1361311-47-8

Basic information

• Product Name: C₅₂H₅₄NO₇PSi
• Synonyms: C₅₂H₅₄NO₇PSi
• CAS NO: 1361311-47-8
• Molecular Weight: 864.063
• Mol File: 1361311-47-8.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: C₅₂H₅₄NO₇PSi(CAS DataBase Reference)
• NIST Chemistry Reference: C₅₂H₅₄NO₇PSi(1361311-47-8)
• EPA Substance Registry System: C₅₂H₅₄NO₇PSi(1361311-47-8)

Safety Data

• Hazardous Substances Data: 1361311-47-8(Hazardous Substances Data)

Upstream product

• 66-72-8 pyridoxal 
• 700-73-2 5-hydroxymethyl-2-methyl-pyridine-3,4-diol 
• 1361311-48-9 C₃₈H₄₁NO₄Si 
• 1361311-50-3 C₃₇H₃₉NO₃Si 
• 1361311-52-5 C₂₃H₂₇NO₃Si 

Downstream Products

• 1361311-45-6 C₃₆H₃₆NO₇P 
• 1361311-14-9 C₅₀H₄₉NO₉P₂ 

Relevant articles and documents

Rational design, synthesis and evaluation of first generation inhibitors of the Giardia lamblia fructose-1,6-biphosphate aldolase

Inhibitors of the Giardia lamblia fructose 1,6-bisphosphate aldolase (GlFBPA), which transforms fructose 1,6-bisphosphate (FBP) to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate, were designed based on 3-hydroxy-2-pyridone and 1,2-dihydroxypyridine scaffolds that position two negatively charged tetrahedral groups for interaction with substrate phosphate binding residues, a hydrogen bond donor to the catalytic Asp83, and a Zn 2+ binding group. The inhibition activities for the GlFBPA catalyzed reaction of FBP of the prepared alkyl phosphonate/phosphate substituted 3-hydroxy-2-pyridinones and a dihydroxypyridine were determined. The 3-hydroxy-2-pyridone inhibitor 8 was found to bind to GlFBPA with an affinity (Ki = 14 μM) that is comparable to that of FBP (Km = 2 μM) or its inert analog TBP (Ki = 1 μM). The X-ray structure of the GlFBPA-inhibitor 8 complex (2.3 A?) shows that 8 binds to the active site in the manner predicted by in silico docking with the exception of coordination with Zn2+. The observed distances and orientation of the pyridone ring O=C-C-OH relative to Zn2+ are not consistent with a strong interaction. To determine if Zn2+coordination occurs in the GlFBPA-inhibitor 8 complex in solution, EXAFS spectra were measured. A four coordinate geometry comprised of the three enzyme histidine ligands and an oxygen atom from the pyridone ring O=C-C-OH was indicated. Analysis of the Zn2+ coordination geometries in recently reported structures of class II FBPAs suggests that strong Zn2+ coordination is reserved for the enediolate-like transition state, accounting for minimal contribution of Zn 2+ coordination to binding of 8 to GlFBPA.