Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

Information on EC 2.3.2.29 - aspartate/glutamate leucyltransferase

for references in articles please use BRENDA:EC2.3.2.29

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.

The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
N-terminal L-glutamyl-[protein]
=
+
N-terminal L-leucyl-L-glutamyl-[protein]
+
N-terminal L-aspartyl-[protein]
=
+
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)
-
-
-
L-leucyl-tRNALeu + N-terminal L-glutamyl-[protein] = tRNALeu + N-terminal L-leucyl-L-glutamyl-[protein]
show the reaction diagram
(1)
-
-
-
PATHWAY SOURCE
PATHWAYS
MetaCyc
N-end rule pathway II (prokaryotic)
Highest Expressing Human Cell Lines
Cell Line Links Gene Links