Microbial reduction of ethyl 2-oxo-4-phenylbutyrate. Searching for R-enantioselectivity. New access to the enalapril like ACE inhibitors

Lacerda, Paulo S. Bergo de; Ribeiro, Joyce Benzaquem; Leite, Selma Gomes Ferreira; Ferrara, Maria Antonieta; Coelho, Ricardo B.; Bon, Elba P. S.; Lima, Edson Luiz da Silva; Antunes, Octávio Augusto Ceva

doi:10.1016/j.tetasy.2006.04.008

Cited by 25 publications

(8 citation statements)

References 31 publications

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“…[8] However, only few microorganisms were described as efficient biocatalysts in the reduction of ethyl 2-oxophenylbutyrate to ethyl (R)-2-hydroxy-4-phenylbutyrate, [7] Lacerda and co-workers reported the reduction of ethyl 2-oxo-4-phenylbutyrate with K. marxianus, P. anomala, P. angusta to give the ethyl (R)-2-hydroxy-4-phenylbutyrate in low to moderate enantioselectivity (35% ee, 35% ee, and 81% ee, respectively). [9] Besides, Chadha et al reported that the enantioselective reduction of ethyl 2-oxophenylbutyrate to ethyl (R)-2-hydroxy-4-phenylbutyrate by using Daucus carota (wild carota) with excellent chemical yield (90%) and ee (99%). [10] However, in this process, a large amount of cells was needed, while this procedure was timeconsuming (10 days).…”

Section: Introductionmentioning

confidence: 99%

Preparation the Key Intermediate of Angiotensin‐Converting Enzyme (ACE) Inhibitors: High Enantioselective Production of Ethyl (R)‐2‐Hydroxy‐4‐Phenylbutyrate with Candida boidinii CIOC21

Chen

Lin

et al. 2008

Adv Synth Catal

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Forty microorganisms belonging to different taxonomical groups were used to catalyze the enantioselective reduction of ethyl 2-oxophenylbutyrate to afford the corresponding ethyl 2-hydroxy-4-phenylbutyrate. Several microorganisms led to over 99% ee of ethyl (S)-2-hydroxy-4-phenylbutyrate. Especially, we firstly found that the Candida boidinii CIOC21 could be effectively used for the enantioselective preparation the ethyl (R)-2-hydroxy-4-phenylbutyrate in pure aqueous medium with 99% ee, a key intermediate in the production of angiotensinconverting enzyme (ACE) inhibitors.

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Section: Introductionmentioning

confidence: 99%

Preparation the Key Intermediate of Angiotensin‐Converting Enzyme (ACE) Inhibitors: High Enantioselective Production of Ethyl (R)‐2‐Hydroxy‐4‐Phenylbutyrate with Candida boidinii CIOC21

Chen

Lin

et al. 2008

Adv Synth Catal

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“…At 4.1 g L −1 OPBE loading, the ee and isolation yield could reach 90% and 58%, respectively, using C. holmii KPY 12402 [33,34]. Kluyveromyces marxianus, Pichia pastoris, Pichia anomala, and Pichia angusta have also been tested in the asymmetric reduction of OPBE into (R)-HPBE, and P. angusta displayed the best performance of 100% conversion and 81% ee [35]. Besides, Chadha et al reported the preparation of (R)-HPBE from OPBE by using Daucus carota with excellent chemical yield (90%) and ee (99%) [36].…”

Section: Screening Of Microorganisms For Bioreductive Preparation Of mentioning

confidence: 99%

Bioreductive preparation of ACE inhibitors precursor (R)-2-hydroxy-4-phenylbutanoate esters: Recent advances and future perspectives

2015

Bioresour. Bioprocess.

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Optically active (R)-2-hydroxy-4-phenylbutanoate esters ((R)-HPBE) are key precursors for the production of angiotension-converting enzyme (ACE) inhibitors, which are important prescriptive drugs for preventing the formation of angiotensin II and lowering the blood pressure. The biocatalytic asymmetric reduction of ethyl 2-oxo-4-phenylbutanoate (OPBE) to (R)-HPBE with carbonyl reductases has several advantageous attributes, including high enantioselectivity, mild reaction condition, high catalytic efficiency, and environmental benignity. An increasing number of OPBE reductases have been discovered owing to the drastic achievements in genomics, screening and evolution technologies, and process engineering. The potential of (R)-HPBE production process has also been intensively evaluated. This review covers recent progress on the bioreductive preparation of (R)-HPBE, especially on various screening approaches for the identification of OPBE reductases and their characterization.

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“…However, the majority of prochiral ketones used in industrial applications are structurally complex. These include ketoesters and heterocyclic ketones bearing bulky substituents, such as ethyl (R)-2-hydroxy-4-phenylbutyrate [(R)-HPBE], a key precursor for the preparation of an anti-hypertension drug, the angiotensin-converting enzyme (ACE) inhibitor (de Lacerda et al 2006), and (S)-N-benzyl-3-pyrrolidinol, an important intermediate for the preparation of antitumor and anesthetic drugs (Kizaki et al 2008). Substrate size-induced deficiency of enzyme activity is still a challenge for the enzymatic reduction of ketones.…”

Section: Introductionmentioning

confidence: 99%

Gene mining-based identification of aldo–keto reductases for highly stereoselective reduction of bulky ketones

Liang

Nie

et al. 2018

Bioresour. Bioprocess.

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Background: Aldo-keto reductase (AKR) or alcohol dehydrogenases (ADH)-mediated stereoselective reduction of prochiral carbonyl compounds is an efficient way of preparing single enantiomers of chiral alcohols. However, steric hindrance of substrate affects the catalytic performance of enzymes. The present study aims to discover and identify AKRs/ADHs capable of catalyzing highly stereoselective reduction of sterically hindered ketones. Results:Five AKRs from different microorganisms (CaCR, ScCR, KmCR, CPR-C1, and CPR-C2) were identified through gene mining, and overexpressed in recombinant Escherichia coli BL21(DE3). The specific activity and stereoselectivity of the AKRs were further evaluated towards various ketoesters and heterocyclic ketones, which are sterically bulky and are valuable in industrial applications. Each purified enzyme exhibited catalytic activity to one or more of the tested substrates. Among the enzymes, ScCR showed a broader substrate spectrum compared to the others. Regarding K m values related to substrate association, we also provided insights into the specificity and preference of certain enzymes. Consequently, enantiopure (R)-methyl mandelate, ethyl (R)-mandelate, ethyl (R)-2-hydroxy-4-phenylbutyrate, and (S)-N-benzyl-3-pyrrolidinol (> 99%e.e.) were obtained through the identified AKRs. Conclusion:The stereospecific AKRs were obtained through gene mining, which possesses the potential for application in the preparation of important optically active alcohols.

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Microbial reduction of ethyl 2-oxo-4-phenylbutyrate. Searching for R-enantioselectivity. New access to the enalapril like ACE inhibitors

Cited by 25 publications

References 31 publications

Preparation the Key Intermediate of Angiotensin‐Converting Enzyme (ACE) Inhibitors: High Enantioselective Production of Ethyl (R)‐2‐Hydroxy‐4‐Phenylbutyrate with Candida boidinii CIOC21

Preparation the Key Intermediate of Angiotensin‐Converting Enzyme (ACE) Inhibitors: High Enantioselective Production of Ethyl (R)‐2‐Hydroxy‐4‐Phenylbutyrate with Candida boidinii CIOC21

Bioreductive preparation of ACE inhibitors precursor (R)-2-hydroxy-4-phenylbutanoate esters: Recent advances and future perspectives

Gene mining-based identification of aldo–keto reductases for highly stereoselective reduction of bulky ketones

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