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Literature summary for 2.3.1.231 extracted from

  • Kato, M.; Araiso, Y.; Noma, A.; Nagao, A.; Suzuki, T.; Ishitani, R.; Nureki, O.
    Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification (2011), Nucleic Acids Res., 39, 1576-1585.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine72 in tRNAPhe + CO2 Saccharomyces cerevisiae the enzyme attaches both the methyl and methoxycarbonyl groups to the aminocarboxyl side chain, to complete wybutosine formation S-adenosyl-L-homocysteine + wybutosine in tRNAPhe
-
?
S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine72 in tRNAPhe + CO2 Saccharomyces cerevisiae BY4742 the enzyme attaches both the methyl and methoxycarbonyl groups to the aminocarboxyl side chain, to complete wybutosine formation S-adenosyl-L-homocysteine + wybutosine in tRNAPhe
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
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Saccharomyces cerevisiae BY4742
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine72 in tRNAPhe + CO2 the enzyme attaches both the methyl and methoxycarbonyl groups to the aminocarboxyl side chain, to complete wybutosine formation Saccharomyces cerevisiae S-adenosyl-L-homocysteine + wybutosine in tRNAPhe
-
?
S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine72 in tRNAPhe + CO2 the enzyme attaches both the methyl and methoxycarbonyl groups to the aminocarboxyl side chain, to complete wybutosine formation Saccharomyces cerevisiae BY4742 S-adenosyl-L-homocysteine + wybutosine in tRNAPhe
-
?

Synonyms

Synonyms Comment Organism
tRNA-yW synthesizing enzyme-4
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Saccharomyces cerevisiae
TYW4
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Saccharomyces cerevisiae