2.3.2.6: lysine/arginine leucyltransferase

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For detailed information about lysine/arginine leucyltransferase, go to the full flat file.

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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

     2 Transferases

         2.3 Acyltransferases

             2.3.2 Aminoacyltransferases

                2.3.2.6 lysine/arginine leucyltransferase

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Results	in table
2	Activating Compound
19074	AA Sequence
3	Application
1	CAS Registry Number
4	Cloned(Commentary)
5	Crystallization (Commentary)
5	General Information
1	General Stability
33	Inhibitors
4	kcat/KM [mM/s]
22	Ki Value [mM]
11	KM Value [mM]
8	Localization
5	Metals/Ions
9	Natural Substrates/ Products (Substrates)
730	Organism
1	Pathway
17	PDB ID
3	pH Optimum
1	pH Range
7	Protein Variants
7	Purification (Commentary)
3	Reaction
3	Reaction Type
28	Reference
4	Specific Activity [micromol/min/mg]
4	Storage Stability
81	Substrates and Products (Substrate)
33	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Stability [°C]
10	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 2.3.2.6 - lysine/arginine leucyltransferase

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SYSTEMATIC NAME

IUBMB Comments

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.