Cytosolic aromatic aldehyde dehydrogenase provides benzoic acid for xanthone biosynthesis in Hypericum

Singh, Pratap; Kaufholdt, David; Awadalah, Mina; Hänsch, Robert; Beerhues, Ludger; Gaid, Mariam

doi:10.1016/j.plaphy.2021.01.011

Cited by 7 publications

(3 citation statements)

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“…Many ALDH enzymes are reported as being non-specific for substrate, demonstrating catalytic activity with a range of natural and synthetic aldehydes, including thermophilic members [ 16 , 22 , 38 , 39 , 40 , 52 , 70 , 71 ]. ALDH Tt could convert aliphatic and aromatic aldehydes, para -substituted benzaldehydes could be efficiently converted by ALDH Tt , while ortho -substituted benzaldehydes demonstrated no catalytic activity.…”

Section: Discussionmentioning

confidence: 99%

Study of ALDH from Thermus thermophilus—Expression, Purification and Characterisation of the Non-Substrate Specific, Thermophilic Enzyme Displaying Both Dehydrogenase and Esterase Activity

Shortall

Durack

Magner

et al. 2021

Cells

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Aldehyde dehydrogenases (ALDH), found in all kingdoms of life, form a superfamily of enzymes that primarily catalyse the oxidation of aldehydes to form carboxylic acid products, while utilising the cofactor NAD(P)+. Some superfamily members can also act as esterases using p-nitrophenyl esters as substrates. The ALDHTt from Thermus thermophilus was recombinantly expressed in E. coli and purified to obtain high yields (approximately 15–20 mg/L) and purity utilising an efficient heat treatment step coupled with IMAC and gel filtration chromatography. The use of the heat treatment step proved critical, in its absence decreased yield of 40% was observed. Characterisation of the thermophilic ALDHTt led to optimum enzymatic working conditions of 50 °C, and a pH of 8. ALDHTt possesses dual enzymatic activity, with the ability to act as a dehydrogenase and an esterase. ALDHTt possesses broad substrate specificity, displaying activity for a range of aldehydes, most notably hexanal and the synthetic dialdehyde, terephthalaldehyde. Interestingly, para-substituted benzaldehydes could be processed efficiently, but ortho-substitution resulted in no catalytic activity. Similarly, ALDHTt displayed activity for two different esterase substrates, p-nitrophenyl acetate and p-nitrophenyl butyrate, but with activities of 22.9 and 8.9%, respectively, compared to the activity towards hexanal.

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Section: Discussionmentioning

confidence: 99%

Study of ALDH from Thermus thermophilus—Expression, Purification and Characterisation of the Non-Substrate Specific, Thermophilic Enzyme Displaying Both Dehydrogenase and Esterase Activity

Shortall

Durack

Magner

et al. 2021

Cells

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“…The cinnamoyl-CoA intermediate is then synthesized to benzoyl-CoA which requires three more enzymatic reaction steps involving cinnamoyl-CoA hydratase/lyase (CHL), benzaldehyde dehydrogenase (BD) and benzoate-CoA ligase (BZL; Abd El-Mawla and Beerhues, 2002;Singh et al, 2020). Although the three proteins have been proven to exist and functioning at the biochemical level from various species (Abd El-Mawla and Beerhues, 2002;Beuerle and Pichersky, 2002;Gaid et al, 2009Gaid et al, , 2019Saini et al, 2017Saini et al, , 2020, only BD and BZL have been verified at the molecular level (coding sequence isolation followed by in vitro heterologous expression and enzymatic assays) in H. calycinum (Singh et al, 2020(Singh et al, , 2021 and in snapdragon (Antirrhinum majus; BD only; Long et al, 2009). The latter BZL gene, also known as HcAAE1 (acyl-activating enzyme 1), has been shown to increase its expression prior to xanthone accumulation post-elicitation, suggesting its role upstream of the xanthone pathway (Singh et al, 2020).…”

Section: Biosynthesis Of Xanthone Core Structures In Plantsmentioning

confidence: 99%

Xanthone Biosynthetic Pathway in Plants: A Review

2022

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Xanthones are secondary metabolites rich in structural diversity and possess a broad array of pharmacological properties, such as antitumor, antidiabetic, and anti-microbes. These aromatic compounds are found in higher plants, such as Clusiaceae, Hypericaceae, and Gentianaceae, yet their biosynthetic pathways have not been comprehensively updated especially within the last decade (up to 2021). In this review, plant xanthone biosynthesis is detailed to illuminate their intricacies and differences between species. The pathway initially involves the shikimate pathway, either through L-phenylalanine-dependent or -independent pathway, that later forms an intermediate benzophenone, 2,3′,4,6-tetrahydoxybenzophenone. This is followed by a regioselective intramolecular mediated oxidative coupling to form xanthone ring compounds, 1,3,5-trihydroxyxanthone (1,3,5-THX) or 1,3,7-THX, the core precursors for xanthones in most plants. Recent evidence has shed some lights onto the enzymes and reactions involved in this xanthone pathway. In particular, several biosynthetic enzymes have been characterized at both biochemical and molecular levels from various organisms including Hypericum spp., Centaurium erythraea and Garcinia mangostana. Proposed pathways for a plethora of other downstream xanthone derivatives including swertianolin and gambogic acid (derived from 1,3,5-THX) as well as gentisin, hyperixanthone A, α-mangostin, and mangiferin (derived from 1,3,7-THX) have also been thoroughly covered. This review reports one of the most complete xanthone pathways in plants. In the future, the information collected here will be a valuable resource for a more directed molecular works in xanthone-producing plants as well as in synthetic biology application.

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“…Recent scientific investigations have been devoted to unraveling the intricate biochemistry of enzymes in photosynthetic organisms, elucidating their catalytic mechanisms, regulatory processes, and evolutionary trajectories. For instance, recent researches have elucidated dynamic diversifying mechanisms underlying the synthesis of phenolic acid in Salvia miltiorrhiza (Zhou et al, 2021), alkaloids in Catharanthus roseus (Eng et al, 2022), triterpenes in Eriobotrya japonica (Su et al, 2021), and xanthones in Hypericum species (Singh et al, 2020;Singh et al, 2021). These studies have yielded valuable insights into the biosynthetic pathways of pivotal compounds in non-model plants.…”

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confidence: 99%

Editorial: Advances in metabolism and chemodiversity - focus - plant enzymes

Liu

et al. 2023

Front. Plant Sci.

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Editorial on the Research TopicAdvances in metabolism and chemodiversityfocusplant enzymes Plant enzymes are indispensable for plant metabolism and are critical determinants of the extensive chemodiversity observed in plants. These enzymes serve as primary catalysts in biosynthetic pathways, enabling the biosynthesis of a diverse range of secondary metabolites, such as alkaloids, terpenes, and phenolics. These metabolites are essential for the distinctive sensory qualities of plants, e.g., flavors, scents, and colors, and they also possess significant biological activities with promising applications in agriculture, medicine, and industry. Recent scientific investigations have been devoted to unraveling the intricate biochemistry of enzymes in photosynthetic organisms, elucidating their catalytic mechanisms, regulatory processes, and evolutionary trajectories. For instance, recent researches have elucidated dynamic diversifying mechanisms underlying the synthesis of phenolic acid in Salvia miltiorrhiza (Zhou et al., 2021), alkaloids in Catharanthus roseus (Eng et al., 2022), triterpenes in Eriobotrya japonica (Su et al., 2021), and xanthones in Hypericum species (Singh et al., 2020;Singh et al., 2021). These studies have yielded valuable insights into the biosynthetic pathways of pivotal compounds in non-model plants. By augmenting the understanding of plant enzyme biochemistry, scientists can harness their immense potential for advancing sustainable agriculture, facilitating drug discovery, and fostering the development of plant-based products, thereby endrosing positive impacts on human health and the environment.This Research Topic includes six original research articles, with a special focus on the function of plant enzymes. Zhang et al. reported that Prunus mume cinnamyl alcohol dehydrogenase 1 and 2 (PmCAD1 and 2) are the major contributors to the cinnamyl alcohol biosynthesis and emission, which was identified after analysing the endogenous volatile compounds and the transcriptomes gleaned from six P. mume cultivars (Figure 1A). Another research on floral fragrant components in Rosa rugosa revealed 156 differential volatile organic compounds, from two metabolic pathways: the monoterpenoid biosynthetic pathway and the amino acid (phenylalanine, tyrosine, and Frontiers in Plant Science frontiersin.org 01

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Cytosolic aromatic aldehyde dehydrogenase provides benzoic acid for xanthone biosynthesis in Hypericum

Cited by 7 publications

References 58 publications

Study of ALDH from Thermus thermophilus—Expression, Purification and Characterisation of the Non-Substrate Specific, Thermophilic Enzyme Displaying Both Dehydrogenase and Esterase Activity

Study of ALDH from Thermus thermophilus—Expression, Purification and Characterisation of the Non-Substrate Specific, Thermophilic Enzyme Displaying Both Dehydrogenase and Esterase Activity

Xanthone Biosynthetic Pathway in Plants: A Review

Editorial: Advances in metabolism and chemodiversity - focus - plant enzymes

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