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15 results for “Marine Metabolites”
Supplementary materials for: Use and detection of a vitamin B1 degradation product yields new views of the marine B1 cycle and plankton metabolite exchange
<p>Vitamin B1 (thiamin) is a vital nutrient for most cells in nature including marine plankton. Early and recent experiments show that B1 degradation products instead of B1 can support the growth of marine bacterioplankton and phytoplankton. However, the use and occurrence of some degradation products remain uninvestigated – namely N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP) – which has been a focus of plant oxidative stress research. We investigated the relevance of FAMP in the ocean. Experiments and global ocean meta-omic data indicate that eukaryotic phytoplankton, including picoeukaryotes and harmful algal bloom species, use FAMP while bacterioplankton appear more likely to use deformylated FAMP, 4-amino-5-aminomethyl-2-methylpyrimidine (AmMP). Measurements of FAMP in seawater and biomass revealed that it occurs at picomolar concentrations in the surface ocean, heterotrophic bacterial cultures produce FAMP in the dark – indicating non-photodegradation of B1 by cells, and B1-requiring (auxotrophic) picoeukaryotic phytoplankton produce intracellular FAMP. Our results require an expansion of thinking about vitamin degradation in the sea, but also the marine B1 cycle – where it is now crucial to consider a new B1-related compound pool (FAMP) – as well as generation (dark degradation – likely via oxidation), turnover (plankton uptake), and exchange of the compound within networks of plankton.</p>
Supplementary materials for: Use and detection of a vitamin B1 degradation product yields new views of the marine B1 cycle and plankton metabolite exchange
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Fig. 8 in Cytotoxic metabolites from the marine-associated Streptomyces sp. ZZ1944
Fig. 8. Effects of autolytimycin (AL, 9) and seco-geldanamycin A (SGA, 10) on apoptosis in glioma U251 and U87MG cells. Bortezomib (BTZ) was used as a positive control. Cells were treated with AL, SGA or BTZ for 24 h, stained with annexin-V FITC and PI and then analyzed by flow cytometry.
Fig. 5 in Cytotoxic metabolites from the marine-associated Streptomyces sp. ZZ1944
Fig. 5. Key HMBC and COSY correlations of seco-geldanamycin A (10) and the structures of herbimycin I (8), autolytimycin (9), herbimycin L (10a) and 19-hydroxyherbimycin L (10b).
Fig. 7 in Cytotoxic metabolites from the marine-associated Streptomyces sp. ZZ1944
Fig. 7. Effects of autolytimycin (AL, 9) and seco-geldanamycin A (SGA, 10) on cell cycle in glioma U251 and U87MG cells. Bortezomib (BTZ) was used as a positive control. Cells were treated with AL, SGA or BTZ for 24 h and percentage of cells at each stage of the cell cycle were shown.
Fig. 3 in Cytotoxic metabolites from the marine-associated Streptomyces sp. ZZ1944
Fig. 3. Key HMBC and COSY correlations of galbonolide I (2) and the experimental ECD spectrum of galbonolide I (2) and the calculated ECD curve of model molecule 2a at the b3lyp/6–311+g (d, p) level.
Fig. 4 in Cytotoxic metabolites from the marine-associated Streptomyces sp. ZZ1944
Fig. 4. Key HMBC and COSY correlations of streptophenylpropionic acid A (3), streptophenylpropyl ester A (4) and streptophenylvaleramide A (5).
Fig. 2 in Cytotoxic metabolites from the marine-associated Streptomyces sp. ZZ1944
Fig. 2. Key HMBC and COSY correlations of galbonolide H (1) and the structure obtained from a single crystal X-ray diffraction of galbonolide H (1).
Figure 5 from: Syahputra G, Gustini N, Bustanussalam B, Hapsari Y, Sari M, Ardiansyah A, Bayu A, Putra MY (2021) Molecular docking of secondary metabolites from Indonesian marine and terrestrial organisms targeting SARS-CoV-2 ACE-2, M pro, and PL pro receptors. Pharmacia 68(3): 533-560. https://doi.org/10.3897/pharmacia.68.e68432
Figure 5 Analysis of the conformation and interaction of hydrogen bonds between ligands and receptors with a distance < 5 Å. A. ACE-2-ptilidepsin; B. PLpro -ptilidepsin; C. Mpro-ptilidepsin.
Figure 4 from: Syahputra G, Gustini N, Bustanussalam B, Hapsari Y, Sari M, Ardiansyah A, Bayu A, Putra MY (2021) Molecular docking of secondary metabolites from Indonesian marine and terrestrial organisms targeting SARS-CoV-2 ACE-2, M pro, and PL pro receptors. Pharmacia 68(3): 533-560. https://doi.org/10.3897/pharmacia.68.e68432
Figure 4 Analysis of the conformation and interaction of hydrogen bonds between ligands and receptors with a distance < 5 Å. A. ACE-2-dieckol; B. PLpro -dieckol; C. Mpro-dieckol.
Figure 2 from: Syahputra G, Gustini N, Bustanussalam B, Hapsari Y, Sari M, Ardiansyah A, Bayu A, Putra MY (2021) Molecular docking of secondary metabolites from Indonesian marine and terrestrial organisms targeting SARS-CoV-2 ACE-2, M pro, and PL pro receptors. Pharmacia 68(3): 533-560. https://doi.org/10.3897/pharmacia.68.e68432
Figure 2 The structure of the PLpro SARS-CoV-2 receptor (PDB ID: 5TL6) along with the distribution of residues on the Ramachandran plot. The PLpro receptor structure is composed of 10 α-helix structures and 19 β-sheet structures. The PLpro receptor structure is ready to use in molecular docking simulations with 96.55% of the residue in the protein-forming region.
Figure 1 from: Syahputra G, Gustini N, Bustanussalam B, Hapsari Y, Sari M, Ardiansyah A, Bayu A, Putra MY (2021) Molecular docking of secondary metabolites from Indonesian marine and terrestrial organisms targeting SARS-CoV-2 ACE-2, M pro, and PL pro receptors. Pharmacia 68(3): 533-560. https://doi.org/10.3897/pharmacia.68.e68432
Figure 1 The structure of the Mpro SARS-CoV-2 receptor (PDB ID: 6LU7) along with the distribution of residues on the Ramachandran plot. The Mpro receptor structure is composed of 10 α-helix structures and 13 β-sheet structures. The Mpro receptor structure is ready to use in molecular docking simulations with 92.15% of the residue in the protein-forming region.
Figure 3 from: Syahputra G, Gustini N, Bustanussalam B, Hapsari Y, Sari M, Ardiansyah A, Bayu A, Putra MY (2021) Molecular docking of secondary metabolites from Indonesian marine and terrestrial organisms targeting SARS-CoV-2 ACE-2, M pro, and PL pro receptors. Pharmacia 68(3): 533-560. https://doi.org/10.3897/pharmacia.68.e68432
Figure 3 Structure of the ACE 2 receptor h receptor (PDB ID: 1R42) along with the distribution of residues on the Ramachandran plot. The ACE-2 receptor structure is composed of 31 α-helix structures and six β-sheet structures. The structure of the hACE-2 receptor is ready to be used in molecular docking simulations with 98.37% of the residue in the protein-forming region.
Fig. 1 in Cytotoxic metabolites from the marine-associated Streptomyces sp. ZZ1944
Fig. 1. Structure of isolated compounds 1–20.
Fig. 6 in Cytotoxic metabolites from the marine-associated Streptomyces sp. ZZ1944
Fig. 6. Key HMBC, COSY and NOE correlations of streptorapamycin A (13).
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International Brain Laboratory public data
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OpenNeuro
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