Streptolydigin

Streptolydigin
Clinical data
ATC code none
Identifiers
CAS Number 7229-50-7 N
PubChem (CID) 220508
DrugBank DB04785 YesY
ChemSpider 16736035 YesY
ChEBI CHEBI:45773 N
ChEMBL CHEMBL1236068 N
Chemical and physical data
Formula C32H44N2O9
Molar mass 600.708 g/mol
3D model (Jmol) Interactive image
 NYesY (what is this?)  (verify)

Streptolydigin (Stl) is an antibiotic that works by inhibiting nucleic acid chain elongation by binding to RNA polymerase, thus inhibiting RNA synthesis inside a cell.[1][2][3] Streptolydigin inhibits bacterial RNA polymerase, but not eukaryotic RNA polymerase.[4] It has antibacterial activity against a number of Gram positive bacteria.

References

  1. Tuske, S.; Sarafianos, S.; Wang, X.; Hudson, B.; Sineva, E.; Mukhopadhyay, J.; Birktoft, J.; Leroy, O.; Ismail, S.; Clark, A.; Dharia, C.; Napoli, A.; Laptenko, O.; Lee, J.; Borokhov, S.; Arnold, E.; Ebright, R. (2005). "Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation". Cell. 122 (4): 541–552. doi:10.1016/j.cell.2005.07.017. PMC 2754413Freely accessible. PMID 16122422.
  2. Temiakov, D; Zenkin, N; Vassylyeva, M. N.; Perederina, A; Tahirov, T. H.; Kashkina, E; Savkina, M; Zorov, S; Nikiforov, V; Igarashi, N; Matsugaki, N; Wakatsuki, S; Severinov, K; Vassylyev, D. G. (2005). "Structural basis of transcription inhibition by antibiotic streptolydigin". Molecular Cell. 19 (5): 655–66. doi:10.1016/j.molcel.2005.07.020. PMID 16167380.
  3. Vassylyev, D. G.; Vassylyeva, M. N.; Zhang, J; Palangat, M; Artsimovitch, I; Landick, R (2007). "Structural basis for substrate loading in bacterial RNA polymerase". Nature. 448 (7150): 163–8. doi:10.1038/nature05931. PMID 17581591.
  4. Tuske, S.; Sarafianos, S.; Wang, X.; Hudson, B.; Sineva, E.; Mukhopadhyay, J.; Birktoft, J.; Leroy, O.; Ismail, S.; Clark, A.; Dharia, C.; Napoli, A.; Laptenko, O.; Lee, J.; Borokhov, S.; Arnold, E.; Ebright, R. (2005). "Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation". Cell. 122 (4): 541–552. doi:10.1016/j.cell.2005.07.017. PMC 2754413Freely accessible. PMID 16122422.


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