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Literature summary for 2.1.1.268 extracted from

  • D'Silva, S.; Haider, S.J.; Phizicky, E.M.
    A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop (2011), RNA, 17, 1100-1110.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichi coli Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q08641
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-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + cytosine32 in tRNA1Thr tRNAThr1 = tRNAThr(IGU). Trm140p does not have detectable activity on a tRNAThr(IGU) transcript with a C32A mutation. No activity with tRNAPhe. It is demonstrated directly that ABP140 is required for the m3C modification of tRNAThr(IGU) in yeast, and it is infered that ABP140 is required for m3C32 formation for all six tRNAThr and tRNASer species for which m3C is documented Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
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Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
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assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction knockout strains in the yeast Saccharomyces cerevisiae lack N3-methylcytosine32 in tRNA1Thr. Lack of the m3C modification does impair translation, albeit mildly Saccharomyces cerevisiae