Celesticetin B
* Please be kindly noted products are not for therapeutic use. We do not sell to patients.
| Category | Antibiotics |
| Catalog number | BBF-00502 |
| CAS | 42715-01-5 |
| Molecular Weight | 478.60 |
| Molecular Formula | C21H38N2O8S |
Online Inquiry
Description
It is produced by the strain of Streptomyces caelestis NRRL 2418. It has anti-gram-positive bacterial activity.
Specification
| Synonyms | Isobutyric acid 2-((2R,3R,4S,5R,6R)-3,4,5-trihydroxy-6-{(R)-2-methoxy-1-[(1-methyl-pyrrolidine-2-carbonyl)-amino]-propyl}-tetrahydro-pyran-2-ylsulfanyl)-ethyl ester |
| IUPAC Name | 2-[(3R,4S,5S,6R)-3,4,5-trihydroxy-6-[(1R,2R)-2-methoxy-1-[[(2S)-1-methylpyrrolidine-2-carbonyl]amino]propyl]oxan-2-yl]sulfanylethyl 2-methylpropanoate |
| Canonical SMILES | CC(C)C(=O)OCCSC1C(C(C(C(O1)C(C(C)OC)NC(=O)C2CCCN2C)O)O)O |
| InChI | InChI=1S/C21H38N2O8S/c1-11(2)20(28)30-9-10-32-21-17(26)15(24)16(25)18(31-21)14(12(3)29-5)22-19(27)13-7-6-8-23(13)4/h11-18,21,24-26H,6-10H2,1-5H3,(H,22,27)/t12-,13+,14-,15+,16+,17-,18-,21?/m1/s1 |
| InChI Key | SHQMPFKIVLYSCS-LXVYJZGXSA-N |
Properties
| Solubility | Soluble in Water |
Reference Reading
1. Induction of ermSV by 16-membered-ring macrolide antibiotics
S Kamimiya, B Weisblum Antimicrob Agents Chemother. 1997 Mar;41(3):530-4. doi: 10.1128/AAC.41.3.530.
The erm family of 23S rRNA adenine-N6-methyltransferases confers resistance to all macrolide-lincosamide-streptograminB (MLS) antibiotics, but not all MLS antibiotics induce synthesis of Erm methyltransferase with equal efficiency in a given organism. The induction efficiency of a test panel of MLS antibiotics was studied by using two translational attenuator-lac reporter gene fusion constructs, one based on ermSV from Streptomyces viridochromogenes NRRL 2860 and the other based on ermC from Staphylococcus aureus RN2442. Four types of responses which were correlated with the macrolide ring size were seen, as follows: group 1, both ermSV and ermC were induced by the 14-membered-ring macrolides erythromycin, lankamycin, and matromycin, as well as by the lincosamide celesticetin; group 2, neither ermSV nor ermC was induced by the 12-membered-ring macrolide methymycin or by the lincosamide lincomycin or the streptogramin type B antibiotic ostreogrycin B; group 3, ermSV was selectively induced over ermC by the 16-membered-ring macrolides carbomycin, chalcomycin, cirramycin, kitasamycin, maridomycin, and tylosin; and group 4, ermC was selectively induced over ermSV by the 14-membered-ring macrolide megalomicin. These data suggest that the leader peptide determines the specificity of induction by different classes of MLS antibiotics and that for a given attenuator, a major factor which determines whether a given macrolide induces resistance is its size.
2. Macrolide resistance in Staphylococcus aureus: inducers of macrolide resistance
N E Allen Antimicrob Agents Chemother. 1977 Apr;11(4):669-74. doi: 10.1128/AAC.11.4.669.
Several macrolide-, lincosamide-, and streptogramin B-type (MLS) antibiotics were tested as inducers of erythromycin A (EM)-resistant [(14)C]leucine incorporation. Only 14-membered-ring macrolides having a glycosidically linked 6-deoxy sugar at the C-3 position of the lactone ring and the structurally dissimilar lincosamide, celesticetin, showed inducer activity. Modifications of EM at the C-4'' position of cladinose can apparently destroy the inducer property but do not affect the inhibitory properties of the antibiotic. The findings clearly show that inducer and inhibitor activities can be dissociated and are consistent with the concept that distinct binding/receptor sites are utilized for inhibition of ribosome function and induction of resistance.
3. The ermC leader peptide: amino acid alterations leading to differential efficiency of induction by macrolide-lincosamide-streptogramin B antibiotics
M Mayford, B Weisblum J Bacteriol. 1990 Jul;172(7):3772-9. doi: 10.1128/jb.172.7.3772-3779.1990.
The inducibility of ermC by erythromycin, megalomicin, and celesticetin was tested with both wild-type ermC and several regulatory mutants altered in the 19-amino-acid-residue leader peptide, MGIFSIFVISTVHYQP NKK. In the model test system that was used, the ErmC methylase was translationally fused to beta-galactosidase. Mutational alterations that mapped in the interval encoding Phe-4 through Ile-9 of the leader peptide not only affected induction by individual antibiotics, but did so differentially. The subset of mutations that affected inducibility by the two macrolides erythromycin and megalomicin overlapped and were distinct from the subset of mutations that affected induction by celesticetin. These studies provide a model system for experimentally varying the relative efficiencies with which different antibiotics induce the expression of ermC. The possibility that antibiotics with inducing activity interact directly with the nascent leader peptide was tested by using a chemically synthesized decapeptide, MGIFSIFVIS--, attached at its C-terminus to a solid-phase support. This peptide, however, failed to bind erythromycin in vitro.
Recommended Products
| BBF-03754 | Castanospermine | Inquiry |
| BBF-02642 | Lactonamycin | Inquiry |
| BBF-05862 | Epirubicin | Inquiry |
| BBF-01826 | Deoxymannojirimycin | Inquiry |
| BBF-01825 | Loganin | Inquiry |
| BBF-01829 | Deoxynojirimycin | Inquiry |
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 ╳
