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Literature summary for 2.3.1.193 extracted from

  • Ikeuchi, Y.; Kitahara, K.; Suzuki, T.
    The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon (2008), EMBO J., 27, 2194-2203.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
hexahistidine-tagged YpfI Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic parameters for ATP-hydrolysis or GTP-hydrolysis Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[elongator tRNAMet]-cytidine34 + ATP + acetyl-CoA Escherichia coli tRNAMet cytidine acetyltransferase acetylates the wobble base C34 of the elongation-specific tRNAMet. TmcA specifically recognizes the anticodon stem of tRNAMet, thus distinguishing between tRNAMet and tRNAIle2, which is structurally similar and has the same anticodon loop [elongator tRNAMet]-N4-acetylcytidine34 + ADP + phosphate + coenzyme A
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[elongator tRNAMet]-cytidine34 + ATP + acetyl-CoA tRNAMet cytidine acetyltransferase acetylates the wobble base C34 of the elongation-specific tRNAMet. TmcA specifically recognizes the anticodon stem of tRNAMet, thus distinguishing between tRNAMet and tRNAIle2, which is structurally similar and has the same anticodon loop Escherichia coli [elongator tRNAMet]-N4-acetylcytidine34 + ADP + phosphate + coenzyme A
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?
[elongator tRNAMet]-cytidine34 + ATP + acetyl-CoA ATP/GTP hydrolysis by TmcA is stimulated in the presence of acetyl-CoA and tRNAMet. TmcA hydrolyses ATP or GTP between the beta- and gamma-phosphates, as shown by the detection of labelled ADP (or GDP). A mutation study reveals that Escherichia coli TmcA strictly discriminates elongator tRNAMet from the structurally similar tRNAIle by mainly recognizing the C27–G43 pair in the anticodon stem Escherichia coli [elongator tRNAMet]-N4-acetylcytidine34 + ADP + phosphate + coenzyme A
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[elongator tRNAMet]-cytidine34 + GTP + acetyl-CoA
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Escherichia coli [elongator tRNAMet]-N4-acetylcytidine34 + GDP + phosphate + coenzyme A
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Synonyms

Synonyms Comment Organism
tmcA
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Escherichia coli
ypfI
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Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information kinetic parameters for ATP-hydrolysis or GTP-hydrolysis Escherichia coli

General Information

General Information Comment Organism
malfunction a tmcA deletion strain does not show a growth defect. Thus, this modification does not appear to be required for faithful translation in an otherwise wild-type strain. A tmcA/dusC double deletion strain has a severe cold-sensitive growth defect Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
additional information kinetic parameters for ATP-hydrolysis or GTP-hydrolysis Escherichia coli