Oganomycin A
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| Category | Bioactive by-products |
| Catalog number | BBF-02146 |
| CAS | 75794-94-4 |
| Molecular Weight | 629.61 |
| Molecular Formula | C24H27N3O13S2 |
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Description
Oganomycin A is produced by the strain of Str. oganonensis Y-G 19Z. It is more stable than cephalosporin and resistant to gram-positive and negative bacteria. And it is more effective against gram-negative bacteria than gram-positive bacteria.
Specification
| IUPAC Name | (6R,7S)-7-[[(5R)-5-amino-5-carboxypentanoyl]amino]-7-methoxy-8-oxo-3-[[(E)-3-(4-sulfooxyphenyl)prop-2-enoyl]oxymethyl]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid |
| Canonical SMILES | COC1(C2N(C1=O)C(=C(CS2)COC(=O)C=CC3=CC=C(C=C3)OS(=O)(=O)O)C(=O)O)NC(=O)CCCC(C(=O)O)N |
| InChI | InChI=1S/C24H27N3O13S2/c1-38-24(26-17(28)4-2-3-16(25)20(30)31)22(34)27-19(21(32)33)14(12-41-23(24)27)11-39-18(29)10-7-13-5-8-15(9-6-13)40-42(35,36)37/h5-10,16,23H,2-4,11-12,25H2,1H3,(H,26,28)(H,30,31)(H,32,33)(H,35,36,37)/b10-7+/t16-,23-,24+/m1/s1 |
| InChI Key | WZUOYYCVBUQXEE-CULMAWHJSA-N |
Properties
| Antibiotic Activity Spectrum | Gram-positive bacteria; Gram-negative bacteria |
Reference Reading
1. Measurement of stress-induced Ca(2+) pulses in single aequorin-transformed tobacco cells
S G Cessna, M A Messerli, K R Robinson, P S Low Cell Calcium. 2001 Sep;30(3):151-6. doi: 10.1054/ceca.2001.0226.
Signaling patterns measured in large cell populations are the sum of differing signals from separate cells, and thus, the detailed kinetics of Ca(2+) pulses can often be masked. In an effort to evaluate whether the cytosolic Ca(2+) pulses previously reported in populations of elicitor- and stress-stimulated tobacco cells accurately represent the pulses that occur in individual cells, a study of single cell Ca(2+) fluxes in stress-stimulated tobacco cells was undertaken. Individual aequorin-transformed cells were isolated from a tobacco suspension culture and placed directly on a sensitive photo-multiplier tube mounted in a dark chamber. Ca(2+)-dependent luminescence was then monitored after stimulation with hypo- or hyper-osmotic shock, cold shock, or defense elicitors (oligogalacturonic acid and harpin). Hypo-osmotic shock induced a biphasic Ca(2+) transient in 67% of the single cells tested that exhibited similar kinetics to the biphasic pulses measured repeatedly in 1ml cell suspensions. In contrast, 33% of the stimulated cells displayed Ca(2+) flux patterns that were not previously seen in cell suspension studies. Additionally, because only 29% of the cells tested responded with measurable Ca(2+) pulses to oligogalacturonic acid and 33% to the harpin protein, we conclude that not all cells in a suspension are simultaneously sensitive to stimulation with defense elicitors. In contrast, all cells tested responded with an immediate Ca(2+) influx after cold or hyperosmotic shock. We conclude that in many cases the Ca(2+) signaling patterns of single cells are accurately represented in the signaling patterns of large populations, but that single cell measurements are still required to characterize the Ca(2+) fluxes of the less prominent cell populations.
2. Protein engineering of a human enzyme that hydrolyzes V and G nerve agents: design, construction and characterization
C A Broomfield, O Lockridge, C B Millard Chem Biol Interact. 1999 May 14;119-120:413-8. doi: 10.1016/s0009-2797(99)00053-8.
Because of deficiencies in the present treatments for organophosphorus anticholinesterase poisoning, we are attempting to develop a catalytic scavenger that can be administered as prophylactic protection. Currently known enzymes are inadequate for this purpose because they have weak binding and slow turnover, so we are trying to make an appropriate enzyme by protein engineering techniques. One butyrylcholinesterase mutant, G117H, has the desired type of activity but reacts much too slowly. This communication describes an attempt to determine the reason for the slow reaction so that a more efficient enzyme might be designed. The results indicate that the mutation at residue 117 has resulted in a distortion of the transition state of the reaction of organophosphorus compounds with the active site serine. This information will be used to develop other mutants that avoid transition state stabilization sites.
3. Interaction of beta-lactamase of Streptomyces cacaoi. II. CP-45,899, izumenolide and cephamycins
A Mantoku, H Ogawara J Antibiot (Tokyo). 1981 Oct;34(10):1347-50. doi: 10.7164/antibiotics.34.1347.
Inhibition of a beta-lactamase of Streptomyces cacaoi by CP-45,899, izumenolide and cephamycins was investigated and compared with that of a beta-lactamase of Bacillus cereus. S. cacaoi enzyme could not hydrolyze CP-45,899. Instead, hydrolysis of benzylpenicillin by the enzyme was inhibited in the presence of CP-45,899. Although inhibition increased gradually with time, the inhibition line produced by CP-45,899 with time less curved than that produced by clavulanic acid and PS-5. Furthermore, preincubation of S. cacaoi beta-lactamase with CP-45,899 for up to 120 seconds did not obviously affect the degree of inhibition. When the concentration was lowered, it behaved as a competitive inhibitor, a Ki value being 6.2 X 10(-7) M. Izumenolide, on the other hand, did not inhibit the enzyme activity of S. cacaoi beta-lactamase at 1.28 X 10(-4) M, although it inhibited B. cereus enzyme slightly in a competitive manner. Oganomycins were inert to the both beta-lactamases.U
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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 ╳
