Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
twitter

MetaCyc Reaction: 2.3.2.6

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: 2.3.2.6

Enzymes and Genes:
leucyl, phenylalanyl-tRNA-protein transferase Inferred from experiment : aat ( Escherichia coli K-12 substr. MG1655 )

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

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.

Citations: [Soffer73, Leibowitz69, Leibowitz70]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:2.3.2.6 , ENZYME:EC:2.3.2.6 , IUBMB-ExplorEnz:EC:2.3.2.6 , UniProt:RELATED-TO:P73571


References

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

Soffer73: Soffer RL (1973). "Peptide acceptors in the leucine, phenylalanine transfer reaction." J Biol Chem 248(24);8424-8. PMID: 4587124


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, BIOCYC13A.