Amiclenomycin
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| Category | Antibiotics |
| Catalog number | BBF-00436 |
| CAS | 53696-70-1 |
| Molecular Weight | 196.25 |
| Molecular Formula | C10H16N2O2 |
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Description
It is produced by the strain of Streptomyces lavendulae subsp. amiclenomycini. It can inhibit the activity of Mycobacterium, and also has effect on kanamycin resistant Mycobacterium nucleum. Biotin and Desthiobiocin can offset their activities.
Specification
| Synonyms | Amyclenomycin; 2-Amino-4-(4-amino-2,5-cyclohexadienyl)butyric acid |
| IUPAC Name | 2-amino-4-(4-aminocyclohexa-2,5-dien-1-yl)butanoic acid |
| Canonical SMILES | C1=CC(C=CC1CCC(C(=O)O)N)N |
| InChI | InChI=1S/C10H16N2O2/c11-8-4-1-7(2-5-8)3-6-9(12)10(13)14/h1-2,4-5,7-9H,3,6,11-12H2,(H,13,14) |
| InChI Key | LAJWZJCOWPUSOA-UHFFFAOYSA-N |
Properties
| Appearance | Pale Yellow and white Powder |
| Antibiotic Activity Spectrum | mycobacteria |
| Boiling Point | 364.3 °C at 760 mmHg |
| Melting Point | 215-216 °C (dec.) |
| Density | 1.155 g/cm3 |
| Solubility | Soluble in Water |
Reference Reading
1. Inhibition of 7,8-diaminopelargonic acid aminotransferase by amiclenomycin and analogues
S Mann, A Marquet, O Ploux Biochem Soc Trans. 2005 Aug;33(Pt 4):802-5. doi: 10.1042/BST0330802.
Cis and trans stereoisomers of amiclenomycin, a natural L-amino acid antibiotic, have been prepared using unequivocal routes. By using 1H NMR spectroscopy, the configuration of the six-membered ring of natural amiclenomycin was shown to be cis and not trans as originally proposed. Amiclenomycin and some synthetic analogues with the cis configuration irreversibly inactivate DAPA AT (7,8-diaminopelargonic acid aminotransferase), an enzyme involved in biotin biosynthesis, by forming an aromatic PLP (pyridoxal-5'-phosphate)-inhibitor adduct that is tightly bound to the active site. The following kinetic parameters for the inactivation of Escherichia coli DAPA AT by amiclenomycin were derived: K(I)=2 microM and k(inact)=0.4 min(-1). The structure of the aromatic adduct formed upon inactivation was confirmed by UV-visible spectroscopy, X-ray crystal structure determination and MS. Because Mycobacterium tuberculosis DAPA AT is a potential drug target, this enzyme was cloned, overexpressed and purified to homogeneity for biochemical characterization.
2. Pyridoxal-5'-phosphate-dependent enzymes involved in biotin biosynthesis: structure, reaction mechanism and inhibition
Stéphane Mann, Olivier Ploux Biochim Biophys Acta. 2011 Nov;1814(11):1459-66. doi: 10.1016/j.bbapap.2010.12.004. Epub 2010 Dec 21.
The four last steps of biotin biosynthesis, starting from pimeloyl-CoA, are conserved among all the biotin-producing microorganisms. Two enzymes of this pathway, the 8-amino-7-oxononanoate synthase (AONS) and the 7,8-diaminopelargonic acid aminotransferase (DAPA AT) are dependent on pyridoxal-5'-phosphate (PLP). This review summarizes our current understanding of the structure, reaction mechanism and inhibition on these two interesting enzymes. Mechanistic studies as well as the determination of the crystal structure of AONS have revealed a complex mechanism involving an acylation with inversion of configuration and a decarboxylation with retention of configuration. This reaction mechanism is shared by the homologous 5-aminolevulinate synthase and serine palmitoyltransferase. While the reaction catalyzed by DAPA AT is a classical PLP-dependent transamination, the inactivation of this enzyme by amiclenomycin, a natural antibiotic that is active against Mycobacterium tuberculosis, involves the irreversible formation of an adduct between PLP and amiclenomycin. Mechanistic and structural studies allowed the complete description of this unique inactivation mechanism. Several potent inhibitors of these two PLP-dependent enzymes have been prepared and might be useful as starting points for the design of herbicides or antibiotics. This article is part of a Special Issue entitled: Pyridoxal Phospate Enzymology.
3. Discovery of the Biosynthetic Machinery for Stravidins, Biotin Antimetabolites
Rana Montaser, Neil L Kelleher ACS Chem Biol. 2020 May 15;15(5):1134-1140. doi: 10.1021/acschembio.9b00890. Epub 2020 Jan 9.
Stravidins are peptide antibiotics produced by Streptomyces spp. Their antibacterial activity derives from an unusual amiclenomycin monomer, the warhead that inhibits biotin biosynthesis. Despite being discovered over five decades ago, stravidin biosynthesis has remained a mystery. Using our "metabologenomics" platform, we discover new stravidin analogues and identify the novel biosynthetic machinery responsible for their production. Analysis of the newly identified biosynthetic gene cluster (BGC) indicates the unusual amiclenomycin warhead is derived from chorismic acid, with initial steps similar to those involved in p-amino phenylalanine biosynthesis. However, a distinctive decarboxylation retains the nonaromatic character of a key ring and precedes a one-carbon extension to afford the warhead in its bioactive, untriggered state. Strikingly, we also identified two streptavidin genes flanking the new stravidin BGC reported here. This aligns with the known synergistic activity between the biotin-binding activity of streptavidin and the stravidins to antagonize both biotin biogenesis and bacterial growth.
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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 ╳
