Streptolydigin: Difference between revisions
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<!--Clinical data--> |
<!--Clinical data--> |
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| pregnancy_category = |
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| legal_status = |
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| routes_of_administration = |
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<!--Pharmacokinetic data--> |
<!--Pharmacokinetic data--> |
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| bioavailability = |
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| protein_bound = |
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| metabolism = |
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| elimination_half-life = |
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| UNII = 6MON4029Q8 |
| UNII = 6MON4029Q8 |
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| ATC_prefix = none |
| ATC_prefix = none |
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| ATC_suffix = |
| ATC_suffix = |
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| ATC_supplemental = |
| ATC_supplemental = |
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| PubChem = 220508 |
| PubChem = 220508 |
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| DrugBank_Ref = {{drugbankcite|correct|drugbank}} |
| DrugBank_Ref = {{drugbankcite|correct|drugbank}} |
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| ChEMBL_Ref = {{ebicite|changed|EBI}} |
| ChEMBL_Ref = {{ebicite|changed|EBI}} |
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| ChEMBL = 1236068 |
| ChEMBL = 1236068 |
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| ChEBI_Ref = {{ebicite|changed|EBI}} |
| ChEBI_Ref = {{ebicite|changed|EBI}} |
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| ChEBI = 45773 |
| ChEBI = 45773 |
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<!--Chemical data--> |
<!--Chemical data--> |
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| C=32 | H=44 | N=2 | O=9 |
| C=32 | H=44 | N=2 | O=9 |
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| 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 |
| 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 |
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| StdInChI_Ref = {{stdinchicite|correct|chemspider}} |
| StdInChI_Ref = {{stdinchicite|correct|chemspider}} |
Revision as of 20:43, 8 January 2023
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CompTox Dashboard (EPA) | |
Chemical and physical data | |
Formula | C32H44N2O9 |
Molar mass | 600.709 g·mol−1 |
3D model (JSmol) | |
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(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
- ^ 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.