4-Chlorothreonine
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| Category | Others |
| Catalog number | BBF-00320 |
| CAS | 142698-80-4 |
| Molecular Weight | 153.56 |
| Molecular Formula | C4H8ClNO3 |
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Description
4-Chlorothreonine is produced by the strain of Streptomyces sp. OH-5093. Its herbicidal activity is similar to that of Bialaphos.
Specification
| Synonyms | 4-chloro-L-threonine; L-Threonine, 4-chloro-; rel-(2S,3S)-2-Amino-4-chloro-3-hydroxybutanoic acid |
| IUPAC Name | (2S,3S)-2-amino-4-chloro-3-hydroxybutanoic acid |
| Canonical SMILES | C(C(C(C(=O)O)N)O)Cl |
| InChI | InChI=1S/C4H8ClNO3/c5-1-2(7)3(6)4(8)9/h2-3,7H,1,6H2,(H,8,9)/t2-,3+/m1/s1 |
| InChI Key | CETUIFTXYGHITB-GBXIJSLDSA-N |
Properties
| Appearance | White Powder |
| Boiling Point | 389.1±42.0 °C at 760 mmHg |
| Melting Point | 142-143 °C |
| Density | 1.5±0.1 g/cm3 |
Reference Reading
1. Insight into the structure-function relationship of the nonheme iron halogenases involved in the biosynthesis of 4-chlorothreonine --Thr3 from Streptomyces sp. OH-5093 and SyrB2 from Pseudomonas syringae pv. syringae B301DR
Maria Rosaria Fullone, Alessandro Paiardini, Rossella Miele, Sara Marsango, Dennis C Gross, Satoshi Omura, Enric Ros-Herrera, Maria Carmela Bonaccorsi di Patti, Aldo Laganà, Stefano Pascarella, Ingeborg Grgurina FEBS J. 2012 Dec;279(23):4269-82. doi: 10.1111/febs.12017. Epub 2012 Oct 30.
Molecular cloning of the biosynthetic gene cluster involved in the production of free 4-chlorothreonine in Streptomyces sp. OH-5093 showed the presence of six ORFs: thr1, thr2, thr3, orf1, orf2 and thr4. According to bioinformatic analysis, thr1, thr2, thr3 and thr4 encode a free-standing adenylation domain, a carrier protein, an Fe(II) nonheme α-ketoglutarate-dependent halogenase and a thioesterase, respectively, indicating the role of these genes in the activation and halogenation of threonine and the release of 4-chlorothreonine in a pathway closely reflecting the formation of this amino acid in the biosynthesis of the lipodepsipeptide syringomycin from Pseudomonas syringae pv. syringae B301DR. Orf1 and orf2 show sequence similarity with alanyl/threonyl-tRNA synthetases editing domains and drug metabolite transporters, respectively. We show that thr3 can replace the halogenase gene syrB2 in the biosynthesis of syringomycin, by functional complementation of the mutant P. s. pv. syringae strain BR135A1 inactivated in syrB2. We also provide an insight into the structure-function relationship of halogenases Thr3 and SyrB2 using homology modelling and site-directed mutagenesis.
2. A new actinomycin Z analogue with an additional oxygen bridge between chromophore and β-depsipentapeptide from Streptomyces sp. KIB-H714
Miao Dong, Pei Cao, Ya-Tuan Ma, Jianying Luo, Yijun Yan, Rong-Tao Li, Sheng-Xiong Huang Nat Prod Res. 2019 Jan;33(2):219-225. doi: 10.1080/14786419.2018.1443097. Epub 2018 Mar 2.
Actinomycin Z6 (1), a new member of the actinomycin family, along with three congeners of the Z-type (Z1, Z3, Z5) actinomycins, are produced from Streptomyces sp. KIB-H714. Their structures were authenticated by comprehensive spectroscopic data interpretation. Different from all the reported Z-type actinomycins, the β-ring of the new compound actinomycin Z6 includes an additional ring linked between the actinoyl chromophore and β-peptidolactone. In Z3 and Z5, the L-threonine in β-depsipeptide is replaced by the unusual 4-chlorothreonine, an amino acid rarely found in actinomycin family. All isolates were evaluated for cytotoxicity against five human tumor cell lines and for inhibitory activity against Candida albicans and Staphylococcus aureus.
3. Structure of the adenylation domain Thr1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces sp. OH-5093-protein flexibility and molecular bases of substrate specificity
Antonella Scaglione, Maria Rosaria Fullone, Linda Celeste Montemiglio, Giacomo Parisi, Carlotta Zamparelli, Beatrice Vallone, Carmelinda Savino, Ingeborg Grgurina FEBS J. 2017 Sep;284(18):2981-2999. doi: 10.1111/febs.14163. Epub 2017 Aug 7.
We determined the crystal structure of Thr1, the self-standing adenylation domain involved in the nonribosomal-like biosynthesis of free 4-chlorothreonine in Streptomyces sp. OH-5093. Thr1 shows two monomers in the crystallographic asymmetric unit with different relative orientations of the C- and N-terminal subdomains both in the presence of substrates and in the unliganded form. Cocrystallization with substrates, adenosine 5'-triphosphate and l-threonine, yielded one monomer containing the two substrates and the other in complex with l-threonine adenylate, locked in a postadenylation state. Steady-state kinetics showed that Thr1 activates l-Thr and its stereoisomers, as well as d-Ala, l- and d-Ser, albeit with lower efficiency. Modeling of these substrates in the active site highlighted the molecular bases of substrate discrimination. This work provides the first crystal structure of a threonine-activating adenylation enzyme, a contribution to the studies on conformational rearrangement in adenylation domains and on substrate recognition in nonribosomal biosynthesis. Database: Structural data are available in the Protein Data Bank under the accession number 5N9W and 5N9X.
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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 ╳
