|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Polynucleotide-Reactions → RNA-Reactions → tRNA-Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions|
EC Number: 188.8.131.52
Enzymes and Genes:
|Escherichia coli K-12 substr. MG1655 :||leucyl, phenylalanyl-tRNA-protein transferase
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: leucyltransferase
Enzyme Commission Synonyms: leucyl, phenylalanine-tRNA-protein transferase, leucyl-phenylalanine-transfer ribonucleate-protein aminoacyltransferase, leucyl-phenylalanine-transfer ribonucleate-protein transferase, L-leucyl-tRNA:protein leucyltransferase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -1.1312561 [Latendresse13]
Enzyme Commission Summary:
Also transfers phenylalanyl groups. Requires a univalent cation. Peptides and proteins containing an N-terminal arginine, lysine or histidine residue can act as acceptors.
Leibowitz69: 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. PMID: 4894363
Leibowitz70: 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
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