New Type II Manumycins Produced by Streptomyces nodosus ssp. asukaensis and Their Biosynthesis.
Open accessAbstract
Five new type II manumycins, containing the hydroxyquinol mC7N unit, asukamycins A-II, B-II, C-II, D-II, E-II, were discovered in cultures of Streptomyces nodosus ssp. asukaensis. The biosynthetic origin of the type II manumycins from the type I compounds, containing an epoxyquinol mC7N unit, was deduced from the time course of production and proven by preparing [7'-13C]asukamycin A and demonstrating its incorporation into asukamycin A-II.
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Manumycin polyketides possess a suite of electrophilic sites that could potentially react covalently with nucleophilic amino acids within proteins, such as cysteines.
“These molecules possess a suite of electrophilic sites that could potentially react covalently with nucleophilic amino acids within proteins, such as cysteines (Figure 1a) 19.”
From Manumycin polyketides act as molecular glues between UBR7 and P53 (2020) · cites this paper as [19]
Manumycin A has been shown to inhibit farnesyl transferase activity and sphingomyelinase activity.
“Manumycin A has also been show to inhibit farnesyl transferase activity and sphingomyelinase activity, but asukamycin is not known to inhibit these targets and its anti-cancer mechanism of action is unclear 19–23.”
From Manumycin polyketides act as molecular glues between UBR7 and P53 (2020) · cites this paper as [19]
Asukamycin is not known to inhibit farnesyl transferase or sphingomyelinase and its anti-cancer mechanism of action is unclear.
“Manumycin A has also been show to inhibit farnesyl transferase activity and sphingomyelinase activity, but asukamycin is not known to inhibit these targets and its anti-cancer mechanism of action is unclear 19–23.”
From Manumycin polyketides act as molecular glues between UBR7 and P53 (2020) · cites this paper as [19]
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Manumycin polyketides act as molecular glues between UBR7 and P53
Isobe, Y., Okumura, M., McGregor, L. M., Brittain, S. M., Jones, M. D., Liang, X., White, R., Forrester, W., McKenna, J. M., Tallarico, J. A., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0557-2 · Cited by 124 · see citing works
- Authors
- HU, Y., & FLOSS, H. G.
- Affiliations
- University of Washington (US)
- ORCID
- HU, YIDING
- Venue
- The Journal of Antibiotics
- Published
- 2001
- Volume
- 54
- Issue
- 4
- Pages
- 340-348
- ISSN
- 0021-8820 (ISSN-L)
- 1881-1469
- OpenAlex
- W1989239108
- Cited by
- 12
- References
- 18
- Citations by year
- 2020: 1 · 2019: 1 · 2015: 2 · 2012: 1
- FWCI
- 0.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Antibiotics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (AI-20264, R01AI020264)
- Topics
- Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Microbial Metabolism and Applications
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- biosynthetic origin, 13C labeling, natural product biosynthesis
- MeSH terms
- Anti-Bacterial Agents, Chromatography, High Pressure Liquid, Chromatography, Thin Layer, Fermentation, Magnetic Resonance Spectroscopy, Polyenes, Mass Spectrometry, Streptomyces, Polyunsaturated Alkamides
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