tRNA isopentenyltransferase
| tRNA isopentenyltransferase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 2.5.1.8 | ||||||
| CAS number | 37277-78-4 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
|
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In enzymology, a tRNA isopentenyltransferase (EC 2.5.1.8) is an enzyme that catalyzes the chemical reaction
- isopentenyl diphosphate + tRNA
diphosphate + tRNA containing 6-isopentenyladenosine
Thus, the two substrates of this enzyme are isopentenyl diphosphate and tRNA, whereas its two products are diphosphate and tRNA containing 6-isopentenyladenosine.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is isopentenyl-diphosphate:tRNA isopentenyltransferase. Other names in common use include transfer ribonucleate isopentenyltransferase, Delta2-isopentenyl pyrophosphate:tRNA-Delta2-isopentenyl, transferase, Delta2-isopentenyl pyrophosphate:transfer ribonucleic acid, and Delta2-isopentenyltransferase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2QGN.
References
Literature
- Kline LK, Fittler F, Hall RH (1969). "N6-(Δ2-isopentenyl)adenosine. Biosynthesis in transfer ribonucleic acid in vitro". Biochemistry 8 (11): 4361–4371. doi:10.1021/bi00839a021. PMID 4311031.
- 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. PMID 4341485.