190079-18-6

Basic information

• Product Name: (2,3-dihydroxy-4-oxo-pentoxy)phosphonic acid
• Synonyms: (2,3-dihydroxy-4-oxo-pentoxy)phosphonic acid;1-Deoxy-D-xylulose 5-phosphate;1-Deoxy-D-xylulose 5-phosphate (DXP);1-Deoxy-D-xylulose-5-phosphate sodium salt
• CAS NO: 190079-18-6
• Molecular Formula: C₅H₁₁O₇P
• Molecular Weight: 214.110401
• Mol File: 190079-18-6.mol
• Article Data: 8

Chemical Properties

• Boiling Point: 528.9°Cat760mmHg
• Flash Point: 273.7°C
• Appearance: /
• Density: 1.653g/cm³
• Vapor Pressure: 0mmHg at 25°C
• Storage Temp.: ?20°C
• PKA: 1.82±0.10(Predicted)
• BRN: 8367371
• CAS DataBase Reference: (2,3-dihydroxy-4-oxo-pentoxy)phosphonic acid(CAS DataBase Reference)
• NIST Chemistry Reference: (2,3-dihydroxy-4-oxo-pentoxy)phosphonic acid(190079-18-6)
• EPA Substance Registry System: (2,3-dihydroxy-4-oxo-pentoxy)phosphonic acid(190079-18-6)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 190079-18-6(Hazardous Substances Data)

Usage

Uses

1-Deoxy-D-xylulose 5-Phosphate is a precursor metabolite of the 2C-Methyl-D-erythritol-4-phosphate (MEP) pathway, from the simple and renewable starting materials D-arabinose and hydroxyacetone.

InChI:InChI=1/C5H11O7P/c1-3(6)5(8)4(7)2-12-13(9,10)11/h4-5,7-8H,2H2,1H3,(H2,9,10,11)/p-2/t4-,5-/m1/s1

Upstream product

• 591-57-1 D-glyceraldehyde-3-phosphate 
• 113-24-6 sodium pyruvate 
• 57-60-3 piruvate 
• 127-17-3 2-oxo-propionic acid 

Downstream Products

• 206440-72-4 2-C-methyl-D-erythritol 4-phosphate 
• 447-05-2 5-hydroxy-4-(hydroxymethyl)-6-methyl-3-pyridylmethyl dihydrogen phosphate 
• 10023-48-0 2-[3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-1,3-thiazol-3-ium-5-yl]ethyl dihydrogen phosphate 

Relevant articles and documents

Observation of thiamin-bound intermediates and microscopic rate constants for their interconversion on 1-deoxy- d -xylulose 5-phosphate synthase: 600-Fold rate acceleration of pyruvate decarboxylation by d -glyceraldehyde-3-phosphate.

The thiamin diphosphate (ThDP)-dependent enzyme 1-deoxy-d-xylulose 5-phosphate (DXP) synthase carries out the condensation of pyruvate as a 2-hydroxyethyl donor with d-glyceraldehyde-3-phosphate (d-GAP) as acceptor forming DXP. Toward understanding catalysis of this potential anti-infective drug target, we examined the pathway of the enzyme using steady state and presteady state kinetic methods. It was found that DXP synthase stabilizes the ThDP-bound predecarboxylation intermediate formed between ThDP and pyruvate (C2α-lactylThDP or LThDP) in the absence of d-GAP, while addition of d-GAP enhanced the rate of decarboxylation by at least 600-fold. We postulate that decarboxylation requires formation of a ternary complex with both LThDP and d-GAP bound, and the central enzyme-bound enamine reacts with d-GAP to form DXP. This appears to be the first study of a ThDP enzyme where the individual rate constants could be evaluated by time-resolved circular dichroism spectroscopy, and the results could have relevance to other ThDP enzymes in which decarboxylation is coupled to a ligation reaction. The acceleration of the rate of decarboxylation of enzyme-bound LThDP in the presence of d-GAP suggests a new approach to inhibitor design.

An improved preparation of D-glyceraldehyde 3-phosphate and its use in the synthesis of 1-deoxy-D-xylulose 5-phosphate

D-Glyceraldehyde 3-phosphate (=D-GAP; 2) was prepared by an improved chemical method (Scheme 2), and it was then employed to synthesize 1-deoxy-d-xylulose 5-phosphate (=DXP; 3) which is enzymatically one of the key intermediates in the MEP (4) terpenoid b

Formation of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol from 2-C- methyl-D-erythritol 4-phosphate by 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, a new enzyme in the nonmevalonate pathway

2-C-Methyl,D-erythritol 4-phosphate is transformed to 4-(cytidine 5'- diphospho)-2-C-methyl-D-erythritol in the presence of cytidine 5'- triphosphate by a novel Escherichia coli enzyme, 2-C-methyl-D-erythritol 4- phosphate cytidylyltransferase, involved in the nonmevalonate pathway. (C) 2000 Elsevier Science Ltd.

DXP synthase-catalyzed c-n bond formation: Nitroso substrate specificity studies guide selective inhibitor design

1-Deoxy-D-xylulose 5-phosphate (DXP) synthase catalyzes the first step in the nonmammalian isoprenoid biosynthetic pathway to form DXP from pyruvate and D-glyceraldehyde 3-phosphate (D-GAP) in a thiamin diphosphate-dependent manner. Its unique structure and mechanism distinguish DXP synthase from its homologues and suggest that it should be pursued as an anti-infective drug target. However, few reports describe any development of selective inhibitors of this enzyme. Here, we reveal that DXP synthase catalyzes C-N bond formation and exploit aromatic nitroso substrates as active site probes. Substrate specificity studies reveal a high affinity of DXP synthase for aromatic nitroso substrates compared to the related ThDP-dependent enzyme pyruvate dehydrogenase (PDH). Results from inhibition and mutagenesis studies indicate that nitroso substrates bind to E. coli DXP synthase in a manner distinct from that of D-GAP. Our results suggest that the incorporation of aryl acceptor substrate mimics into unnatural bisubstrate analogues will impart selectivity to DXP synthase inhibitors. As a proof of concept, we show selective inhibition of DXP synthase by benzylacetylphosphonate (BnAP).