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

BRENDA support

Literature summary for 3.4.25.2 extracted from

  • Bogyo, M.; McMaster, J.S.; Gaczynska, M.; Tortorella, D.; Goldberg, A.L.; Ploegh, H.
    Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors (1997), Proc. Natl. Acad. Sci. USA, 94, 6629-6634.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
additional information the I125-labeled nitrophenyl derivative 125iodo-NIP-Leu-Leu-Leu vinyl sulfone covalently modifies and inhibits HslV, but only in presence of HslU and ATP Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-