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Literature summary for 2.5.1.75 extracted from

  • Zhou, C.; Huang, R.H.
    Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: insight into tRNA recognition and reaction mechanism (2008), Proc. Natl. Acad. Sci. USA, 105, 16142-16147.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
DMATase-tRNACys complex in four distinct forms, which provide snapshots of the RNA modification reaction catalyzed by DMATase Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P07884
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Reaction

Reaction Comment Organism Reaction ID
dimethylallyl diphosphate + adenine37 in tRNA = diphosphate + N6-dimethylallyladenine37 in tRNA ordered substrate binding Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme recognizes the tRNA substrate through indirect sequence readout. The targeted nucleotide A37 flips out from the anticodon loop of tRNA and flips into a channel in DMATase, where it meets its reaction partner dimethylallyl diphosphate, which enters the channel from the opposite end. Structural changes accompanying the transfer reaction result in disengagement of DMATase-tRNA interaction near the reaction center Saccharomyces cerevisiae ?
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Synonyms

Synonyms Comment Organism
DMATase
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Saccharomyces cerevisiae