|
|
Your query returned 1 entry. 
Printable version
| EC | 2.3.2.29 | ||
| Accepted name: | aspartate/glutamate leucyltransferase | ||
| Reaction: | (1) L-leucyl-tRNALeu + N-terminal L-glutamyl-[protein] = tRNALeu + N-terminal L-leucyl-L-glutamyl-[protein] (2) L-leucyl-tRNALeu + N-terminal L-aspartyl-[protein] = tRNALeu + N-terminal L-leucyl-L-aspartyl-[protein] |
||
| Other name(s): | leucylD,E-transferase; bpt (gene name) | ||
| Systematic name: | L-leucyl-tRNALeu:[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. | ||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||
| References: |
| ||