Heliquinomycin
* Please be kindly noted products are not for therapeutic use. We do not sell to patients.
| Category | Enzyme inhibitors |
| Catalog number | BBF-01333 |
| CAS | 178182-49-5 |
| Molecular Weight | 698.58 |
| Molecular Formula | C33H30O17 |
| Purity | >95% |
Online Inquiry
Description
It is produced by the strain of Streptomyces sp. MJ929-SF2. It has anti-DNA helicase activity with Ki value of 6.8 X 10-6 mol/L. It has strong anti-gram-positive bacteria (including MR-SA) activity (MIC is 0.05-0.39 μg/mL), but has no effect on gram-negative bacteria and fungi. It has anti-tumor activity on HeLa S3, L1210, IMC, B16 and FS-3 cells with IC50 (μg/mL) of 1.6, 0.97, 1.56, 0.88 and 0.83, respectively. Its acute toxicity is low, LD50 is 100 mg/kg (mouse, enterocoelia).
Specification
| Synonyms | NSC 702208; Rubymycin |
| IUPAC Name | methyl (2R,3R,3'R)-3,4',9',10-tetrahydroxy-3'-[(2R,4S,5R,6R)-5-hydroxy-4-methoxy-6-methyloxan-2-yl]oxy-7'-methoxy-5',8',9-trioxospiro[3,4-dihydropyrano[4,3-g]chromene-2,2'-3H-benzo[f][1]benzofuran]-7-carboxylate |
| Canonical SMILES | CC1C(C(CC(O1)OC2C3=C(C4=C(C(=C3OC25C(CC6=C(O5)C(=C7C(=C6)C=C(OC7=O)C(=O)OC)O)O)O)C(=O)C(=CC4=O)OC)O)OC)O |
| InChI | InChI=1S/C33H30O17/c1-10-23(36)15(44-3)9-18(46-10)48-30-22-25(38)20-13(34)8-14(43-2)24(37)21(20)27(40)29(22)50-33(30)17(35)7-12-5-11-6-16(31(41)45-4)47-32(42)19(11)26(39)28(12)49-33/h5-6,8,10,15,17-18,23,30,35-36,38-40H,7,9H2,1-4H3/t10-,15+,17-,18-,23-,30-,33-/m1/s1 |
| InChI Key | MLFZQFHGXSVTGX-OEQCCVQYSA-N |
Properties
| Appearance | Red Powder |
| Antibiotic Activity Spectrum | Gram-positive bacteria; Neoplastics (Tumor) |
| Boiling Point | 966.0 °C at 760 mmHg |
| Melting Point | 213-214 °C |
| Density | 1.72 g/cm3 |
| Solubility | Soluble in Methanol |
Reference Reading
1. Characterization of Streptomyces piniterrae sp. nov. and Identification of the Putative Gene Cluster Encoding the Biosynthesis of Heliquinomycins
Xiaoxin Zhuang, Zhiyan Wang, Chenghui Peng, Can Su, Congting Gao, Yongjiang Wang, Shengxiong Huang, Chongxi Liu Microorganisms. 2020 Mar 31;8(4):495. doi: 10.3390/microorganisms8040495.
A novel actinomycete producing heliquinomycin and 9'-methoxy-heliquinomycin, designated strain jys28T, was isolated from rhizosphere soil of Pinus yunnanensis and characterized using a polyphasic approach. The strain had morphological characteristics and chemotaxonomic properties identical to those of members of the genus Streptomyces. It formed spiral chains of spores with spiny surfaces. The menaquinones detected were MK-9(H6), MK-9(H8) and MK-9(H4). The major fatty acids were iso-C16:0, C15:0, C16:1ω7с and anteiso-C15:0. The phospholipids were diphosphatidylglycerol, phosphatidylmethylethanolamine, phosphatidylethanolamine and phosphatidylinositol mannoside. The DNA G + C content of the draft genome sequence, consisting of 8.5 Mbp, was 70.6%. Analysis of the 16S rRNA gene sequence showed that strain jys28T belongs to the genus Streptomyces with the highest sequence similarities to Streptomyces chattanoogensis NBRC 13058T (99.2%) and Streptomyces lydicus DSM 40002T (99.2%) and phylogenetically clustered with them. Multilocus sequence analysis based on five other house-keeping genes (atpD, gyrB, rpoB, recA and trpB) and the low level of DNA-DNA relatedness and phenotypic differences allowed the novel isolate to be differentiated from its most closely related strains. Therefore, the strain is concluded to represent a novel species of the genus Streptomyces, for which the name Streptomyces piniterrae sp. nov. is proposed. Furthermore, the putative biosynthetic gene cluster of heliquinomycins was identified and the biosynthetic pathway was discussed. The type strain is jys28T (=CCTCC AA 2018051T =DSM 109823T).
2. Interaction of heliquinomycin with single-stranded DNA inhibits MCM4/6/7 helicase
Takafumi Sugiyama, Makoto Chino, Toshiki Tsurimoto, Naohito Nozaki, Yukio Ishimi J Biochem. 2012 Feb;151(2):129-37. doi: 10.1093/jb/mvr130. Epub 2011 Oct 24.
The antibiotic heliquinomycin inhibited cellular DNA replication at IC(50) of 2.5 µM without affecting level of chromatin-bound MCM4 and without activating the DNA replication stress checkpoint system, suggesting that heliquinomycin perturbs DNA replication mainly by inhibiting the activity of replicative DNA helicase that unwinds DNA duplex at replication forks. Among the DNA helicases involved in DNA replication, DNA helicase B was inhibited by heliquinomycin at IC(50) of 4.3 µM and RECQL4 helicase at IC(50) of 14 µM; these values are higher than that of MCM4/6/7 helicase (2.5 µM). These results suggest that heliquinomycin mainly targets actions of the replicative DNA helicases. Gel-retardation experiment indicates that heliquinomycin binds to single-stranded DNA. The single-stranded DNA-binding ability of MCM4/6/7 was affected in the presence of heliquinomycin. The data suggest that heliquinomycin inhibits the DNA helicase activity of MCM4/6/7 complex by stabilizing its interaction with single-stranded DNA.
3. Effect of heliquinomycin on the activity of human minichromosome maintenance 4/6/7 helicase
Yukio Ishimi, Takafumi Sugiyama, Ryou Nakaya, Makoto Kanamori, Toshiyuki Kohno, Takemi Enomoto, Makoto Chino FEBS J. 2009 Jun;276(12):3382-91. doi: 10.1111/j.1742-4658.2009.07064.x. Epub 2009 May 11.
The antibiotic heliquinomycin, which inhibits cellular DNA replication at a half-maximal inhibitory concentration (IC(50)) of 1.4-4 microM, was found to inhibit the DNA helicase activity of the human minichromosome maintenance (MCM) 4/6/7 complex at an IC(50) value of 2.4 microM. In contrast, 14 microM heliquinomycin did not inhibit significantly either the DNA helicase activity of the SV40 T antigen and Werner protein or the oligonucleotide displacement activity of human replication protein A. At IC(50) values of 25 and 6.5 microM, heliquinomycin inhibited the RNA priming and DNA polymerization activities, respectively, of human DNA polymerase-alpha/primase. Thus, of the enzymes studied, the MCM4/6/7 complex was the most sensitive to heliquinomycin; this suggests that MCM helicase is one of the main targets of heliquinomycin in vivo. It was observed that heliquinomycin did not inhibit the ATPase activity of the MCM4/6/7 complex to a great extent in the absence of single-stranded DNA. In contrast, heliquinomycin at an IC(50) value of 5.2 microM inhibited the ATPase activity of the MCM4/6/7 complex in the presence of single-stranded DNA. This suggests that heliquinomycin interferes with the interaction of the MCM4/6/7 complex with single-stranded DNA.
Recommended Products
| BBF-01826 | Deoxymannojirimycin | Inquiry |
| BBF-02642 | Lactonamycin | Inquiry |
| BBF-00677 | 3-Amino-3-deoxy-D-glucose | Inquiry |
| BBF-03754 | CASTANOSPERMINE | Inquiry |
| BBF-01825 | Loganin | Inquiry |
| BBF-03755 | Actinomycin D | 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 ╳
