CATH Classification

Domain Context

CATH Clusters

Superfamily Leucyl/phenylalanyl-tRNA-protein transferase, C-terminal domain
Functional Family Leucyl/phenylalanyl-tRNA--protein transferase

Enzyme Information

2.3.2.6
Lysine/arginine leucyltransferase.
based on mapping to UniProt P0A8P1
(1) L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = tRNA(Leu) + N-terminal L-leucyl-L-lysyl-[protein]. (2) L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] = tRNA(Leu) + N-terminal L-leucyl-L-arginyl-[protein].
-!- 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 enzyme also transfers L-phenylalanine in vitro, but this has not been observed in vivo. -!- Cf. EC 2.3.2.8 and EC 2.3.2.29.

UniProtKB Entries (1)

P0A8P1
LFTR_ECOLI
Escherichia coli K-12
Leucyl/phenylalanyl-tRNA--protein transferase

PDB Structure

PDB 2DPS
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog
Suto, K., Shimizu, Y., Watanabe, K., Ueda, T., Fukai, S., Nureki, O., Tomita, K.
Embo J.