tRNA isopentenyltransferase

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
tRNA isopentenyltransferase
Identifiers
EC number2.5.1.8
CAS number37277-78-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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.

N6-Isopentenyladenosine

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2QGN.

gollark: This was a bit difficult when I learned about negative numbers but I eventually found a resolution.
gollark: This is why when I see any number, I simply imagine that many apples.
gollark: You jest, but intuitive perception of numbers is kind of weird.
gollark: Probably psychology a bit, like why people put .99 on the end of prices lots.
gollark: Historical quirks.

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.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.