Acidic proteinase from Aspergillus usamii catalyzed Michael addition of ketones to nitroolefins

Xu, Ke-Ling; Guan, Zhi; He, Yan‐Hong

doi:10.1016/j.molcatb.2011.04.005

Cited by 19 publications

(3 citation statements)

References 41 publications

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“…Some elegant works on the enzyme catalytic promiscuity have been described. 8,9 For example, a number of hydrolases were found to have the ability to catalyze aldol, 1,2,[10][11][12][13][14][15] Michael, [16][17][18][19][20][21] Henry, [22][23][24] Mannich 25 and Knoevenagel [26][27][28] reactions, and even some domino reactions. 29 Nevertheless, promiscuous enzyme catalyzed multicomponent reactions are still rather rare although there are a few examples reported.…”

Section: Introductionmentioning

confidence: 99%

Biocatalytic one-pot three-component synthesis of 3,3′-disubstituted oxindoles and spirooxindole pyrans using α-amylase from hog pancreas

Zeng

Yang

et al. 2015

RSC Adv.

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Section: Introductionmentioning

confidence: 99%

Biocatalytic one-pot three-component synthesis of 3,3′-disubstituted oxindoles and spirooxindole pyrans using α-amylase from hog pancreas

Zeng

Yang

et al. 2015

RSC Adv.

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“…Unfortunately, enzymes that naturally catalyse carbon–carbon bond-forming Michael-type additions are extremely rare 10 . A few elegant studies on promiscuous enzyme-catalysed carbon–carbon bond-forming Michael-type additions have been reported; however, most of these reactions proceed in organic solvent with low or moderate stereocontrol and do not involve acetaldehyde as donor substrate 11 12 13 14 15 16 17 18 .…”

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confidence: 99%

Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases

et al. 2016

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The Michael-type addition reaction is widely used in organic synthesis for carbon–carbon bond formation. However, biocatalytic methodologies for this type of reaction are scarce, which is related to the fact that enzymes naturally catalysing carbon–carbon bond-forming Michael-type additions are rare. A promising template to develop new biocatalysts for carbon–carbon bond formation is the enzyme 4-oxalocrotonate tautomerase, which exhibits promiscuous Michael-type addition activity. Here we present mutability landscapes for the expression, tautomerase and Michael-type addition activities, and enantioselectivity of 4-oxalocrotonate tautomerase. These maps of neutral, beneficial and detrimental amino acids for each residue position and enzyme property provide detailed insight into sequence–function relationships. This offers exciting opportunities for enzyme engineering, which is illustrated by the redesign of 4-oxalocrotonate tautomerase into two enantiocomplementary ‘Michaelases'. These ‘Michaelases' catalyse the asymmetric addition of acetaldehyde to various nitroolefins, providing access to both enantiomers of γ-nitroaldehydes, which are important precursors for pharmaceutically active γ-aminobutyric acid derivatives.

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“…In addition, among the many reported lipase‐catalyzed Michael additions, a general problem was the lack of enantioselectivity. In continuation of our work with enzymatic Michael additions,41, 42 we report herein the lipase from porcine pancreas (PPL) catalyzed Michael addition of 4‐hydroxycoumarin and α,β‐unsaturated enones to prepare warfarin and derivatives in organic medium in the presence of water.…”

Section: Introductionmentioning

confidence: 99%

Promiscuous enzyme‐catalyzed Michael addition: synthesis of warfarin and derivatives

Xie

Guan

2012

J of Chemical Tech & Biotech

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BACKGROUND: Biocatalytic promiscuity has attracted much attention from chemists and biochemists in recent years. Warfarin, one of the most effective anticoagulants, has been introduced for clinical use as a racemate for more than half a century. Although some different chemical strategies towards the synthesis of optically active warfarin have been reported, biocatalytic preparation of warfarin remains unexploited. RESULTS: Lipase from porcine pancreas (PPL) was used as a biocatalyst to catalyze the Michael addition of 4‐hydroxycoumarin to α,β‐unsaturated enones in organic medium in the presence of water to synthesize warfarin and derivatives. The products were obtained in moderate to high yields (up to 95%) with none or low enantioselectivities (up to 28% ee). The influence of reaction conditions including solvents, temperature and molar ratio of substrates was systematically investigated. CONCLUSION: Among the many reported lipase‐catalyzed Michael additions, only a few showed enantioselectivity. Therefore, this Michael addition activity of, for example, PPL is a valuable case of enantioselective lipase catalytic promiscuity. In addition, it was the first time warfarin and derivatives were prepared using a biocatalyst. Copyright © 2012 Society of Chemical Industry

show abstract

Acidic proteinase from Aspergillus usamii catalyzed Michael addition of ketones to nitroolefins

Cited by 19 publications

References 41 publications

Biocatalytic one-pot three-component synthesis of 3,3′-disubstituted oxindoles and spirooxindole pyrans using α-amylase from hog pancreas

Biocatalytic one-pot three-component synthesis of 3,3′-disubstituted oxindoles and spirooxindole pyrans using α-amylase from hog pancreas

Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases

Promiscuous enzyme‐catalyzed Michael addition: synthesis of warfarin and derivatives

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