3913-64-2

Usage

Uses

Used in Pharmaceutical Industry:
[S,(+)]-2-Hydroxypropionaldehyde is used as an intermediate in the synthesis of various pharmaceutical compounds for its ability to contribute to the development of new drugs.
Used in Fragrance Industry:
[S,(+)]-2-Hydroxypropionaldehyde is used as a component in the creation of fragrance compounds due to its reactive nature and potential to form complex aromatic molecules.
Used in Agricultural Chemical Industry:
[S,(+)]-2-Hydroxypropionaldehyde is used as an intermediate in the production of agricultural chemicals, contributing to the development of effective pest control agents and other agrochemicals.
Used in Polymer and Plastics Industry:
[S,(+)]-2-Hydroxypropionaldehyde is used in the synthesis of 1,3-propanediol, which is an important industrial chemical for the production of polymers and plastics, known for their diverse applications in various consumer and industrial products.
Used in Food Preservation:
[S,(+)]-2-Hydroxypropionaldehyde is used as a preservative in the food industry, leveraging its antimicrobial properties to extend the shelf life of perishable goods.
Used in Cosmetics Industry:
[S,(+)]-2-Hydroxypropionaldehyde is used in cosmetics for its antioxidant properties, helping to prevent the oxidation of ingredients and maintain product stability and efficacy.

Upstream product

• 3913-65-3 2-hydroxypropanal 
• 42919-42-6 (S)-1,1-dimethoxy-2-hydroxypropane 
• 92418-41-2 L-Fuculose-1-phosphate 

Downstream Products

• 177981-87-2 (Z)-N-[(S)-benzoxypropylidene]benzylamine N-oxide 
• 113421-83-3 5-deoxy-L-xylose hydrate 
• 113421-72-0 5-deoxy-α-L-xylose 
• 113421-73-1 5-deoxy-β-L-xylose 
• 128613-49-0 C₁₀H₁₃NO₃ 
• 14807-05-7 6-deoxy-L-arabino-2-hexulose 
• 73-34-7 L-rhamnose 
• 92418-41-2 L-Fuculose-1-phosphate 
• 444-09-7 L-rhamnulose 1-phosphate 

Relevant academic research and scientific papers

Structural characterization of an L-fuculose-1-phosphate aldolase from Klebsiella pneumoniae

Fuculose phosphate aldolases play an important role in glycolysis and gluconeogenesis pathways. L-fuculose 1-phosphate aldolase catalyzes the reversible cleavage of L-fuculose 1-phosphate to DHAP and L-lactaldehyde. Class II aldolases found in bacteria are linked to pathogenesis of human pathogens, and have potential applications in the biosynthesis of carbohydrates and other chiral compounds. Here we report the structure of a putative L-fuculose 1-phosphate aldolase (KpFucA) from the nosocomial pathogen Klebsiella pneumoniae to 1.85 ? resolution. The enzyme crystallizes in space group P422 with one monomer per asymmetric unit. Analytical ultracentrifugation analysis confirms that KpFucA is a tetramer in solution. A magnesium ion cofactor and sulfate ion were identified in the active pocket. Enzyme activity assays confirmed that KpFcuA has a strong preference for L-fuculose 1-phosphate as a substrate, but can also catalyze the cleavage of fructose-1,6-bisphosphate and glucose-6-phosphate. This work should provide a starting point for further investigation of the role of KpFucA in K. pneumoniae pathogenesis or in industrial applications.

Enzymatic vs. Fermentative Synthesis: Thermostable Glucose Dehydrogenase Catalyzed Regeneration of NAD(P)H for use in Enzymatic Synthesis

Procedures are described for regeneration of reduced nicotinamide cofactors NADH and NADPH from NAD(P) based on glucose and a thermostable glucose dehydrogenase from Bacillus cereus immobilized in polyacrylamide gels.The turnover number for NAD in a synthesis of 200 mmol of D-lactate is 40000.Application of this system to other syntheses is demonstrated with preparations of ethyl (R)-4-chloro-3-hydroxybutanoate, (R)-2,2,2-trifluoro-1-phenylethanol, ethyl (S)-3-hydroxyvalerate, (S)-lactaldehyde dimethyl acetal, and (S)-3-hydroxybutanal dimethyl acetal.Further investigation of the kinetics regarding the thermoresistance of glucose dehydrogenase in the presence of NaCl has been carried out, and it appears that the enhancement by NaCl of the thermal stability of the enzyme is approximately third order.The immobilized glucose dehydrogenase incubated at 55 deg C, pH 7.5, for 7 days is still fully active while many other enzymes are completely inactivated in 1-2 days.Addition of NaCl enhances the thermal stability more significantly than the immobilization does, and a remarkable increase in thermal stability was observed with these two combined factors.The half-life of the immobilized glucose dehydrogenase at 55 deg C in a buffer (pH 7.0-7.5) containing 1 M NaCl is more than 30 days compared to 3 min for the free enzyme, corresponding to an overall ca. 50000-fold increase in thermal stability.