Cephabacin F1
* Please be kindly noted products are not for therapeutic use. We do not sell to patients.
| Category | Antibiotics |
| Catalog number | BBF-00533 |
| CAS | 95041-98-8 |
| Molecular Weight | 687.72 |
| Molecular Formula | C26H41N9O11S |
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Description
It is produced by the strain of Lysobacter lactamgenus YK-90, Xanthomonas lactamgena YK-278、YK-280 and YK-431. It has anti-gram positive and negative bacterial activity. The Cephabacin F series is stable and has inhibitory effect on cephalosporin enzyme.
Specification
| IUPAC Name | 7-[(5-amino-5-carboxypentanoyl)amino]-3-[[4-(2-aminopropanoylamino)-7-(diaminomethylideneamino)-3-hydroxyheptanoyl]oxymethyl]-7-formamido-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid |
Properties
| Appearance | Powder |
| Antibiotic Activity Spectrum | Gram-positive bacteria; Gram-negative bacteria |
| Solubility | Soluble in Water |
Reference Reading
1. Cephabacins, new cephem antibiotics of bacterial origin. IV. Antibacterial activities, stability to beta-lactamases and mode of action
Y Nozaki, K Okonogi, N Katayama, H Ono, S Harada, M Kondo, H Okazaki J Antibiot (Tokyo). 1984 Dec;37(12):1555-65. doi: 10.7164/antibiotics.37.1555.
Cephabacin F group antibiotics with a 7-formylamino substituent showed antibacterial activity against a wide variety of bacteria including beta-lactamase-producing clinical isolates and anaerobic bacteria. Cephabacin H group antibiotics without the substituent showed more potent activity against Gram-positive bacteria than cephabacin F group antibiotics, but were not active against Gram-negative bacteria producing beta-lactamases. Cephabacin F group antibiotics were highly resistant to hydrolysis by various types of beta-lactamases and showed strong inhibitory activity against a cephalosporinase of Proteus vulgalis GN 4413 due to the 7-formylamino substituent. Mode of action of cephabacin F1 and H1 was examined using Escherichia coli and Bacillus subtilis as the test organisms. They showed strong lytic activity against these organisms and inhibited their peptidoglycan synthesis. Cephabacin F1 had the highest affinity for penicillin-binding protein (PBP) 1 in E. coli and PBP 4 in B. subtilis. Cephabacins showed a protective effect in experimentally infected mice.
2. Cephabacins, new cephem antibiotics of bacterial origin. III. Structural determination
S Tsubotani, T Hida, F Kasahara, Y Wada, S Harada J Antibiot (Tokyo). 1984 Dec;37(12):1546-54. doi: 10.7164/antibiotics.37.1546.
The structures of 15 new cephem antibiotics, cephabacin F1-9 and H1-6, were determined by their spectroscopic analyses and decomposition studies. They are consisted of a cephalosporin nucleus and a di, tri or tetrapeptide including a new amino acid which is bound at the position 3 with an ester bond. The components, F1-9, showed unique biological activities by the presence of a formylamino group at the position 7.
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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 ╳
