Tuberactinomycin A
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| Category | Antibiotics |
| Catalog number | BBF-02725 |
| CAS | 33103-21-8 |
| Molecular Weight | 701.69 |
| Molecular Formula | C25H43N13O11 |
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Description
Tuberactinomycin A is produced by the strain of Streptoverticillium griseoverticillatus var. tuberacticus B-386. It is effective against mycobacteria, but less effective against gram-positive and gram-negative bacteria.
Specification
| IUPAC Name | 3,6-diamino-N-[(6E)-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]-4-hydroxyhexanamide |
| 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(C(CCN)O)N |
| InChI | InChI=1S/C25H43N13O11/c26-2-1-15(41)9(27)3-16(42)32-11-5-30-23(48)18(10-4-17(43)37-24(28)36-10)38-20(45)12(6-31-25(29)49)33-21(46)13(7-39)35-22(47)14(8-40)34-19(11)44/h6,9-11,13-15,17-18,39-41,43H,1-5,7-8,26-27H2,(H,30,48)(H,32,42)(H,33,46)(H,34,44)(H,35,47)(H,38,45)(H3,28,36,37)(H3,29,31,49)/b12-6+ |
| InChI Key | JCTPGOAHEVLZAB-WUXMJOGZSA-N |
Properties
| Appearance | White Powder |
| Antibiotic Activity Spectrum | Gram-positive bacteria; Gram-negative bacteria; mycobacteria |
| Melting Point | ≥244°C |
| Density | 1.9±0.1 g/cm3 |
Reference Reading
1. Tuberactinomycin antibiotics: Biosynthesis, anti-mycobacterial action, and mechanisms of resistance
Zane T Laughlin, Graeme L Conn Front Microbiol. 2022 Aug 11;13:961921. doi: 10.3389/fmicb.2022.961921. eCollection 2022.
The tuberactinomycins are a family of cyclic peptide ribosome-targeting antibiotics with a long history of use as essential second-line treatments for drug-resistant tuberculosis. Beginning with the identification of viomycin in the early 1950s, this mini-review briefly describes tuberactinomycin structures and biosynthesis, as well as their past and present application in the treatment of tuberculosis caused by infection with Mycobacterium tuberculosis. More recent studies are also discussed that have revealed details of tuberactinomycin action on the ribosome as well as resistance mechanisms that have emerged since their introduction into the clinic. Finally, future applications of these drugs are considered in the context of their recent removal from the World Health Organization's List of Essential Medicines.
2. A Survey of Spontaneous Antibiotic-Resistant Mutants of the Halophilic, Thermophilic Bacterium Rhodothermus marinus
Sophia Silvia, Samantha A Donahue, Erin E Killeavy, Gerwald Jogl, Steven T Gregory Antibiotics (Basel). 2021 Nov 11;10(11):1384. doi: 10.3390/antibiotics10111384.
Rhodothermus marinus is a halophilic extreme thermophile, with potential as a model organism for studies of the structural basis of antibiotic resistance. In order to facilitate genetic studies of this organism, we have surveyed the antibiotic sensitivity spectrum of R. marinus and identified spontaneous antibiotic-resistant mutants. R. marinus is naturally insensitive to aminoglycosides, aminocylitols and tuberactinomycins that target the 30S ribosomal subunit, but is sensitive to all 50S ribosomal subunit-targeting antibiotics examined, including macrolides, lincosamides, streptogramin B, chloramphenicol, and thiostrepton. It is also sensitive to kirromycin and fusidic acid, which target protein synthesis factors. It is sensitive to rifampicin (RNA polymerase inhibitor) and to the fluoroquinolones ofloxacin and ciprofloxacin (DNA gyrase inhibitors), but insensitive to nalidixic acid. Drug-resistant mutants were identified using rifampicin, thiostrepton, erythromycin, spiramycin, tylosin, lincomycin, and chloramphenicol. The majority of these were found to have mutations that are similar or identical to those previously found in other species, while several novel mutations were identified. This study provides potential selectable markers for genetic manipulations and demonstrates the feasibility of using R. marinus as a model system for studies of ribosome and RNA polymerase structure, function, and evolution.
3. Molecular mechanism of viomycin inhibition of peptide elongation in bacteria
Mikael Holm, Anneli Borg, Måns Ehrenberg, Suparna Sanyal 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.
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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 ╳
