2.3.2.6: lysine/arginine leucyltransferase
This is an abbreviated version!
For detailed information about lysine/arginine leucyltransferase, go to the full flat file.
Word Map on EC 2.3.2.6
-
2.3.2.6
-
aminoacyl-trnas
-
diphtheria
-
toxin
-
aa
-
eubacterial
-
ribosylation
-
n-termini
-
peptidoglycan
-
trna-dependent
-
cycloaddition
-
non-ribosomal
-
puromycin
-
n-degrons
-
alkyne
-
transferase-mediated
-
toxin-dependent
-
leu-trnaleu
-
synthesis
-
analysis
- 2.3.2.6
- aminoacyl-trnas
- diphtheria
- toxin
- aa
-
eubacterial
-
ribosylation
-
n-termini
- peptidoglycan
-
trna-dependent
-
cycloaddition
-
non-ribosomal
- puromycin
-
n-degrons
-
alkyne
-
transferase-mediated
-
toxin-dependent
- leu-trnaleu
- synthesis
- analysis
Reaction
Synonyms
AAT, aminoacyl transferase, aminoacyl tRNA protein transferase, L/F transferase, L/F-transferase, L/F-tRNA-protein transferase, leucyl, phenylalanine-tRNA-protein transferase, leucyl, phenylalanyl transfer ribonucleic acid-protein transferase, leucyl-phenylalanine-transfer ribonucleate-protein aminoacyltransferase, leucyl-phenylalanine-transfer ribonucleate-protein transferase, leucyl/phenylalaninyl tRNA protein transferase, leucyl/phenylalanyl tRNA protein transferase, leucyl/phenylalanyl-tRNA protein transferase, leucyl/phenylalanyl-tRNA-protein transferase, leucyltransferase, LF-transferase, LFTR, R/K-transferase
ECTree
Advanced search results
Crystallization
Crystallization on EC 2.3.2.6 - lysine/arginine leucyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
crystal structures of the Escherichia coli LF-transferase complex with phenyalanyl adenosine (rA-Phe), with or without a short peptide bearing an N-terminal Arg residue. In the presence of both the donor and acceptor substrates, the peptide formation proceedes within the crystals, and the product peptide bearing Phe at the N terminus is retained on the LF-transferase
enzyme adopts a monomeric structure consisting of two domains that form a bilobate molecule. The n-terminal domain forms a small lobe with an unusual fold. The large C-terminal domain has a highly conserved fold. Comparison with bacterial peptidoglycan synthase FemX
in complex with minimal substrate phenylalanyl adenosine inhibitor puromycin
-
in complex with puromycin. The p-methoxybenzyl group of puromycin is accomodated in a highly hydrophobic pocket. Model of complex with tRNA and a substrate bearing an N-terminal Arg or Lys