Glutamycin
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| Category | Antibiotics |
| Catalog number | BBF-01266 |
| CAS | 38473-18-6 |
| Molecular Weight | 237.25 |
| Molecular Formula | C12H15NO4 |
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Description
It is produced by the strain of Aspergillus flavipes F-2090/7. It is a glutarimide antibiotic. It has anti-gram-positive bacteria, negative bacteria and fungi (individual) activity.
Specification
| Related CAS | 72597-14-9 (S-isomer) |
| Synonyms | Flavipucin; (-)-Flavipucin; 1-oxa-7-azaspiro[2.5]oct-5-ene-4,8-dione, 6-methyl-2-(3-methylbutanoyl)-, (2R,3R)- |
| IUPAC Name | (2R,3R)-6-methyl-2-(3-methylbutanoyl)-1-oxa-7-azaspiro[2.5]oct-5-ene-4,8-dione |
| Canonical SMILES | CC1=CC(=O)C2(C(O2)C(=O)CC(C)C)C(=O)N1 |
| InChI | InChI=1S/C12H15NO4/c1-6(2)4-8(14)10-12(17-10)9(15)5-7(3)13-11(12)16/h5-6,10H,4H2,1-3H3,(H,13,16)/t10-,12-/m0/s1 |
| InChI Key | DWCXXICTUDDKTB-JQWIXIFHSA-N |
Properties
| Appearance | White Acicular Crystal |
| Antibiotic Activity Spectrum | Gram-positive bacteria; Gram-negative bacteria; Fungi |
| Melting Point | 130-131 °C |
| Solubility | Soluble in Ethanol |
Reference Reading
1. V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis
J Moser, W D Schubert, V Beier, I Bringemeier, D Jahn, D W Heinz EMBO J. 2001 Dec 3;20(23):6583-90. doi: 10.1093/emboj/20.23.6583.
Processes vital to life such as respiration and photosynthesis critically depend on the availability of tetrapyrroles including hemes and chlorophylls. tRNA-dependent catalysis generally is associated with protein biosynthesis. An exception is the reduction of glutamyl-tRNA to glutamate-1-semialdehyde by the enzyme glutamyl-tRNA reductase. This reaction is the indispensable initiating step of tetrapyrrole biosynthesis in plants and most prokaryotes. The crystal structure of glutamyl-tRNA reductase from the archaeon Methanopyrus kandleri in complex with the substrate-like inhibitor glutamycin at 1.9 A resolution reveals an extended yet planar V-shaped dimer. The well defined interactions of the inhibitor with the active site support a thioester-mediated reduction process. Modeling the glutamyl-tRNA onto each monomer reveals an extensive protein-tRNA interface. We furthermore propose a model whereby the large void of glutamyl-tRNA reductase is occupied by glutamate-1-semialdehyde-1,2-mutase, the subsequent enzyme of this pathway, allowing for the efficient synthesis of 5-aminolevulinic acid, the common precursor of all tetrapyrroles.
2. Mechanism of a GatCAB amidotransferase: aspartyl-tRNA synthetase increases its affinity for Asp-tRNA(Asn) and novel aminoacyl-tRNA analogues are competitive inhibitors
Jonathan L Huot, Christian Balg, Dieter Jahn, Jürgen Moser, Audrey Emond, Sébastien P Blais, Robert Chênevert, Jacques Lapointe Biochemistry. 2007 Nov 13;46(45):13190-8. doi: 10.1021/bi700602n. Epub 2007 Oct 11.
The trimeric GatCAB aminoacyl-tRNA amidotransferases catalyze the amidation of Asp-tRNAAsn and/or Glu-tRNAGln to Asn-tRNAAsn and/or Gln-tRNAGln, respectively, in bacteria and archaea lacking an asparaginyl-tRNA synthetase and/or a glutaminyl-tRNA synthetase. The two misacylated tRNA substrates of these amidotransferases are formed by the action of nondiscriminating aspartyl-tRNA synthetases and glutamyl-tRNA synthetases. We report here that the presence of a physiological concentration of a nondiscriminating aspartyl-tRNA synthetase in the transamidation assay decreases the Km of GatCAB for Asp-tRNAAsn. These conditions, which were practical for the testing of potential inhibitors of GatCAB, also allowed us to discover and characterize two novel inhibitors, aspartycin and glutamycin. These analogues of the 3'-ends of Asp-tRNA and Glu-tRNA, respectively, are competitive inhibitors of the transamidase activity of Helicobacter pylori GatCAB with respect to Asp-tRNAAsn, with Ki values of 134 microM and 105 microM, respectively. Although the 3' end of aspartycin is similar to the 3' end of Asp-tRNAAsn, this analogue was neither phosphorylated nor transamidated by GatCAB. These novel inhibitors could be used as lead compounds for designing new types of antibiotics targeting GatCABs, since the indirect pathway for Asn-tRNAAsn or Gln-tRNAGln synthesis catalyzed by these enzymes is not present in eukaryotes and is essential for the survival of the above-mentioned bacteria.
3. Methanopyrus kandleri glutamyl-tRNA reductase
J Moser, S Lorenz, C Hubschwerlen, A Rompf, D Jahn J Biol Chem. 1999 Oct 22;274(43):30679-85. doi: 10.1074/jbc.274.43.30679.
The initial reaction of tetrapyrrole formation in archaea is catalyzed by a NADPH-dependent glutamyl-tRNA reductase (GluTR). The hemA gene encoding GluTR was cloned from the extremely thermophilic archaeon Methanopyrus kandleri and overexpressed in Escherichia coli. Purified recombinant GluTR is a tetrameric enzyme with a native M(r) = 190,000 +/- 10,000. Using a newly established enzyme assay, a specific activity of 0.75 nmol h(-1) mg(-1) at 56 degrees C with E. coli glutamyl-tRNA as substrate was measured. A temperature optimum of 90 degrees C and a pH optimum of 8.1 were determined. Neither heme cofactor, nor flavin, nor metal ions were required for GluTR catalysis. Heavy metal compounds, Zn(2+), and heme inhibited the enzyme. GluTR inhibition by the newly synthesized inhibitor glutamycin, whose structure is similar to the 3' end of the glutamyl-tRNA substrate, revealed the importance of an intact chemical bond between glutamate and tRNA(Glu) for substrate recognition. The absolute requirement for NADPH in the reaction of GluTR was demonstrated using four NADPH analogues. Chemical modification and site-directed mutagenesis studies indicated that a single cysteinyl residue and a single histidinyl residue were important for catalysis. It was concluded that during GluTR catalysis the highly reactive sulfhydryl group of Cys-48 acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of an enzyme-localized thioester intermediate and the concomitant release of tRNA(Glu). In the presence of NADPH, direct hydride transfer to enzyme-bound glutamate, possibly facilitated by His-84, leads to glutamate-1-semialdehyde formation. In the absence of NADPH, a newly discovered esterase activity of GluTR hydrolyzes the highly reactive thioester of tRNA(Glu) to release glutamate.
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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 ╳
