Pravastatin (Pravachol, Mevalotin)

Hara, Yasushi; Nagaoka, Sadao

doi:10.1007/978-981-13-8906-1_3

Cited by 3 publications

(5 citation statements)

References 11 publications

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“…During the compactin medication research phase, Sankyo Co., Ltd. (now Daiichi Sankyo) found pravastatin (C 23 H 36 O 7 ) as an active compactin metabolite in canine urine 53 . Blocking the cholesterol-producing enzyme HMG-CoA reductase reduces cholesterol production in the liver [54][55][56] .…”

Section: Fig 4: Chemical Structure Of Fluvastatinmentioning

confidence: 99%

Untitled

2023

IJPSR

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Statins are the first line of defense in the treatment of dyslipidemia and hypercholesterolemia illness. HMG-CoA reductase inhibitors or statins are the most widely prescribed drugs for persons at risk of cardiovascular disease. Cardiovascular disease (CVD) is the leading cause of death and a major cause of morbidity around the world. Statins have the same mechanism of action, but their chemical structures, pharmacokinetic profiles, and lipid-modifying potency differ. Triglycerides, cholesterol, and low-density lipoprotein (LDL) levels in the blood are all known risk factors for vascular disease, but statin drugs help to increase high-density lipoprotein (HDL) levels in our bloodstream. Some of the drugs utilized include rosuvastatin, atorvastatin, simvastatin, and pravastatin. According to clinical data, rosuvastatin is the most effective drug for decreasing low-density lipoprotein cholesterol and triglycerides, followed by atorvastatin, simvastatin and pravastatin. A brief review of the analytical methods developed from 2001-2021 for the estimation of Antilipidemic drugs has been discussed in the present study. This study will help the researchers to develop better methods for this class of drugs.

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Section: Fig 4: Chemical Structure Of Fluvastatinmentioning

confidence: 99%

Untitled

2023

IJPSR

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“…$5 billion. 229 It was detected as an active urinary metabolite of compactin and was subsequently isolated from canine urine. 230 Structure elucidation revealed that pravastatin represented a 6β-hydroxylated derivative of compactin, and it ́s activity was found to be 10fold higher than that of compactin.…”

Section: Alcoholsmentioning

confidence: 99%

“…By 2003, pravastatin became a blockbuster drug with annual sales of ca. $5 billion . It was detected as an active urinary metabolite of compactin and was subsequently isolated from canine urine .…”

Section: Functional Groups Formed In Biocatalytic Reactions For Api S...mentioning

confidence: 99%

“…It was detected as an active urinary metabolite of compactin and was subsequently isolated from canine urine . Structure elucidation revealed that pravastatin represented a 6β-hydroxylated derivative of compactin, and it́s activity was found to be 10-fold higher than that of compactin . Although an industrial chemical synthesis of pravastatin had initially been attempted, it was deemed economically unfeasible.…”

Section: Functional Groups Formed In Biocatalytic Reactions For Api S...mentioning

confidence: 99%

“…230 Structure elucidation revealed that pravastatin represented a 6β-hydroxylated derivative of compactin, and it ́s activity was found to be 10fold higher than that of compactin. 229 Although an industrial chemical synthesis of pravastatin had initially been attempted, it was deemed economically unfeasible. As a solution, microbial hydroxylation of compactin (obtained by fermentation) was developed.…”

Section: Alcoholsmentioning

confidence: 99%

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Shortening Synthetic Routes to Small Molecule Active Pharmaceutical Ingredients Employing Biocatalytic Methods

et al. 2021

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Biocatalysis, using enzymes for organic synthesis, has emerged as powerful tool for the synthesis of active pharmaceutical ingredients (APIs). The first industrial biocatalytic processes launched in the first half of the last century exploited whole-cell microorganisms where the specific enzyme at work was not known. In the meantime, novel molecular biology methods, such as efficient gene sequencing and synthesis, triggered breakthroughs in directed evolution for the rapid development of process-stable enzymes with broad substrate scope and good selectivities tailored for specific substrates. To date, enzymes are employed to enable shorter, more efficient, and more sustainable alternative routes toward (established) small molecule APIs, and are additionally used to perform standard reactions in API synthesis more efficiently. Herein, large-scale synthetic routes containing biocatalytic key steps toward >130 APIs of approved drugs and drug candidates are compared with the corresponding chemical protocols (if available) regarding the steps, reaction conditions, and scale. The review is structured according to the functional group formed in the reaction.

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Comparative Analysis of Bioelectrocatalytic Cytochrome P450 3A4 Systems

Koroleva,

Shumyantseva

2024

BMCRM

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This article describes the approaches developed by the authors with the aim to increase the efficiency of electro enzymatic reactions catalyzed by cytochrome P450 3A4. A comparative analysis of cytochrome P450 3A4 systems was carried out during the formation of the functional complexes hemoprotein-flavin nucleotides as low-molecular models of NAD(P)H-dependent cytochrome P450 reductase. The formation of a productive enzyme-substrate complex before the stage ofaccepting electrons from the modified electrode was studied from the electocatalytic viewpoint. Incorporation of the enzyme into nanopores of different nature on the electrode (2D-3D transition) was also studied. The results on the electrochemical reduction of bactosomes as the functionally active models of the microsomal monooxygenase system are also considered. The electrochemical and electrocatalytic parameters of cytochrome P450 3A4 were compared for different models of the electrocatalytic generation of metabolites.

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Pravastatin (Pravachol, Mevalotin)

Cited by 3 publications

References 11 publications

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Untitled

Shortening Synthetic Routes to Small Molecule Active Pharmaceutical Ingredients Employing Biocatalytic Methods

Comparative Analysis of Bioelectrocatalytic Cytochrome P450 3A4 Systems

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