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Information on EC 2.3.2.29 - aspartate/glutamate leucyltransferase

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.29 aspartate/glutamate leucyltransferase
IUBMB Comments
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-aspartate or L-glutamate residue. Once modified, the proteins are recognized by EC 3.4.21.92, the ClpAP/ClpS endopeptidase system. cf. EC 2.3.2.6, lysine/arginine leucyltransferase, and EC 2.3.2.8, arginyltransferase.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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N-terminal L-glutamyl-[protein]
=
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N-terminal L-leucyl-L-glutamyl-[protein]
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N-terminal L-aspartyl-[protein]
=
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N-terminal L-leucyl-L-aspartyl-[protein]
Synonyms
bacterial protein transferase, BPT, LD,E-transferase, Leu-conjugating aa-transferase, leucylD,E-transferase, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-leucyl-tRNALeu + N-terminal L-aspartyl-[protein] = tRNALeu + N-terminal L-leucyl-L-aspartyl-[protein]
show the reaction diagram
(2)
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L-leucyl-tRNALeu + N-terminal L-glutamyl-[protein] = tRNALeu + N-terminal L-leucyl-L-glutamyl-[protein]
show the reaction diagram
(1)
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PATHWAY SOURCE
PATHWAYS
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