Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology

Arora, Benu; Mukherjee, Jaya; Gupta, Munishwar N.

doi:10.1186/s40508-014-0025-y

Cited by 36 publications

(33 citation statements)

References 87 publications

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“…Hydrolases, and in particular lipases, are some of enzymes where catalytic promiscuity has been most extensively studied, as they are able to catalyze a variety of different reactions other than hydrolysis of esters in nonaqueous media, such as transesterification alcoholysis or acidolysis [55]. However, more recently other enzymes have been described to have catalytic promiscuity, including NAD(P)H-dependent oxidoreductases.…”

Section: Specificity and Promiscuity Of Oxidoreductasesmentioning

confidence: 99%

“…This indicates that the two enzymes probably had a common ancestor from which they diverged to catalyze consecutive steps of the same metabolic pathway. Substrate promiscuity refers to the property of an enzyme of being able to catalyze the same reaction with a range of different but related substrates [55]. Some are very specific and have just one possible substrate, such as D-hydroxyisovalerate dehydrogenase from the depsipeptide-producing fungus Fusarium sambucinum [58].…”

Section: Specificity and Promiscuity Of Oxidoreductasesmentioning

confidence: 99%

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Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application

Vidal

Kelly

Mordaka

et al. 2018

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

248

147

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A B S T R A C T NAD(P)H-dependent oxidoreductases catalyze the reduction or oxidation of a substrate coupled to the oxidation or reduction, respectively, of a nicotinamide adenine dinucleotide cofactor NAD(P)H or NAD(P) + . NAD(P)Hdependent oxidoreductases catalyze a large variety of reactions and play a pivotal role in many central metabolic pathways. Due to the high activity, regiospecificity and stereospecificity with which they catalyze redox reactions, they have been used as key components in a wide range of applications, including substrate utilization, the synthesis of chemicals, biodegradation and detoxification. There is great interest in tailoring NAD(P)H-dependent oxidoreductases to make them more suitable for particular applications. Here, we review the main properties and classes of NAD(P)H-dependent oxidoreductases, the types of reactions they catalyze, some of the main protein engineering techniques used to modify their properties and some interesting examples of their modification and application.

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Section: Specificity and Promiscuity Of Oxidoreductasesmentioning

confidence: 99%

Section: Specificity and Promiscuity Of Oxidoreductasesmentioning

confidence: 99%

Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application

Vidal

Kelly

Mordaka

et al. 2018

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

248

147

View full text Add to dashboard Cite

show abstract

“…The catalytic promiscuity refers to enzymes belonging to a particular class in the enzyme classification (EC) system catalyzing reactions of the type which are generally catalyzed by another class of enzymes. Lipases, classified as hydrolases, have been shown to catalyze many C-C bond formation reactions [10,11,14,15]. It is believed that in such cases, substrates interact with the active site in a manner different from that observed by natural substrates [10].…”

Section: Introductionmentioning

confidence: 99%

Enhancement of stability of a lipase by subjecting to three phase partitioning (TPP): structures of native and TPP-treated lipase from Thermomyces lanuginosa

Kumar

Mukherjee

Sinha

et al. 2015

Sustain Chem Process

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Background:The lipase enzyme converts long chain acyltriglycerides into di-and monoglycerides, glycerol and fatty acids. The catalytic site in lipase is situated deep inside the molecule. It is connected through a tunnel to the surface of the molecule. In the unbound state under aqueous conditions, the tunnel remains closed. The tunnel can be opened when the enzyme is exposed to a lipid bilayer or a detergent or many hydrophobic/hydrophilic surfaces. Results:In the present study, the lipase was subjected to three-phase partitioning (TPP) which consisted of mixing in tert-butanol and ammonium sulphate to the solution of lipase in the aqueous buffer. The enzyme formed an interfacial precipitate between the tert-butanol rich and water rich phases. The stability of the enzyme subjected to TPP was found to be higher (T m of 80 °C) than the untreated enzyme (T m of 77 °C). The activity of the enzyme subjected to TPP (3.3 U/mg) was nearly half of that of the untreated one (5.8 U/mg). However, the activity of the treated enzyme was higher (17.8 U/mg) than the untreated one (8.6 U/mg) when a detergent was incorporated in the assay buffer. Conclusions:The structure determination showed that the substrate binding site in the treated enzyme was more tightly closed than that of the untreated protein.

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“…That still may be the best option but not necessarily the only option. Enzymes can catalyse reactions which are not expected according to their EC classification [46]. For example, recently we showed that a simple lipase can carry out Cannizaro reaction [47].…”

Section: Choosing/tailoring Biocatalystsmentioning

confidence: 99%

Biocatalysis for biomass valorization

Mukherjee

Gupta

2015

Sustain Chem Process

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Biocatalysis is a more sustainable alternative to chemical catalysis. While trying to obtain value added products from a biomass, looking beyond lignocelluloses (e.g.: marine polysaccharides, plant gums) may pay dividend. Many waste materials can be looked upon as a source of oil. Oil can be a rich source of diverse types of chemicals apart from biodiesel. Similarly, glycerol, the common by-product during biodiesel production, irrespective of the oil used, itself is the starting material of many products. Biocatalysis already is a viable option for the biodiesel formation step and may have a greater potential scope in glycerol chemistry. The ways to obtain the necessary biocatalysts and tailoring a given biocatalyst for a particular activity in the context of biomass valorization are discussed.

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Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology

Cited by 36 publications

References 87 publications

Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application

Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application

Enhancement of stability of a lipase by subjecting to three phase partitioning (TPP): structures of native and TPP-treated lipase from Thermomyces lanuginosa

Biocatalysis for biomass valorization

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