Urdamycin A
(Synonyms: Antibiotic A 32Y2, Kerriamycin B, NSC 372208, NSC 606397) 目录号 : GC48226
A bacterial metabolite
Cas No.:98474-21-6
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >70.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Urdamycin A is a bacterial metabolite originally isolated from S. fradiae that has antibacterial and anticancer activities.1,2 It is active against a variety of Gram-positive and Gram-negative bacteria, including B. subtilis and strains of Arthrobacter and Streptomyces, but not the fungus S. cerevisiae, in a disc assay when used at a concentration of 1 mg/ml.2 Urdamycin A is cytotoxic to L1210 and HT-29, but not A549, cancer cells (IC50s = 7.5, 5, and >10 µg/ml, respectively).1
1.Henkel, T., Ciesiolka, T., Rohr, J., et al.Urdamycins, new angucycline antibiotics from Streptomyces fradiae. V. Derivatives of urdamycin AJ. Antibiot. (Tokyo)42(2)299-311(1989) 2.Drautz, H., ZÄhner, H., Rohr, J., et al.Metabolic products of microorganisms. 234. Urdamycins, new angucycline antibiotics from Streptomyces fradiae. I. Isolation, characterization and biological propertiesJ. Antibiot. (Tokyo)39(12)1657-1669(1986)
| Cas No. | 98474-21-6 | SDF | |
| 别名 | Antibiotic A 32Y2, Kerriamycin B, NSC 372208, NSC 606397 | ||
| Canonical SMILES | O[C@@H]1C[C@H](O[C@H]2CC[C@H](O[C@H]3[C@H](O)[C@@H](C)O[C@](C4=C(O)C(C(C(C=C[C@@](C[C@](O)(C)C5)(O)[C@]6(O[C@H]7CC[C@H](O)[C@H](C)O7)C5=O)=C6C8=O)=O)=C8C=C4)([H])C3)O[C@H]2C)O[C@H](C)[C@H]1O | ||
| 分子式 | C43H56O17 | 分子量 | 844.9 |
| 溶解度 | Dichloromethane: soluble,DMSO: soluble,Ethanol: soluble,Methanol: soluble | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 1.1836 mL | 5.9179 mL | 11.8357 mL |
| 5 mM | 0.2367 mL | 1.1836 mL | 2.3671 mL |
| 10 mM | 0.1184 mL | 0.5918 mL | 1.1836 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Cloning and characterization of a polyketide synthase gene from Streptomyces fradiae Tü2717, which carries the genes for biosynthesis of the angucycline antibiotic Urdamycin A and a gene probably involved in its oxygenation
J Bacteriol 1995 Nov;177(21):6126-36.PMID:7592377DOI:10.1128/jb.177.21.6126-6136.1995.
A DNA fragment was cloned as cosmid purd8, which encodes a polyketide synthase involved in the production of the angucycline antibiotic urdamycin from Streptomyces fradiae Tü2717. Deletion of the polyketide synthase genes from the chromosome abolished urdamycin production. In addition, purd8 conferred urdamycin resistance on introduction into Streptomyces lividans TK24. Sequence analysis of 5.7 kb of purd8 revealed six open reading frames transcribed in the same direction. The deduced amino acid sequences of the six open reading frames strongly resemble proteins from known type II polyketide synthase gene clusters: a ketoacyl synthase, a chain length factor, an acyl carrier protein, a ketoreductase, a cyclase, and an oxygenase. Heterologous expression of the urdamycin genes encoding a ketoacyl synthase and a chain length factor in Streptomyces glaucescens tetracenomycin C-nonproducing mutants impaired in either the TcmK ketoacyl synthase or TcmL chain length factor resulted in the production of tetracenomycin C. Heterologous expression of a putative oxygenase gene from the urdamycin gene cluster in S. glaucescens GLA.O caused production of the hybrid antibiotic 6-hydroxy tetracenomycin C.
Surprising production of a new urdamycin derivative by S. fradiae Delta urdQ/R
J Biotechnol 2007 May 31;130(1):32-8.PMID:17434221DOI:10.1016/j.jbiotec.2007.02.018.
A strain (S. fradiae Delta urdQ/R) with mutations in urdQ and urdR encoding a dTDP-hexose-3,4-dehydratase and a dTDP-hexose-4-ketoreductase, respectively, produces a new urdamycin analogue (urdamycin X) with changes in the polyketide structure. The structure of urdamycin X has been elucidated by NMR spectroscopy. Urdamycin X was not detectable, even in small amounts, in either S. fradiae Delta urdQ, in S. fradiae DeltaurdR or in S. fradiae A0, a mutant lacking all glycosyltransferase genes. Complementation of S. fradiae Delta urdQ/R restored Urdamycin A production indicating that the mutations did not cause any polar effect.
Function of glycosyltransferase genes involved in Urdamycin A biosynthesis
Chem Biol 2000 Feb;7(2):133-42.PMID:10662691DOI:10.1016/s1074-5521(00)00079-x.
Background: Urdamycin A, the principle product of Streptomyces fradiae Tü2717, is an angucycline-type antibiotic. The polyketide-derived aglycone moiety is glycosylated at two positions, but only limited information is available about glycosyltransferases involved in urdamycin biosynthesis. Results: To determine the function of three glycosyltransferase genes in the urdamycin biosynthetic gene cluster, we have carried out gene inactivation and expression experiments. Inactivation of urdGT1a resulted in the predominant accumulation of urdamycin B. A mutant lacking urdGT1b and urdGT1c mainly produced compound 100-2. When urdGT1c was expressed in the urdGT1b/urdGT1c double mutant, urdamycin G and Urdamycin A were detected. The mutant lacking all three genes mainly accumulated aquayamycin and urdamycinone B. Expression of urdGT1c in the triple mutant led to the formation of compound 100-1, whereas expression of urdGT1a resulted in the formation of compound 100-2. Co-expression of urdGT1b and urdGT1c resulted in the production of 12b-derhodinosyl-urdamycin A, and co-expression of urdGT1a, urdGT1b and urdGT1c resulted in the formation of Urdamycin A. Conclusions: Analysis of glycosyltransferase genes of the urdamycin biosynthetic gene cluster led to an unambiguous assignment of each glycosyltransferase to a certain biosynthetic saccharide attachment step.
Two new tailoring enzymes, a glycosyltransferase and an oxygenase, involved in biosynthesis of the angucycline antibiotic Urdamycin A in Streptomyces fradiae Tü2717
Microbiology (Reading) 2000 Jan;146 ( Pt 1):147-154.PMID:10658661DOI:10.1099/00221287-146-1-147.
Urdamycin A, the principal product of Streptomyces fradiae Tu2717, is an angucycline-type antibiotic and anticancer agent containing C-glycosidically linked D-olivose. To extend knowledge of the biosynthesis of Urdamycin A the authors have cloned further parts of the urdamycin biosynthetic gene cluster. Three new ORFs (urdK, urdJ and urdO) were identified on a 3.35 kb fragment, and seven new ORFs (urdL, urdM, urdJ2, urdZl, urdGT2, urdG and urdH) on an 8.05 kb fragment. The deduced products of these genes show similarities to transporters (urdJ and urdJ2), regulatory genes (urdK), reductases (urdO), cyclases (urdL) and deoxysugar biosynthetic genes (urdG, urdH and urdZ1). The product of urdM shows striking sequence similarity to oxygenases (N-terminal sequence) as well as reductases (C-terminal sequence), and the deduced amino acid sequence of urdGT2 resembles those of glycosyltransferases. To determine the function of urdM and urdGT2, targeted gene inactivation experiments were performed. The resulting urdM deletion mutant strains accumulated predominantly rabelomycin, indicating that UrdM is involved in oxygenation at position 12b of Urdamycin A. A mutant in which urdGT2 had been deleted produced urdamycin I, urdamycin J and urdamycin K instead of Urdamycin A. Urdamycins I, J and K are tetracyclic angucyclinones lacking a C-C connected deoxysugar moiety. Therefore UrdGT2 must catalyse the earliest glycosyltransfer step in the urdamycin biosynthetic pathway, the C-glycosyltransfer of one NDP-D-olivose.
LanV, a bifunctional enzyme: aromatase and ketoreductase during landomycin A biosynthesis
Chembiochem 2005 Dec;6(12):2312-5.PMID:16283688DOI:10.1002/cbic.200500205.
LanV is involved in the biosynthesis of landomycin A. The exact function of this enzyme was elucidated with combinatorial biosynthesis by using Streptomyces fradiae mutants that produce Urdamycin A. After expression of lanV in S. fradiae DeltaurdM, which is a mutant that accumulates rabelomycin, urdamycinon B and urdamycin B were found to be produced by the strain. This result indicates that LanV is involved in the 6-ketoreduction of the angucycline core, which preceeds a 5,6-dehydration reaction. 9-C-D-Olivosyltetrangulol was also produced by this strain; this demonstrates that LanV catalyses the aromatization of ring A of the angucycline structure. Coexpression of lanV and lanGT2 in S. fradiae AO, a mutant that lacks all four urdamycin glycosyltransferases, resulted in the production of tetrangulol and the glycoside landomycin H, both of which have an aromatic ring A. As glycosylated angucyclines were not observed after expression of lanGT2 in the absence of lanV, we conclude that LanGT2 needs an aromatized ring A for substrate recognition.