EC 2.3.2.6 - Lysine/arginine leucyltransferase

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IntEnz Enzyme Nomenclature
EC 2.3.2.6

Names

Accepted name:
lysine/arginine leucyltransferase
Other names:
leucyl, phenylalanine-tRNA-protein transferase
leucyl-phenylalanine-transfer ribonucleate-protein aminoacyltransferase
leucyl-phenylalanine-transfer ribonucleate-protein transferase
leucyl/phenylalanyl-tRNA--protein transferase
leucyl-tRNA--protein transferase
L/F transferase
L-leucyl-tRNA:protein leucyltransferase
leucyltransferase [misleading]
L/FK,R-transferase
aat (gene name)
L-leucyl-tRNALeu:protein leucyltransferase
Systematic name:
L-leucyl-tRNALeu:[protein] N-terminal L-lysine/L-arginine leucyltransferase

Reactions

Cofactor

Comments:

Requires a univalent cation. The enzyme participates in the N-end rule protein degradation pathway in certain bacteria, by attaching the primary destabilizing residue L-leucine to the N-termini of proteins that have an N-terminal L-arginine or L-lysine residue. Once modified, the proteins are recognized by EC 3.4.21.92, the ClpAP/ClpS endopeptidase system. The enzyme also transfers L-phenylalanine in vitro, but this has not been observed in vivo [5]. cf. EC 2.3.2.29, aspartate/glutamate leucyltransferase, and EC 2.3.2.8, arginyltransferase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008914
CAS Registry Number: 37257-22-0
UniProtKB/Swiss-Prot: (305) [show] [UniProt]

References

  1. Leibowitz, M.J. and Soffer, R.L.
    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 (1969). [PMID: 4894363]
  2. Leibowitz, M.J. and Soffer, R.L.
    Enzymatic modification of proteins. 3. Purification and properties of a leucyl, phenylalanyl transfer ribonucleic acid protein transferase from Escherichia coli.
    J. Biol. Chem. 245: 2066-2073 (1970). [PMID: 4909560]
  3. Soffer, R.L.
    Peptide acceptors in the leucine, phenylalanine transfer reaction.
    J. Biol. Chem. 248: 8424-8428 (1973). [PMID: 4587124]
  4. Tobias, J. W., Shrader, T. E., Rocap, G., Varshavsky, A.
    The N-end rule in bacteria.
    Science 254: 1374-1377 (1991). [PMID: 1962196]
  5. Shrader, T. E., Tobias, J. W., Varshavsky, A.
    The N-end rule in Escherichia coli: cloning and analysis of the leucyl, phenylalanyl-tRNA-protein transferase gene aat.
    J. Bacteriol. 175: 4364-4374 (1993). [PMID: 8331068]
  6. Abramochkin, G., Shrader, T. E.
    The leucyl/phenylalanyl-tRNA-protein transferase. Overexpression and characterization of substrate recognition, domain structure, and secondary structure.
    J. Biol. Chem. 270: 20621-20628 (1995). [PMID: 7657641]

[EC 2.3.2.6 created 1972, modified 1976, modified 2013, modified 2016]