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2.3.1.193: tRNAMet cytidine acetyltransferase

This is an abbreviated version!
For detailed information about tRNAMet cytidine acetyltransferase, go to the full flat file.

Reaction

[elongator tRNAMet]-cytidine34
+
ATP
+
acetyl-CoA
+
H2O
=
CoA
+
[elongator tRNAMet]-N4-acetylcytidine34
+
ADP
+
phosphate

Synonyms

tmcA, ypfI

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.193 tRNAMet cytidine acetyltransferase

Crystallization

Crystallization on EC 2.3.1.193 - tRNAMet cytidine acetyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of tRNAMet cytidine acetyltransferase from Escherichia coli complexed with two natural ligands, acetyl-CoA and ADP, at 2.35 A resolution. The structure reveals an idiosyncratic RNA helicase module fused with a GCN5-related N-acetyltransferase (GNAT) fold, which intimately crossinteract. It is proposed that an RNA helicase motor driven by ATP hydrolysis is used to deliver the wobble base to the active centre of the GNAT domain