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
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2.3.2.6
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aminoacyl-trnas
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diphtheria
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toxin
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aa
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eubacterial
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ribosylation
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n-termini
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peptidoglycan
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trna-dependent
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cycloaddition
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non-ribosomal
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puromycin
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n-degrons
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alkyne
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transferase-mediated
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toxin-dependent
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leu-trnaleu
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synthesis
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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
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Systematic Name
Systematic Name on EC 2.3.2.6 - lysine/arginine leucyltransferase
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L-leucyl-tRNALeu:[protein] N-terminal L-lysine/L-arginine leucyltransferase
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.