Synonyms:Acid, Pyruvic;Pyruvate;Pyruvic Acid
99% *data from raw suppliers
There total 19 articles about Pyruvate which guide to synthetic route it. The literature collected by LookChem mainly comes from the sharing of users and the free literature resources found by Internet computing technology. We keep the original model of the professional version of literature to make it easier and faster for users to retrieve and use. At the same time, we analyze and calculate the most feasible synthesis route with the highest yield for your reference as below:
Reference yield: 88.0%
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The research study on DXP Synthase-Catalyzed C-N Bond Formation, which is crucial for the selective inhibitor design targeting the enzyme DXP synthase. The purpose of the study was to understand the substrate specificity of DXP synthase, particularly its affinity for aromatic nitroso substrates, and to explore its potential as a drug target for anti-infective agents. The researchers discovered that DXP synthase has a high affinity for aromatic nitroso substrates, which are more reactive than their aldehyde counterparts, and that it can catalyze the formation of C-N bonds to generate aromatic hydroxamic acids or amides. They also found that DXP synthase has a larger active site compared to related enzymes like pyruvate dehydrogenase (PDH), which allows it to accommodate sterically demanding substrates. The study concluded that incorporating aryl acceptor substrate mimics into unnatural bisubstrate analogues could lead to selective inhibitors of DXP synthase. Key chemicals used in the process include 1-deoxy-d-xylulose 5-phosphate (DXP), pyruvate, d-glyceraldehyde 3-phosphate (d-GAP), thiamin diphosphate (ThDP), and various aromatic nitroso substrates such as nitrosobenzene and nitrosonaphthols. The researchers also synthesized benzylacetylphosphonate (BnAP) as a potential selective inhibitor of DXP synthase, demonstrating its effectiveness in inhibiting the enzyme with higher selectivity compared to PDH.
The study investigates the use of hydrogen-bonding catalysts, specifically thioureas and phosphoric acids, in the three-component reactions of pyruvate, anilines, and aldehydes to produce 3-amino-1,5-dihydro-2H-pyrrol-2-ones. These catalysts significantly enhance the reaction yields, with the most effective catalysts identified through screening experiments. The study also explores the substrate scope, demonstrating the reaction's versatility with various substituted anilines and aldehydes. Additionally, the research delves into asymmetric catalysis using chiral versions of these catalysts, achieving moderate enantioselectivity. The findings highlight the potential of hydrogen-bonding catalysts in synthesizing structurally diverse compounds, which are valuable in drug discovery.
This study explores the use of N-acetylneuraminate pyruvate lyase (sialyl aldolase) in organic synthesis. The study demonstrates that sialyl aldolase can catalyze the condensation of pyruvate with various non-nitrogenous sugars, such as D-mannose, to produce ulosonic acids like 3-deoxy-D-glycero-D-galacto-2-nonulosonic acid (KDN). The enzyme shows a broad specificity, accepting substrates with different substituents at C(2) provided the D-manno configuration is retained. The authors successfully synthesized several ulosonic acids using immobilized lyase, achieving good yields and demonstrating the potential for scaling up the process. They also explored the enzyme's tolerance to various modifications at different positions of the sugar molecule, revealing its preference for certain configurations and the challenges in using D-arabinose as a substrate.
The research investigates the inhibitory effects of oxythiamine pyrophosphate (OTPP) and 3-deazathiamine pyrophosphate (DATPP) on the pyruvate dehydrogenase complex (PDHC) and their impact on HeLa cell growth. The study found that DATPP was a stronger competitive inhibitor of PDHC with a Ki value of 0.0026 mM compared to OTPP's Ki value of 0.025 mM. However, despite its superior inhibitory properties on PDHC, DATPP did not significantly affect HeLa cell growth or viability, whereas OTPP and oxythiamine (OT) showed a significant cytostatic effect. The researchers hypothesize that the differences in the cytostatic effects may be due to the physicochemical properties of the compounds and the difficulty in transporting DATPP across the cell membrane. The findings suggest that while DATPP is a potent inhibitor of PDHC, its effectiveness as a cytostatic agent may be limited by its cellular uptake and transport mechanisms.
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