ExplorEnz: EC 2.3.2.29

2.3.2.29

Accepted name:

aspartate/glutamate leucyltransferase

Reaction:

(1) L-leucyl-tRNA^Leu + N-terminal L-glutamyl-[protein] = tRNA^Leu + N-terminal L-leucyl-L-glutamyl-[protein]
(2) L-leucyl-tRNA^Leu + N-terminal L-aspartyl-[protein] = tRNA^Leu + N-terminal L-leucyl-L-aspartyl-[protein]

Other name(s):

leucylD,E-transferase; bpt (gene name)

Systematic name:

L-leucyl-tRNA^Leu:[protein] N-terminal L-glutamate/L-aspartate leucyltransferase

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.

References:

1.	Graciet, E., Hu, R.G., Piatkov, K., Rhee, J.H., Schwarz, E.M. and Varshavsky, A. Aminoacyl-transferases and the N-end rule pathway of prokaryotic/eukaryotic specificity in a human pathogen. Proc. Natl. Acad. Sci. USA 103 (2006) 3078–3083. [PMID: 16492767]

[EC 2.3.2.29 created 2016]