Viomycin
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| Category | Antibiotics |
| Catalog number | BBF-03426 |
| CAS | 32988-50-4 |
| Molecular Weight | 685.69 |
| Molecular Formula | C25H43N13O10 |
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Description
Tuberactinomycin B is a member of the tuberactinomycin family of antibiotics used for the treatment of multidrug-resistant tuberculosis. Tuberactinomycin B inhibits group I intron splicing and prokaryotic protein synthesis, and freezes bacterial ribosomes in either the pre-or post-translational state.
Specification
| Synonyms | Tuberactinomycin B; Celiomycin; Florimycin; Viomicina; Viomycine; Viomycinum |
| Storage | Store at-20°C |
| IUPAC Name | 3,6-diamino-N-[(6Z)-3-(2-amino-4-hydroxy-1,4,5,6-tetrahydropyrimidin-6-yl)-6-[(carbamoylamino)methylidene]-9,12-bis(hydroxymethyl)-2,5,8,11,14-pentaoxo-1,4,7,10,13-pentazacyclohexadec-15-yl]hexanamide |
| Canonical SMILES | C1C(NC(=NC1O)N)C2C(=O)NCC(C(=O)NC(C(=O)NC(C(=O)NC(=CNC(=O)N)C(=O)N2)CO)CO)NC(=O)CC(CCCN)N |
| InChI | InChI=1S/C25H43N13O10/c26-3-1-2-10(27)4-16(41)32-12-6-30-23(47)18(11-5-17(42)37-24(28)36-11)38-20(44)13(7-31-25(29)48)33-21(45)14(8-39)35-22(46)15(9-40)34-19(12)43/h7,10-12,14-15,17-18,39-40,42H,1-6,8-9,26-27H2,(H,30,47)(H,32,41)(H,33,45)(H,34,43)(H,35,46)(H,38,44)(H3,28,36,37)(H3,29,31,48)/b13-7- |
| InChI Key | GXFAIFRPOKBQRV-QPEQYQDCSA-N |
Properties
| Appearance | White Powder |
| Application | the treatment of multidrug-resistant tuberculosis |
| Antibiotic Activity Spectrum | Gram-positive bacteria; Gram-negative bacteria; mycobacteria |
| Boiling Point | 695.81°C at 760 mmHg |
| Density | 1.36 g/cm3 |
| Solubility | Soluble to 75 mM in water |
Reference Reading
1.Molecular mechanism of viomycin inhibition of peptide elongation in bacteria.
Holm M1, Borg A1, Ehrenberg M1, Sanyal S2. Proc Natl Acad Sci U S A. 2016 Jan 26;113(4):978-83. doi: 10.1073/pnas.1517541113. Epub 2016 Jan 11.
Viomycin is a tuberactinomycin antibiotic essential for treating multidrug-resistant tuberculosis. It inhibits bacterial protein synthesis by blocking elongation factor G (EF-G) catalyzed translocation of messenger RNA on the ribosome. Here we have clarified the molecular aspects of viomycin inhibition of the elongating ribosome using pre-steady-state kinetics. We found that the probability of ribosome inhibition by viomycin depends on competition between viomycin and EF-G for binding to the pretranslocation ribosome, and that stable viomycin binding requires an A-site bound tRNA. Once bound, viomycin stalls the ribosome in a pretranslocation state for a minimum of ∼45 s. This stalling time increases linearly with viomycin concentration. Viomycin inhibition also promotes futile cycles of GTP hydrolysis by EF-G. Finally, we have constructed a kinetic model for viomycin inhibition of EF-G catalyzed translocation, allowing for testable predictions of tuberactinomycin action in vivo and facilitating in-depth understanding of resistance development against this important class of antibiotics.
2.From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases.
Shi D1,2, Allewell NM3,4, Tuchman M5,6. Int J Mol Sci. 2015 Aug 12;16(8):18836-64. doi: 10.3390/ijms160818836.
Enzymes in the transcarbamylase family catalyze the transfer of a carbamyl group from carbamyl phosphate (CP) to an amino group of a second substrate. The two best-characterized members, aspartate transcarbamylase (ATCase) and ornithine transcarbamylase (OTCase), are present in most organisms from bacteria to humans. Recently, structures of four new transcarbamylase members, N-acetyl-L-ornithine transcarbamylase (AOTCase), N-succinyl-L-ornithine transcarbamylase (SOTCase), ygeW encoded transcarbamylase (YTCase) and putrescine transcarbamylase (PTCase) have also been determined. Crystal structures of these enzymes have shown that they have a common overall fold with a trimer as their basic biological unit. The monomer structures share a common CP binding site in their N-terminal domain, but have different second substrate binding sites in their C-terminal domain. The discovery of three new transcarbamylases, l-2,3-diaminopropionate transcarbamylase (DPTCase), l-2,4-diaminobutyrate transcarbamylase (DBTCase) and ureidoglycine transcarbamylase (UGTCase), demonstrates that our knowledge and understanding of the spectrum of the transcarbamylase family is still incomplete.
3.Movement of elongation factor G between compact and extended conformations.
Salsi E1, Farah E1, Netter Z1, Dann J1, Ermolenko DN2. J Mol Biol. 2015 Jan 30;427(2):454-67. doi: 10.1016/j.jmb.2014.11.010. Epub 2014 Nov 15.
Previous structural studies suggested that ribosomal translocation is accompanied by large interdomain rearrangements of elongation factor G (EF-G). Here, we follow the movement of domain IV of EF-G relative to domain II of EF-G using ensemble and single-molecule Förster resonance energy transfer. Our results indicate that ribosome-free EF-G predominantly adopts a compact conformation that can also, albeit infrequently, transition into a more extended conformation in which domain IV moves away from domain II. By contrast, ribosome-bound EF-G predominantly adopts an extended conformation regardless of whether it is interacting with pretranslocation ribosomes or with posttranslocation ribosomes. Our data suggest that ribosome-bound EF-G may also occasionally sample at least one more compact conformation. GTP hydrolysis catalyzed by EF-G does not affect the relative stability of the observed conformations in ribosome-free and ribosome-bound EF-G.
4.Identification of differentially expressed genes and small molecule drugs for the treatment of tendinopathy using microarray analysis.
Cai X1, Cai M1, Lou L1. Mol Med Rep. 2015 Apr;11(4):3047-54. doi: 10.3892/mmr.2014.3081. Epub 2014 Dec 11.
Tendinopathy is a critical clinical problem as it is often asymptomatic at onset and during development, and is only recognized upon rupture of the tendon. It is common among recreational and competitive athletes. The present study sought to examine the molecular mechanism of the progression of tendinopathy by screening out differentially expressed genes (DEGs) and investigating their functions. In addition, the present study aimed to identify the small molecules, which exhibit potential effects, which could be utilized for the treatment of tendinopathy. The gene expression profile of tendinopathy, GSE26051 was downloaded from the Gene Expression Omnibus database, which included 23 control samples and 18 samples of tendinopathy. The DEGs were identified using the Limma package in the R programming language, and gene ontology and pathway enrichment analysis were performed. In addition, the potential regulatory microRNAs and the target sites of the transcription factors were screened out based on the molecular signature database.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
