Transferases;
Acyltransferases;
Aminoacyltransferases
BRITE hierarchy

L-leucyl-tRNALeu:[protein] N-terminal L-lysine/L-arginine leucyltransferase

(1) L-leucyl-tRNALeu + N-terminal L-lysyl-[protein] = tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]  [RN:R11443];
(2) L-leucyl-tRNALeu + N-terminal L-arginyl-[protein] = tRNALeu + N-terminal L-leucyl-L-arginyl-[protein] [RN:R11444]

R11443 R11444;
(other) R03813
Reaction

L-leucyl-tRNA(Leu) [CPD:C02047];
N-terminal L-lysyl-[protein] [CPD:C21388];
N-terminal L-arginyl-[protein] [CPD:C16739]

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.

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