Leucyltransferase
From Wikipedia the free encyclopedia
| leucyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.2.6 | ||||||||
| CAS no. | 37257-22-0 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
In enzymology, a leucyltransferase (EC 2.3.2.6) is an enzyme that catalyzes the chemical reaction
- L-leucyl-tRNA + protein 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.
Structural studies[edit]
As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes 2CXA, 2DPS, and 2DPT.
References[edit]
- 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 (1): 47–53. doi:10.1016/0006-291X(69)90647-0. 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 (8): 2066–73. PMID 4909560.
- Soffer RL (1973). "Peptide acceptors in the leucine, phenylalanine transfer reaction". J. Biol. Chem. 248 (24): 8424–8. PMID 4587124.
