Screening for hydroxynitrile lyase activity in non-commercialised plants

Kassim, Muhammad Arshad; Sooklal, Selisha A.; Archer, Robert H.; Rumbold, Karl

doi:10.1016/j.sajb.2014.03.004

Cited by 11 publications

(8 citation statements)

References 20 publications

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“…Limitations of currently known HNLs are low activity 11 , low stability 12 , low expression levels 6 , or low flexibility in the choice of the expression host 13 . Approximately 3,000 plant species utilize cyanogenic defense, and HNL activity has been shown in a wide variety of families 14 15 16 17 , but only few amino acid sequences of confirmed HNLs are found in common gene and protein databases. However, knowledge of an enzyme’s amino acid sequence is essential for its recombinant expression and engineering.…”

mentioning

confidence: 99%

Enzyme discovery beyond homology: a unique hydroxynitrile lyase in the Bet v1 superfamily

Lanfranchi

Pavkov‐Keller

Koehler

et al. 2017

Sci Rep

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Homology and similarity based approaches are most widely used for the identification of new enzymes for biocatalysis. However, they are not suitable to find truly novel scaffolds with a desired function and this averts options and diversity. Hydroxynitrile lyases (HNLs) are an example of non-homologous isofunctional enzymes for the synthesis of chiral cyanohydrins. Due to their convergent evolution, finding new representatives is challenging. Here we show the discovery of unique HNL enzymes from the fern Davallia tyermannii by coalescence of transcriptomics, proteomics and enzymatic screening. It is the first protein with a Bet v1-like protein fold exhibiting HNL activity, and has a new catalytic center, as shown by protein crystallography. Biochemical properties of D. tyermannii HNLs open perspectives for the development of a complementary class of biocatalysts for the stereoselective synthesis of cyanohydrins. This work shows that systematic integration of -omics data facilitates discovery of enzymes with unpredictable sequences and helps to extend our knowledge about enzyme diversity.

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mentioning

confidence: 99%

Enzyme discovery beyond homology: a unique hydroxynitrile lyase in the Bet v1 superfamily

Lanfranchi

Pavkov‐Keller

Koehler

et al. 2017

Sci Rep

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“…screened for plant HNLs on the basis of plant families. They observed HNL activity in Adenia sp., Adenia firingalavensis , Adenia fruticose , and Adenia pechuelii , all four belonging to the Passifloraceae family …”

Section: Different Approaches To Discovering Hnlsmentioning

confidence: 99%

Modern Approaches to Discovering New Hydroxynitrile Lyases for Biocatalysis

Padhi

2016

ChemBioChem

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Hydroxynitrile lyases (HNLs) have grown in importance from laboratory to industry due to their potential to catalyze stereoselective C-C bond-formation reactions in the synthesis of several chiral intermediates, such as enantiopure α-cyanohydrins, β-nitro alcohols, and their derivatives with multiple functional groups. With these wide applications, the demand for finding new HNLs has increased, and this has led to exploration not only of new HNLs but also of new ways to discover them. An exclusive review article on HNLs by Asano et al. in 2011 described the discovery of HNLs along with their applications. Since then many scientific advancements have been seen in this area. This article aims to highlight the modern HNL discovery approaches, based mainly on 1) genome mining, 2) use of INTMSAlign software, 3) rational design (based on a millipede HNL), 4) evolution of catalytic mechanisms, 5) protein engineering guided by catalytic mechanisms, and 6) screening of plants with cyanogen glycoside (CG) content. This description is followed by future prospects. Overall this review represents the present state and the future potential of HNL discovery approaches, and so might be hoped to be instrumental not only in exploration of new HNLs but also in the invention of methods for potential biotechnological applications.

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“…Hydroxynitrile lyases catalyse the conversion of cyanohydrins to hydrogen cyanide, aldehydes, or ketones. (Kassim & Rumbold, 2014;Dadashipour & Asano, 2011;Sharma et al ., 2005). Plants, arthopods, and bacteria all have HNLs (Hussain et al ., 2012;Wiedner et al ., 2014;Dadashipour et al ., 2015).…”

Section: Introductionmentioning

confidence: 99%

A Comprehensive Overview of Novel Hydroxynitrile Lyases

Kumari

Chauhan

Arya

et al. 2021

Preprint

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Hydroxynitrile lyases (HNLs) are a heterogeneous family of enzymes that are of particular interest because of their structurally unique categories, a wide range of immobilisation techniques and procedures, and a wide range of sources with varying degrees of enantiopurity and enantioselectivity. Cupin, which contains a new type of HNL from bacteria, the lipocalin superfamily, which has HNLs from millipedes, and the + barrel fold superfamily, which contains HNL from a fern, have all been discovered in recent decades. Their biochemistry has been deciphered, and engineering efforts have been made to boost their productivity, purity, and activity. These remarkable enzymes opened up a new vista in the field of industrial catalysts since they are actively used in the synthesis of crucially important agrochemicals, medicines, physiologically active substances, and chemo-enzymatic follow-up procedures. This review focuses on recent advances, evolutionary history, and recombinant engineering of HNL from the previous decade.

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Screening for hydroxynitrile lyase activity in non-commercialised plants

Cited by 11 publications

References 20 publications

Enzyme discovery beyond homology: a unique hydroxynitrile lyase in the Bet v1 superfamily

Enzyme discovery beyond homology: a unique hydroxynitrile lyase in the Bet v1 superfamily

Modern Approaches to Discovering New Hydroxynitrile Lyases for Biocatalysis

A Comprehensive Overview of Novel Hydroxynitrile Lyases

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