Candida parapsilosis: A versatile biocatalyst for organic oxidation-reduction reactions

Chadha, Anju; Venkataraman, Sowmyalakshmi; Radhakrishnan, P.; Padhi, Santosh Kumar

doi:10.1016/j.bioorg.2016.08.007

Cited by 25 publications

(12 citation statements)

References 184 publications

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“…Lipase, esterase, halohydrin dehalogenase, and HNL catalyzed retro-Henry reaction are used in the kinetic resolution of a racemic β-nitroalcohol or an epoxide. [12][13][14][15][16] Alcohol dehydrogenase catalyzed asymmetric reduction, [17][18][19][20] and HNL catalyzed nitroaldol reaction [21][22][23][24][25] are the other two routes. Both kinetic resolution and asymmetric reduction requires an additional step of substrate preparation, while the former could provide a maximum 50% theoretical yield.…”

Section: Introductionmentioning

confidence: 99%

One‐Pot Enzyme Cascade Catalyzed Asymmetrization of Primary Alcohols: Synthesis of Enantiocomplementary Chiral β‐Nitroalcohols

2021

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Biocatalytic asymmetrization of inexpensive and stable primary alcohols to prepare enantioenriched β-nitroalcohols is an important development in green chemistry for the production of chiral pharmaceutical intermediates. Herein, we report a one-pot, two-step cascade reaction sequence in which first benzylic alcohols were oxidized to produce corresponding benzaldehydes using horse liver alcohol dehydrogenase (HLADH). The in situ generated aldehydes were then reacted in a biphasic medium with nitromethane by Arabidopsis thaliana hydroxynitrile lyase (AtHNL) or Baliospermum montanum HNL (BmHNL) catalyzed Henry reaction to produce stereoselective β-nitroalcohols with (R) or (S) configuration, respectively. Using HLADH-AtHNL, (R)-β-nitroalcohols were obtained in up to 64% conversion, and HLADH-BmHNL, (S)-β-nitroalcohols in up to 70% conversion, while in both cases excellent stereoselectivity (up to > 99% ee) was achieved. The concept was proven by functionalization of sp 3 CÀ H bond of ten simple achiral benzylic alcohols to enantiocomplementary chiral β-nitroalcohols.

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Section: Introductionmentioning

confidence: 99%

One‐Pot Enzyme Cascade Catalyzed Asymmetrization of Primary Alcohols: Synthesis of Enantiocomplementary Chiral β‐Nitroalcohols

2021

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“…The present study reports the isolation and characterization of a stereospecific imine reductase CpIM1 from Candida parapsilosis ATCC 7330, a rich source of oxidoreductases [27] , [28] , [29] . Imine reducing activities of various yeasts are known, and our earlier work on Candida parapsilosis ATCC 7330 reported the reduction of aryl imines using whole cells of this yeast [ 6 , 30 ].…”

Section: Introductionmentioning

confidence: 99%

Imine reduction by an Ornithine cyclodeaminase/μ-crystallin homolog purified from Candida parapsilosis ATCC 7330

Mahesh¹,

Chadha²

2021

Biotechnology Reports

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Highlights Novel imine reductase from yeast Candida parapsilosis purified and characterized. CpIM1 belongs to unexplored Ornithine cyclodeaminase/Mu crystallin protein family CpIM1 catalyzed stereospecific alkylamination of α-ketoacids/ketoesters. CpIM1 also reduced cyclic and aryl imines. First report on enzymatic alkylamination of α-ketoesters and reduction of arylimines.

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“…CpCR belongs to MDR superfamily and is reported to catalyse reductions of ketoesters, ketones and aldehydes leading to the production of some important pharmaceutical precursors [3]. It is one of the important enzymes present in Candida parapsilosis ATCC 7330, which is a well-known whole-cell biocatalyst [4]. CpCR, a heterodimer (PDB: 4OAQ), has two different Zn atoms viz.…”

Section: Introductionmentioning

confidence: 99%

Understanding (R) Specific Carbonyl Reductase from Candida parapsilosis ATCC 7330 [CpCR]: Substrate Scope, Kinetic Studies and the Role of Zinc

2019

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CpCR, an (R) specific carbonyl reductase, so named because it gave (R)-alcohols on asymmetric reduction of ketones and ketoesters, is a recombinantly expressed enzyme from Candida parapsilosis ATCC 7330. It turns out to be a better aldehyde reductase and catalyses cofactor (NADPH) specific reduction of aliphatic and aromatic aldehydes. Kinetics studies against benzaldehyde and 2,4-dichlorobenzaldehyde show that the enzyme affinity and rate of reaction change significantly upon substitution on the benzene ring of benzaldehyde. CpCR, an MDR (medium chain reductase/dehydrogenase) containing both structural and catalytic Zn atoms, exists as a dimer, unlike the (S) specific reductase (SRED) from the same yeast which can exist in both dimeric and tetrameric forms. Divalent metal salts inhibit the enzyme even at nanomolar concentrations. EDTA chelation decreases CpCR activity. However, chelation done after the enzyme is pre-incubated with the NADPH retains most of the activity implying that Zn removal is largely prevented by the formation of the enzyme-cofactor complex.

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Candida parapsilosis: A versatile biocatalyst for organic oxidation-reduction reactions

Cited by 25 publications

References 184 publications

One‐Pot Enzyme Cascade Catalyzed Asymmetrization of Primary Alcohols: Synthesis of Enantiocomplementary Chiral β‐Nitroalcohols

One‐Pot Enzyme Cascade Catalyzed Asymmetrization of Primary Alcohols: Synthesis of Enantiocomplementary Chiral β‐Nitroalcohols

Imine reduction by an Ornithine cyclodeaminase/μ-crystallin homolog purified from Candida parapsilosis ATCC 7330

Understanding (R) Specific Carbonyl Reductase from Candida parapsilosis ATCC 7330 [CpCR]: Substrate Scope, Kinetic Studies and the Role of Zinc

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