Leucyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a leucyltransferase (EC 2.3.2.6) is an enzyme that catalyzes the chemical reaction

L-leucyl-tRNA + protein $\rightleftharpoons$ tRNA + L-leucyl-protein

Thus, the two substrates of this enzyme are L-leucyl-tRNA and protein, whereas its two products are tRNA and L-leucyl-protein.

This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is L-leucyl-tRNA:protein leucyltransferase. Other names in common use include leucyl, phenylalanine-tRNA-protein transferase, leucyl-phenylalanine-transfer ribonucleate-protein, aminoacyltransferase, and leucyl-phenylalanine-transfer ribonucleate-protein transferase.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2CXA, 2DPS, and 2DPT.

[edit] References

IUBMB entry for 2.3.2.6
BRENDA references for 2.3.2.6 (Recommended.)
PubMed references for 2.3.2.6
PubMed Central references for 2.3.2.6
Google Scholar references for 2.3.2.6
Leibowitz MJ, Soffer RL (1969). "A soluble enzyme from Escherichia coli which catalyzes the transfer of leucine and phenylalanine from tRNA to acceptor proteins". Biochem. Biophys. Res. Commun. 36: 47–53. PMID 4894363.
Leibowitz MJ, Soffer RL (1970). "Enzymatic modification of proteins. 3. Purification and properties of a leucyl, phenylalanyl transfer ribonucleic acid protein transferase from Escherichia coli". J. Biol. Chem. 245: 2066–73. PMID 4909560.
Soffer RL (1973). "Peptide acceptors in the leucine, phenylalanine transfer reaction". J. Biol. Chem. 248: 8424–8. PMID 4587124.