Substrate selectivity and kinetic studies of (S)-specific alcohol dehydrogenase purified from Candida parapsilosis ATCC 7330

Pinto, Jerrina; Chadha, Anju; Gummadi, Sathyanarayana N.

doi:10.1016/j.bcab.2022.102410

Cited by 4 publications

(3 citation statements)

References 42 publications

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“…Pinto et al. found similar outcomes, with ortho substituents other than fluorine showing low conversion rates [49] . Additionally, both CmADH (ADH from Candida maris ) and PfADH (ADH from Pichia finlandica ) showed higher conversion rates for substrate 21 a over 1 a , echoing our findings [50] .…”

Section: Resultssupporting

confidence: 89%

“…Pinto et al found similar outcomes, with ortho substituents other than fluorine showing low conversion rates. [49] Additionally, both CmADH (ADH from Candida maris) and PfADH (ADH from Pichia finlandica) showed higher conversion rates for substrate 21 a over 1 a, echoing our findings. [50] Our variants, particularly ELK and EMK, demonstrated relatively high activity for most substrates, indicating a degree of catalytic promiscuity.…”

Section: Substrate Scope Of Lbadhsupporting

confidence: 85%

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Directed Evolution and Immobilization of Lactobacillus brevis Alcohol Dehydrogenase for Chemo‐Enzymatic Synthesis of Rivastigmine

Su,

Ran,

Liu

et al. 2024

Chemistry A European J

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Rivastigmine is one of the several pharmaceuticals widely prescribed for the treatment of Alzheimer's disease. However, its practical synthesis still faces many issues, such as the involvement of toxic metals and harsh reaction conditions. Herein, we report a chemo‐enzymatic synthesis of Rivastigmine. The key chiral intermediate was synthesized by an engineered alcohol dehydrogenase from Lactobacillus brevis (LbADH). A semi‐rational approach was employed to improve its catalytic activity and thermal stability. Several LbADH variants were obtained with a remarkable increase in activity and melting temperature. Exploration of the substrate scope of these variants demonstrated improved activities toward various ketones, especially acetophenone analogs. To further recycle and reuse the biocatalyst, one LbADH variant and glucose dehydrogenase were co‐immobilized on nanoparticles. By integrating enzymatic and chemical steps, Rivastigmine was successfully synthesized with an overall yield of 66%. This study offers an efficient chemo‐enzymatic route for Rivastigmine and provides several efficient LbADH variants with a broad range of potential applications.

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Section: Resultssupporting

confidence: 89%

Section: Substrate Scope Of Lbadhsupporting

confidence: 85%

Directed Evolution and Immobilization of Lactobacillus brevis Alcohol Dehydrogenase for Chemo‐Enzymatic Synthesis of Rivastigmine

Su,

Ran,

Liu

et al. 2024

Chemistry A European J

View full text Add to dashboard Cite

show abstract

“…57,58 In biology, this reaction mechanism is called the ordered Bi-Bi mechanism, and many dehydrogenases, such as alcohol dehydrogenase, formic acid dehydrogenase, malate dehydrogenase, and 6-phosphate glucose dehydrogenase, follow this mechanism. 49,59,60 Thus, the N-C and Fe-N-C nanozymes demonstrated a Ping-Pong and ordered Bi-Bi mechanism, respectively. This indicated the necessity of a catalyst to promote this reaction.…”

Section: Resultsmentioning

confidence: 94%

Insights of Oxygen Reduction Selectivity and Fe Leaching from Fe-N-C Nanozyme in Ascorbate Oxidation

Cao¹,

Zhu²,

Hong³

et al. 2023

Preprint

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Ascorbic acid (H2A) is a well-known antioxidant to protect cellular components from free radical damage, meanwhile it is also emerged as pro-oxidant in cancer therapy. However, such contradictory mechanisms underlying H2A oxidation are not well understood. Here, we report the discovery of Fe leaching during catalytic H2A oxidation using Fe-N-C nanozyme as a ferritin mimic and its influence in selectivity of oxygen reduction reaction (ORR). Owing to the heterogeneity, Fe-Nx sites in Fe-N-C primarily catalyzed the H2A oxidation and 4e ORR via an iron-oxo intermediate; meanwhile marginal N-C sites catalyzed the 2e ORR via an O2 intermediate with H2O2 production, although which was less favorable in kinetics and hardly observable in the early stage. Nonetheless, trace O2 accumulated and attacked Fe-Nx sites, leading to a linear leakage of unstable Fe ions up to 420 ppb when the concentration of H2A increased. As a result, a substantial fraction (~40%) of N-C sites on Fe-N-C were activated, and a new path for Fenton-type H2A oxidation was finally enabled. After Fe ions diffused into the bulk solution, the ORR at the N-C sites stopped at H2O2 production, which was the origin for the pro-oxidant effect by H2A. This work highlights the Fe-leakage occurring on Fe-N-C nanozymes and uncovers the multifaceted insights of ORR selectivity in H2A oxidation under realistic conditions.

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Insight into Iron Leaching from an Ascorbate‐Oxidase‐like Fe−N−C Nanozyme and Oxygen Reduction Selectivity**

et al. 2023

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Ascorbate (H 2 A) is a well-known antioxidant to protect cellular components from free radical damage and has also emerged as a pro-oxidant in cancer therapies. However, such "contradictory" mechanisms underlying H 2 A oxidation are not well understood. Herein, we report Fe leaching during catalytic H 2 A oxidation using an FeÀ NÀ C nanozyme as a ferritin mimic and its influence on the selectivity of the oxygen reduction reaction (ORR). Owing to the heterogeneity, the Fe-N x sites in FeÀ NÀ C primarily catalyzed H 2 A oxidation and 4 e À ORR via an iron-oxo intermediate. Nonetheless, trace O 2 *À produced by marginal NÀ C sites through 2 e À ORR accumulated and attacked Fe-N x sites, leading to the linear leakage of unstable Fe ions up to 420 ppb when the H 2 A concentration increased to 2 mM. As a result, a substantial fraction (ca. 40 %) of the NÀ C sites on FeÀ NÀ C were activated, and a new 2 + 2 e À ORR path was finally enabled, along with Fentontype H 2 A oxidation. Consequently, after Fe ions diffused into the bulk solution, the ORR at the NÀ C sites stopped at H 2 O 2 production, which was the origin of the pro-oxidant effect of H 2 A.

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Substrate selectivity and kinetic studies of (S)-specific alcohol dehydrogenase purified from Candida parapsilosis ATCC 7330

Cited by 4 publications

References 42 publications

Directed Evolution and Immobilization of Lactobacillus brevis Alcohol Dehydrogenase for Chemo‐Enzymatic Synthesis of Rivastigmine

Directed Evolution and Immobilization of Lactobacillus brevis Alcohol Dehydrogenase for Chemo‐Enzymatic Synthesis of Rivastigmine

Insights of Oxygen Reduction Selectivity and Fe Leaching from Fe-N-C Nanozyme in Ascorbate Oxidation

Insight into Iron Leaching from an Ascorbate‐Oxidase‐like Fe−N−C Nanozyme and Oxygen Reduction Selectivity**

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