Epithienamycin B
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| Category | Antibiotics |
| Catalog number | BBF-03187 |
| CAS | |
| Molecular Weight | 312.34 |
| Molecular Formula | C13H16N2O5S |
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Description
Epithienamycin B is a carbapenem antibiotic produced by Streptomyces flavogriseus MA-4434 and MB-4638. It has anti-gram-positive bacteria and anti-gram-negative bacteria activity.
Specification
| IUPAC Name | (5R,6R)-3-[(E)-2-acetamidoethenyl]sulfanyl-6-[(1S)-1-hydroxyethyl]-7-oxo-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid |
| Canonical SMILES | CC(C1C2CC(=C(N2C1=O)C(=O)O)SC=CNC(=O)C)O |
| InChI | InChI=1S/C13H16N2O5S/c1-6(16)10-8-5-9(21-4-3-14-7(2)17)11(13(19)20)15(8)12(10)18/h3-4,6,8,10,16H,5H2,1-2H3,(H,14,17)(H,19,20)/b4-3+/t6-,8+,10-/m0/s1 |
| InChI Key | PRPNUZWHFGSGRV-NJFHWYBASA-N |
Properties
| Antibiotic Activity Spectrum | Gram-positive bacteria; Gram-negative bacteria |
| Boiling Point | 604.4±55.0°C at 760 mmHg |
| Density | 1.5±0.1 g/cm3 |
Reference Reading
1. Methylations in complex carbapenem biosynthesis are catalyzed by a single cobalamin-dependent radical S-adenosylmethionine enzyme
Erica K Sinner, Michael S Lichstrahl, Rongfeng Li, Daniel R Marous, Craig A Townsend Chem Commun (Camb). 2019 Dec 10;55(99):14934-14937. doi: 10.1039/c9cc07197k.
Complex carbapenem β-lactam antibiotics contain diverse C6 alkyl substituents constructed by cobalamin-dependent radical SAM enzymes. TokK installs the C6 isopropyl chain found in asparenomycin. Time-course analyses of TokK and its ortholog ThnK, which forms the C6 ethyl chain of thienamycin, indicate that catalysis occurs through a sequence of discrete, non-processive methyl transfers.
2. Structural characterization of cobalamin-dependent radical S-adenosylmethionine methylases
Hayley L Knox, Squire J Booker Methods Enzymol. 2022;669:3-27. doi: 10.1016/bs.mie.2021.12.013. Epub 2022 Jan 28.
Cobalamin-dependent radical S-adenosylmethionine (SAM) methylases catalyze key steps in the biosynthesis of numerous biomolecules, including protein cofactors, antibiotics, herbicides, and other natural products, but have remained a relatively understudied subclass of radical SAM enzymes due to their inherent insolubility upon overproduction in Escherichia coli. These enzymes contain two cofactors: a [4Fe-4S] cluster that is ligated by three cysteine residues, and a cobalamin cofactor typically bound by residues in the N-terminal portion of the enzyme. Recent advances in the expression and purification of these enzymes in their active states and with both cofactors present has allowed for more detailed biochemical studies as well as structure determination by X-ray crystallography. Herein, we use KsTsrM and TokK to highlight methods for the structural characterization of cobalamin-dependent radical SAM (RS) enzymes and describe recent advances in in the overproduction and purification of these enzymes.
3. Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea
Seydina M Diene, Lucile Pinault, Nicholas Armstrong, Said Azza, Vivek Keshri, Saber Khelaifia, Eric Chabrière, Gustavo Caetano-Anolles, Jean-Marc Rolain, Pierre Pontarotti, Didier Raoult Life (Basel). 2020 Nov 14;10(11):280. doi: 10.3390/life10110280.
β-lactam antibiotics have a well-known activity which disturbs the bacterial cell wall biosynthesis and may be cleaved by β-lactamases. However, these drugs are not active on archaea microorganisms, which are naturally resistant because of the lack of β-lactam target in their cell wall. Here, we describe that annotation of genes as β-lactamases in Archaea on the basis of homologous genes is a remnant of identification of the original activities of this group of enzymes, which in fact have multiple functions, including nuclease, ribonuclease, β-lactamase, or glyoxalase, which may specialized over time. We expressed class B β-lactamase enzyme from Methanosarcina barkeri that digest penicillin G. Moreover, while weak glyoxalase activity was detected, a significant ribonuclease activity on bacterial and synthetic RNAs was demonstrated. The β-lactamase activity was inhibited by β-lactamase inhibitor (sulbactam), but its RNAse activity was not. This gene appears to have been transferred to the Flavobacteriaceae group especially the Elizabethkingia genus, in which the expressed gene shows a more specialized activity on thienamycin, but no glyoxalase activity. The expressed class C-like β-lactamase gene, from Methanosarcina sp., also shows hydrolysis activity on nitrocefin and is more closely related to DD-peptidase enzymes. Our findings highlight the need to redefine the nomenclature of β-lactamase enzymes and the specification of multipotent enzymes in different ways in Archaea and bacteria over time.
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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 ╳
