TRNA dimethylallyltransferase explained

TRNA dimethylallyltransferase
Ec Number:	2.5.1.75

TRNA dimethylallyltransferase (tRNA prenyltransferase, MiaA, transfer ribonucleate isopentenyltransferase, Delta2-isopentenyl pyrophosphate:tRNA-Delta2-isopentenyl transferase, Delta2-isopentenyl pyrophosphate:transfer ribonucleic acid Delta2-isopentenyltransferase) is an enzyme with systematic name dimethylallyl-diphosphate: tRNA dimethylallyltransferase.^{[1] [2] [3]} This enzyme catalyses the following chemical reaction

\rightleftharpoons diphosphate + tRNA containing 6-dimethylallyladenosine

Formerly known as tRNA isopentenyltransferase (EC 2.5.1.8), but it is now known that dimethylallyl diphosphate, rather than isopentenyl diphosphate, is the substrate.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .

Literature

• Kline LK, Fittler F, Hall RH . 1969 . N⁶-(Δ²-isopentenyl)adenosine. Biosynthesis in transfer ribonucleic acid in vitro . Biochemistry . 8 . 11 . 4361–4371 . 4311031 . 10.1021/bi00839a021 .
• Rosenbaum N, Gefter ML . 1972 . Δ²-Isopentenylpyrophosphate: Transfer Ribonucleic Acid Δ²-Isopentenyltransferase from Escherichia coli. Purification and properties of the enzyme . J. Biol. Chem. . 247 . 18 . 5675–5680 . 4341485 .

Notes and References

1. Leung HC, Chen Y, Winkler ME . Regulation of substrate recognition by the MiaA tRNA prenyltransferase modification enzyme of Escherichia coli K-12 . The Journal of Biological Chemistry . 272 . 20 . 13073–83 . May 1997 . 9148919 . 10.1074/jbc.272.20.13073 . free .
2. Soderberg T, Poulter CD . Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: essential elements for recognition of tRNA substrates within the anticodon stem-loop . Biochemistry . 39 . 21 . 6546–53 . May 2000 . 10828971 . 10.1021/bi992775u .
3. Moore JA, Mathis JR, Poulter CD . Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: pre-steady-state kinetic studies . Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology . 1479 . 1–2 . 166–74 . June 2000 . 11004538 . 10.1016/S0167-4838(00)00031-5 .