Bottromycin
* Please be kindly noted products are not for therapeutic use. We do not sell to patients.
| Category | Antibiotics |
| Catalog number | BBF-00165 |
| CAS | 15005-62-6 |
| Molecular Weight | 823.05 |
| Molecular Formula | C42H62N8O7S |
Online Inquiry
Description
Bottromycin is a peptide antibiotic produced by Streptomyces bottropensis. It has anti-gram-positive bacteria, mycobacteria, gram-negative bacteria (individually) and mycoplasma activity.
Specification
| Synonyms | Bottromycin A2 |
| IUPAC Name | methyl 3-[[2-[[2-[(6-tert-butyl-13-methyl-2,8,11-trioxo-9-propan-2-yl-1,4,7,10-tetrazabicyclo[10.3.0]pentadec-4-en-5-yl)amino]-3,3-dimethylbutanoyl]amino]-3-phenylbutanoyl]amino]-3-(1,3-thiazol-2-yl)propanoate |
| Canonical SMILES | CC1CCN2C1C(=O)NC(C(=O)NC(C(=NCC2=O)NC(C(=O)NC(C(C)C3=CC=CC=C3)C(=O)NC(CC(=O)OC)C4=NC=CS4)C(C)(C)C)C(C)(C)C)C(C)C |
| InChI | InChI=1S/C42H62N8O7S/c1-23(2)30-36(53)49-33(41(5,6)7)35(44-22-28(51)50-19-17-24(3)32(50)38(55)46-30)48-34(42(8,9)10)39(56)47-31(25(4)26-15-13-12-14-16-26)37(54)45-27(21-29(52)57-11)40-43-18-20-58-40/h12-16,18,20,23-25,27,30-34H,17,19,21-22H2,1-11H3,(H,44,48)(H,45,54)(H,46,55)(H,47,56)(H,49,53) |
| InChI Key | KSIZLOPUXFSFNR-UHFFFAOYSA-N |
Properties
| Antibiotic Activity Spectrum | Gram-positive bacteria; Gram-negative bacteria; mycobacteria; mycoplasma |
| Boiling Point | 1061.3°C at 760 mmHg |
| Melting Point | 146°C |
| Density | 1.28 g/cm3 |
Reference Reading
1. Author Correction: The bottromycin epimerase BotH defines a group of atypical α/β-hydrolase-fold enzymes
Asfandyar Sikandar, Laura Franz, Sebastian Adam, Javier Santos-Aberturas, Liliya Horbal, Andriy Luzhetskyy, Andrew W Truman, Olga V Kalinina, Jesko Koehnke Nat Chem Biol. 2020 Sep;16(9):1034. doi: 10.1038/s41589-020-0624-8.
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
2. The bottromycin epimerase BotH defines a group of atypical α/β-hydrolase-fold enzymes
Asfandyar Sikandar, Laura Franz, Sebastian Adam, Javier Santos-Aberturas, Liliya Horbal, Andriy Luzhetskyy, Andrew W Truman, Olga V Kalinina, Jesko Koehnke Nat Chem Biol. 2020 Sep;16(9):1013-1018. doi: 10.1038/s41589-020-0569-y. Epub 2020 Jun 29.
D-amino acids endow peptides with diverse, desirable properties, but the post-translational and site-specific epimerization of L-amino acids into their D-counterparts is rare and chemically challenging. Bottromycins are ribosomally synthesized and post-translationally modified peptides that have overcome this challenge and feature a D-aspartate (D-Asp), which was proposed to arise spontaneously during biosynthesis. We have identified the highly unusual α/β-hydrolase (ABH) fold enzyme BotH as a peptide epimerase responsible for the post-translational epimerization of L-Asp to D-Asp during bottromycin biosynthesis. The biochemical characterization of BotH combined with the structures of BotH and the BotH-substrate complex allowed us to propose a mechanism for this reaction. Bioinformatic analyses of BotH homologs show that similar ABH enzymes are found in diverse biosynthetic gene clusters. This places BotH as the founding member of a group of atypical ABH enzymes that may be able to epimerize non-Asp stereocenters across different families of secondary metabolites.
3. Regulation of Bottromycin Biosynthesis Involves an Internal Transcriptional Start Site and a Cluster-Situated Modulator
Natalia M Vior, Eva Cea-Torrescassana, Tom H Eyles, Govind Chandra, Andrew W Truman Front Microbiol. 2020 Mar 26;11:495. doi: 10.3389/fmicb.2020.00495. eCollection 2020.
Bottromycin is a ribosomally synthesized and post-translationally modified peptide (RiPP) produced by several streptomycetes, including the plant pathogen Streptomyces scabies. There is significant interest in this molecule as it possesses strong antibacterial activity against clinically relevant multidrug resistant pathogens and is structurally distinct from all other antibiotics. However, studies into its efficacy are hampered by poor yields. An understanding of how bottromycin biosynthesis is regulated could aid the development of strategies to increase titres. Here, we use 5'-tag-RNA-seq to identify the transcriptional organization of the gene cluster, which includes an internal transcriptional start site that precedes btmD, the gene that encodes the bottromycin precursor peptide. We show that the gene cluster does not encode a master regulator that controls pathway expression and instead encodes a regulatory gene, btmL, which functions as a modulator that specifically affects the expression of btmD but not genes up- or downstream of btmD. In order to identify non-cluster associated proteins involved in regulation, proteins were identified that bind to the main promoter of the pathway, which precedes btmC. This study provides insights into how this deceptively complex pathway is regulated in the absence of a pathway specific master regulator, and how it might coordinate with the central metabolism of the cell.
Recommended Products
| BBF-03754 | CASTANOSPERMINE | Inquiry |
| BBF-03753 | Baicalin | Inquiry |
| BBF-01825 | Loganin | Inquiry |
| BBF-00677 | 3-Amino-3-deoxy-D-glucose | Inquiry |
| BBF-01829 | Deoxynojirimycin | Inquiry |
| BBF-02614 | Nystatin | 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 ╳
