Coumermycin A1
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| Category | Antibiotics |
| Catalog number | BBF-01744 |
| CAS | 4434-05-3 |
| Molecular Weight | 1110.09 |
| Molecular Formula | C55H59N5O20 |
| Purity | >98% |
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Description
Coumemycin A1 is found to bind at a second ATP-binding site in the C-terminal domain of Hsp90, IC50 70 μmol/L. It is produced by the strain of Streptomyces rishirensis, Str. spinichromogene and Str. Spinicoumarensis. It has anti-gram positive bacteria, negative bacteria, mycobacterium (weak) activity, cross-resistance with Novobiocin.
Specification
| Synonyms | coumermycin a1; Coumamycine; Coumamycinum; Cumamicina; Notomycin; Coumamycin; Notomycin A1; Sugordomycin D-1a; Sugordomycin; Antibiotic Bu-620 |
| Storage | -20 °C |
| IUPAC Name | [(3R,4S,5R,6R)-5-hydroxy-6-[4-hydroxy-3-[[5-[[4-hydroxy-7-[(2R,3R,4S,5R)-3-hydroxy-5-methoxy-6,6-dimethyl-4-(5-methyl-1H-pyrrole-2-carbonyl)oxyoxan-2-yl]oxy-8-methyl-2-oxochromen-3-yl]carbamoyl]-4-methyl-1H-pyrrole-3-carbonyl]amino]-8-methyl-2-oxochromen-7-yl]oxy-3-methoxy-2,2-dimethyloxan-4-yl] 5-methyl-1H-pyrrole-2-carboxylate |
| Canonical SMILES | CC1=CC=C(N1)C(=O)O[C@H]2[C@H](C(OC([C@@H]2OC)(C)C)OC3=C(C4=C(C=C3)C(=O)C(=C(O4)O)NC(=O)C5=CNC(=C5C)C(=O)NC6=C(OC7=C(C6=O)C=CC(=C7C)OC8[C@@H]([C@@H]([C@H](C(O8)(C)C)OC)OC(=O)C9=CC=C(N9)C)O)O)C)O |
| InChI | InChI=1S/C55H59N5O20/c1-21-12-16-29(57-21)48(67)77-42-38(63)52(79-54(6,7)44(42)71-10)73-31-18-14-26-36(61)34(50(69)75-40(26)24(31)4)59-46(65)28-20-56-33(23(28)3)47(66)60-35-37(62)27-15-19-32(25(5)41(27)76-51(35)70)74-53-39(64)43(45(72-11)55(8,9)80-53)78-49(68)30-17-13-22(2)58-30/h12-20,38-39,42-45,52-53,56-58,61-64H,1-11H3,(H,59,65)(H,60,66)/t38-,39-,42+,43+,44-,45-,52-,53-/m1/s1 |
| InChI Key | WTIJXIZOODAMJT-DHFGXMAYSA-N |
Properties
| Appearance | Solid powder |
| Application | Topoisomerase II Inhibitors |
| Antibiotic Activity Spectrum | Gram-positive bacteria; Gram-negative bacteria; Mycobacteria |
| Boiling Point | 821.5 °C (Predicted) |
| Melting Point | 240-245 °C |
| Density | 1.1866 g/cm3 (Predicted) |
| Solubility | Soluble in DMSO (50 mg/mL) |
Reference Reading
1.The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs.
Ali JA;Jackson AP;Howells AJ;Maxwell A Biochemistry. 1993 Mar 16;32(10):2717-24.
We have cloned and overexpressed a gene encoding a 43-kDa protein corresponding to the N-terminal fragment of the DNA gyrase B subunit. We show that this protein hydrolyzes ATP and binds coumarin drugs. The hydrolysis of ATP shows distinctly non-Michaelis-Menten kinetics and is consistent with a scheme in which the active form of the protein is a dimer, a conclusion supported by molecular weight studies. The coumarin drugs bind very tightly to the 43-kDa fragment, with novobiocin binding to the protein monomer and coumermycin A1 apparently inducing the formation of a dimer. The implications of these results with respect to the mechanism of supercoiling by DNA gyrase and the inhibition of gyrase by coumarin drugs are discussed.
2.The effects of inhibitors of topoisomerase II and quinacrine on ultraviolet-light-induced DNA incision in normal and xeroderma pigmentosum fibroblasts.
Thielmann HW;Popanda O;Edler L J Cancer Res Clin Oncol. 1991;117(1):19-26.
The aim of our work was to investigate whether DNA topoisomerase II participates in the repair-specific incision of UV-irradiated genomic DNA. Therefore, the influence upon DNA incision of the topoisomerase II inhibitors (nalidixic and oxolinic acid, novobiocin and coumermycin A1) as well as the intercalating agent quinacrine has been measured in normal human fibroblasts using the alkaline elution technique. In addition, inhibition by novobiocin has been determined in fibroblast strains from 11 normal donors and from 16 xeroderma pigmentosum (XP) patients belonging to the complementation groups A, C, D, E, and XP variant. Nalidixic and oxolonic acid did not inhibit endonucleolytic cleavage, whereas novobiocin was a potent inhibitor of DNA incision. It was observed that in normal and in all XP strains 50% inhibition by novobiocin occurred on average in the dose range 315-590 microM. Since inhibition by novobiocin was not paralleled by that with the other topoisomerase II inhibitors nalidixic and oxolinic acid, it must be concluded that reduction of enzyme-catalysed breaks was not due to the participation of topoisomerase II in the incision step, but to the displacement of ATP at the binding site of the DNA-incising enzyme.
3.Coumarin formation in novobiocin biosynthesis: beta-hydroxylation of the aminoacyl enzyme tyrosyl-S-NovH by a cytochrome P450 NovI.
Chen H;Walsh CT Chem Biol. 2001 Apr;8(4):301-12.
BACKGROUND: ;Coumarin group antibiotics, such as novobiocin, coumermycin A1 and clorobiocin, are potent inhibitors of DNA gyrase. These antibiotics have been isolated from various Streptomyces species and all possess a 3-amino-4-hydroxy-coumarin moiety as their structural core. Prior labeling experiments on novobiocin established that the coumarin moiety was derived from L-tyrosine, probably via a beta-hydroxy-tyrosine (beta-OH-Tyr) intermediate. Recently the novobiocin gene cluster from Streptomyces spheroides was cloned and sequenced and allows analysis of the biosynthesis of the coumarin at the biochemical level using overexpressed and purified proteins.;RESULTS: ;Two open reading frames (ORFs), NovH and NovI, from the novobiocin producer S. spheroides have been overexpressed in Escherichia coli, purified and characterized for tyrosine activation and oxygenation which are the initial steps in coumarin formation. The 65 kDa NovH has two predicted domains, an adenylation (A) and a peptidyl carrier protein (PCP), reminiscent of non-ribosomal peptide synthetases. Purified NovH catalyzes L-tyrosyl-AMP formation by its A domain, can be posttranslationally phosphopantetheinylated on the PCP domain, and accumulates the covalent L-tyrosyl-S-enzyme intermediate on the holo PCP domain.
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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 ╳
