barbey, C.; Li, X.; Golinelli-Pimpaneau, B.
    Insights into the hyperthermostability and unusual region-specificity of archaeal Pyrococcus abyssi tRNA m1A57/58 methyltransferase (2010), Nucleic Acids Res., 38, 6206-6218.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure TrmI in complex with SAH is determined in two different space groups at 2.6 and 2.05 A resolution, and in complex with S-adenosyl-L-methionine (SAM) at 1.6 A resolution Pyrococcus abyssi

Organism

Organism UniProt Comment Textmining
Pyrococcus abyssi Q9V1J7
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-

Purification (Commentary)

Purification (Comment) Organism
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Pyrococcus abyssi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + adenine57/adenine58 in tRNAAsp the presence of adenine at position 59 in Pyrococcus abyssi tRNA(Asp) is important for the multi-site specificity of the archaeal enzyme at both positions 57 and 58 in tRNAAsp. His78 near the active site is important for efficient catalysis Pyrococcus abyssi 2 S-adenosyl-L-homocysteine + N1-methyladenine57/N1-methyladenine58 in tRNAAsp
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Synonyms

Synonyms Comment Organism
TrmI
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Pyrococcus abyssi
tRNA m1A57/58 methyltransferase
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Pyrococcus abyssi