Alazopeptin
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| Category | Enzyme inhibitors |
| Catalog number | BBF-00401 |
| CAS | 1397-84-8 |
| Molecular Weight | 364.36 |
| Molecular Formula | C15H20N6O5 |
| Purity | 99% |
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Description
It is produced by the strain of Streptomyces griseoplanus. Corneas and Salmonella gallinarum were inhibited, and sarcoma cell 180 was moderately inhibited.
Specification
| Synonyms | L-Allyl-(6-diazo-5-oxo)-L-norleucyl-(6-diazo-5-oxo)-L-norleucine; Allyl-(6-diazo-5-oxo)-norleucyl-(6-diazo-5-oxo)-norleucine; Allyl-(6-diazo-5-oxo)-L-norleucyl-(6-diazo-5-oxo)-L-norleucine; (Z)-6-[[(Z)-1-carboxy-5-diazonio-4-oxidopent-4-enyl]amino]-1-diazonio-6-oxo-5-(prop-2-enylamino)hex-1-en-2-olate; Ambomycin; Alazopeptin(6CI,7CI,8CI); Norleucine, 6-diazo-5-oxo-N-2-propenylnorleucyl-6-diazo-5-oxo-(9CI) |
| Storage | 2-8 °C |
| IUPAC Name | (2S)-6-diazo-2-[[(2S)-6-diazo-5-oxo-2-(prop-2-enylamino)hexanoyl]amino]-5-oxohexanoic acid |
| Canonical SMILES | C=CCNC(CCC(=O)C=[N+]=[N-])C(=O)NC(CCC(=O)C=[N+]=[N-])C(=O)O |
| InChI | InChI=1S/C15H20N6O5/c1-2-7-18-12(5-3-10(22)8-19-16)14(24)21-13(15(25)26)6-4-11(23)9-20-17/h2,8-9,12-13,18H,1,3-7H2,(H,21,24)(H,25,26)/t12-,13-/m0/s1 |
| InChI Key | LYUGICBKRYXVHJ-STQMWFEESA-N |
Properties
| Appearance | Crystal |
| Solubility | Soluble in Water |
Reference Reading
1. The α/β Hydrolase AzpM Catalyzes Dipeptide Synthesis in Alazopeptin Biosynthesis Using Two Molecules of Carrier Protein-Tethered Amino Acid
Seiji Kawai, Yohei Katsuyama, Yasuo Ohnishi Chembiochem. 2022 Apr 5;23(7):e202100700. doi: 10.1002/cbic.202100700. Epub 2022 Feb 21.
During the biosynthesis of alazopeptin, a tripeptide composed of two molecules of 6-diazo-5-oxo-L-norleucine (DON) and one of alanine, the α/β hydrolase AzpM synthesizes the DON-DON dipeptide using DON tethered to the carrier protein AzpF (DON-AzpF). However, whether AzpM catalyzes the condensation of DON-AzpF with DON or DON-AzpF remains unclear. Here, to distinguish between these two condensation possibilities, the reaction catalyzed by AzpM was examined in vitro using a DON analogue, azaserine (AZS). We found that AzpM catalyzed the condensation between AZS-AzpF and DON-AzpF, but not between AZS-AzpF and DON. Possible reaction intermediates, DON-DON-AzpF and AZS-AZS-AzpF, were also detected during AzpM-catalyzed dipeptide formation from DON-AzpF and AZS-AzpF, respectively. From these results, we concluded that AzpM catalyzed the condensation of the two molecules of DON-AzpF and subsequent hydrolysis to produce DON-DON. Thus, AzpM is an unprecedented α/β hydrolase that catalyzes dipeptide synthesis from two molecules of a carrier protein-tethered amino acid.
2. Complete Biosynthetic Pathway of Alazopeptin, a Tripeptide Consisting of Two Molecules of 6-Diazo-5-oxo-l-norleucine and One Molecule of Alanine
Seiji Kawai, Yuko Sugaya, Ryota Hagihara, Hiroya Tomita, Yohei Katsuyama, Yasuo Ohnishi Angew Chem Int Ed Engl. 2021 Apr 26;60(18):10319-10325. doi: 10.1002/anie.202100462. Epub 2021 Mar 24.
DON (6-diazo-5-oxo-l-norleucine), a diazo-containing amino acid, has been studied for more than 60 years as a potent antitumor agent, but its biosynthesis has not been elucidated. Here we reveal the complete biosynthetic pathway of alazopeptin, the tripeptide Ala-DON-DON, which has antitumor activity, by gene inactivation and in vitro analysis of recombinant enzymes. We also established heterologous production of N-acetyl-DON in Streptomyces albus. DON is synthesized from lysine by three enzymes and converted to alazopeptin by five enzymes and one carrier protein. Most interestingly, transmembrane protein AzpL was indicated to catalyze diazotization using 5-oxolysine and nitrous acid as substrates. Site-directed mutagenesis of AzpL indicated that the hydroxy group of Tyr-93 is important for the diazotization. These findings expand our knowledge of the enzymology of N-N bond formation.
3. In vitro and in vivo antitrypanosomal activitiy of two microbial metabolites, KS-505a and alazopeptin
Aki Ishiyama, Kazuhiko Otoguro, Miyuki Namatame, Aki Nishihara, Toshiaki Furusawa, Rokuro Masuma, Kazuro Shiomi, Yoko Takahashi, Michio Ichimura, Haruki Yamada, Satoshi Omura J Antibiot (Tokyo). 2008 Oct;61(10):627-32. doi: 10.1038/ja.2008.83.
Our on-going screening program to discover new antitrypanosomal antibiotics has been evaluating compounds isolated from soil microorganisms as well as investigating the antibiotic libraries of the Kitasato Institute for Life Sciences and BioFrontier Laboratories of Kyowa Hakko Kogyo Co., Ltd. We have now discovered two compounds, KS-505a and alazopeptin, which exhibit moderate antitrypanosomal characteristics. We report here the in vitro and in vivo antitrypanosomal activities and cytotoxicities of KS-505a and alazopeptin, compared with some commonly-used antitrypanosomal drugs. This is the first report of in vitro and in vivo antitrypanosomal activities of either KS-505a or alazopeptin.
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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 ╳
