Streptolydigin

Streptolydigin
Clinical data
ATC code	none;
Identifiers
	IUPAC name 2-[4-[6-(1,6-dimethylspiro[8,9-dioxabicyclo[3.3.1]non-3-ene-2,2'-oxirane]-7;
CAS Number	7229-50-7 ;
PubChem CID	220508;
DrugBank	DB04785 ;
ChemSpider	16736035 ;
UNII	6MON4029Q8;
ChEBI	CHEBI:45773 ;
ChEMBL	ChEMBL1236068 ;
CompTox Dashboard (EPA)	DTXSID20905083 ;
Chemical and physical data
Formula	C32H44N2O9
Molar mass	600.709 g·mol−1
3D model (JSmol)	Interactive image;
	SMILES CNC(=O)C(C)C2C(=O)/C(C(=O)N2C1CCC(O)C(C)O1)=C(\O)/C=C/C(/C)=C/C(C)C5OC4(C)OC(\C=C/C34CO3)C5C;
	InChI InChI=1S/C32H44N2O9/c1-16(14-17(2)28-18(3)23-12-13-32(15-40-32)31(6,42-23)43-28)8-9-22(36)25-27(37)26(19(4)29(38)33-7)34(30(25)39)24-11-10-21(35)20(5)41-24/h8-9,12-14,17-21,23-24,26,28,35-36H,10-11,15H2,1-7H3,(H,33,38)/b9-8+,16-14+,25-22+ ; Key:KVTPRMVXYZKLIG-NCFIBNQNSA-N ;
	(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.^{[citation needed]}

References[edit]

^ Tuske S, Sarafianos SG, Wang X, Hudson B, Sineva E, Mukhopadhyay J, et al. (August 2005). "Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation". Cell. 122 (4): 541–52. doi:10.1016/j.cell.2005.07.017. PMC 2754413. PMID 16122422.
^ Temiakov D, Zenkin N, Vassylyeva MN, Perederina A, Tahirov TH, Kashkina E, et al. (September 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.
^ Vassylyev DG, Vassylyeva MN, Zhang J, Palangat M, Artsimovitch I, Landick R (July 2007). "Structural basis for substrate loading in bacterial RNA polymerase". Nature. 448 (7150): 163–8. arXiv:0707.3064. Bibcode:2007Natur.448..163V. doi:10.1038/nature05931. PMID 17581591. S2CID 4320480.
^ Tuske S, Sarafianos SG, Wang X, Hudson B, Sineva E, Mukhopadhyay J, et al. (August 2005). "Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation". Cell. 122 (4): 541–52. doi:10.1016/j.cell.2005.07.017. PMC 2754413. PMID 16122422.

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[1] Tuske S, Sarafianos SG, Wang X, Hudson B, Sineva E, Mukhopadhyay J, et al. (August 2005). "Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation". Cell. 122 (4): 541–52. doi:10.1016/j.cell.2005.07.017. PMC 2754413. PMID 16122422.

[2] Temiakov D, Zenkin N, Vassylyeva MN, Perederina A, Tahirov TH, Kashkina E, et al. (September 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 DG, Vassylyeva MN, Zhang J, Palangat M, Artsimovitch I, Landick R (July 2007). "Structural basis for substrate loading in bacterial RNA polymerase". Nature. 448 (7150): 163–8. arXiv:0707.3064. Bibcode:2007Natur.448..163V. doi:10.1038/nature05931. PMID 17581591. S2CID 4320480.

[4] Tuske S, Sarafianos SG, Wang X, Hudson B, Sineva E, Mukhopadhyay J, et al. (August 2005). "Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation". Cell. 122 (4): 541–52. doi:10.1016/j.cell.2005.07.017. PMC 2754413. PMID 16122422.

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