1-Deoxy-D-threo-pentulose - CAS 60299-43-6
Catalog number: BBF-01830
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|Description||It is produced by the strain of Streptomyces hygroscopicus UC5601. 1-Deoxy-D-threo-pentulose has specific inhibition against Mycobacterium avium UC-159 with MIC of 1μg/mL.|
|Antibiotic Activity Spectrum||mycobacteria|
|Synonyms||1-deoxy-D-xylulose; 1-Deoxy-2-pentulose; 1-Deoxy-D-threo-2-pentulose|
|Solubility||Soluble in DMSO, Methanol|
1.Mechanistic binding insights for 1-deoxy-d-Xylulose-5-Phosphate synthase, the enzyme catalyzing the first reaction of isoprenoid biosynthesis in the malaria-causing protists, Plasmodium falciparum and Plasmodium vivax.
Battistini MR1, Shoji C1, Handa S2, Breydo L3, Merkler DJ4. Protein Expr Purif. 2016 Apr;120:16-27. doi: 10.1016/j.pep.2015.12.003. Epub 2015 Dec 15.
We have successfully truncated and recombinantly-expressed 1-deoxy-d-xylulose-5-phosphate synthase (DXS) from both Plasmodium vivax and Plasmodium falciparum. We elucidated the order of substrate binding for both of these ThDP-dependent enzymes using steady-state kinetic analyses, dead-end inhibition, and intrinsic tryptophan fluorescence titrations. Both enzymes adhere to a random sequential mechanism with respect to binding of both substrates: pyruvate and d-glyceraldehyde-3-phosphate. These findings are in contrast to other ThDP-dependent enzymes, which exhibit classical ordered and/or ping-pong kinetic mechanisms. A better understanding of the kinetic mechanism for these two Plasmodial enzymes could aid in the development of novel DXS-specific inhibitors that might prove useful in treatment of malaria.
2.Molecular cloning, functional characterization and expression of potato (Solanum tuberosum) 1-deoxy-d-xylulose 5-phosphate synthase 1 (StDXS1) in response to Phytophthora infestans.
Henriquez MA1, Soliman A2, Li G3, Hannoufa A4, Ayele BT3, Daayf F5. Plant Sci. 2016 Feb;243:71-83. doi: 10.1016/j.plantsci.2015.12.001. Epub 2015 Dec 3.
1-Deoxy-d-xylulose 5-phosphate synthase (DXS) catalyzes the initial step of the plastidial 2C-methyl-d-erythritol-4-phosphate (DOXP-MEP) pathway involved in isoprenoid biosynthesis. In this study, we cloned the complete cDNA of potato DXS gene that was designated StDXS1. StDXS1 cDNA encodes for 719 amino acid residues, with MW of 77.8kDa, and is present in one copy in the potato genome. Phylogenetic analysis and protein sequence alignments assigned StDXS1 to a group with DXS homologues from closely related species and exhibited homodomain identity with known DXS proteins from other plant species. Late blight symptoms occurred in parallel with a reduction in StDXS1 transcript levels, which may be associated with the levels of isoprenoids that contribute to plant protection against pathogens. Subcellular localization indicated that StDXS1 targets the chloroplasts where isoprenoids are synthesized. Arabidopsis expressing StDXS1 showed a higher accumulation of carotenoids and chlorophyll as compared to wild type controls.