YMR152W from Saccharomyces cerevisiae encoding a novel aldehyde reductase for detoxification of aldehydes derived from lignocellulosic biomass

Ouyang, Yidan; Li, Qian; Kuang, Xiaolin; Wang, Hanyu; Wu, Jinjian; Ayepa, Ellen; Chen, Huan; Abrha, Getachew Tafere; Zhang, Zhengyue; Li, Xi; Ma, Menggen

doi:10.1016/j.jbiosc.2020.09.004

Cited by 11 publications

(4 citation statements)

References 41 publications

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“…ALDH enzymes are diverse in their function across all kingdoms of life, contributing to detoxification Esterbauer et al (1991), Kelson et al (1997), Choudhary et al (2005), Ho and Weiner (2005), Rodríguez-Zavala et al (2006), Marchitti et al (2007), Shin et al (2009), Jackson et al (2011), Ouyang et al (2020, biosynthesis Yoshida et al (1992), Mellema et al (2002), Kim et al (2015), Pequerul et al (2020), and non-enzymatic functions such as anti-oxidant Estey et al (2007), Lassen et al (2008), Marchitti et al (2011, Voulgaridou et al (2020), structural Piatigorsky (1998), Voulgaridou et al (2017) and regulatory mechanisms Moreb (2008), Vassalli (2019), Voulgaridou et al (2020) (Table 1). Proper function of these enzymes is essential for maintenance of cell function and survival, with prominent ALDH-linked diseases arising from mutation, catalytic knockout and structural disruption.…”

Section: Structural Perspective Of Aldehyde Dehydrogenase Related Diseasesmentioning

confidence: 99%

Insights into Aldehyde Dehydrogenase Enzymes: A Structural Perspective

Shortall

Djeghader

Magner

et al. 2021

Front. Mol. Biosci.

117

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Aldehyde dehydrogenases engage in many cellular functions, however their dysfunction resulting in accumulation of their substrates can be cytotoxic. ALDHs are responsible for the NAD(P)-dependent oxidation of aldehydes to carboxylic acids, participating in detoxification, biosynthesis, antioxidant and regulatory functions. Severe diseases, including alcohol intolerance, cancer, cardiovascular and neurological diseases, were linked to dysfunctional ALDH enzymes, relating back to key enzyme structure. An in-depth understanding of the ALDH structure-function relationship and mechanism of action is key to the understanding of associated diseases. Principal structural features 1) cofactor binding domain, 2) active site and 3) oligomerization mechanism proved critical in maintaining ALDH normal activity. Emerging research based on the combination of structural, functional and biophysical studies of bacterial and eukaryotic ALDHs contributed to the appreciation of diversity within the superfamily. Herewith, we discuss these studies and provide our interpretation for a global understanding of ALDH structure and its purpose–including correct function and role in disease. Our analysis provides a synopsis of a common structure-function relationship to bridge the gap between the highly studied human ALDHs and lesser so prokaryotic models.

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Section: Structural Perspective Of Aldehyde Dehydrogenase Related Diseasesmentioning

confidence: 99%

Insights into Aldehyde Dehydrogenase Enzymes: A Structural Perspective

Shortall

Djeghader

Magner

et al. 2021

Front. Mol. Biosci.

117

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“…ALDHs are often not substrate specific, and can oxidise a wide range of aliphatic and aromatic, endogenous and exogenous aldehydes [ 16 , 17 , 18 ], which might be related to their broad spectrum of associated biological functions [ 5 ]. The primary function of ALDHs is their role in detoxification mechanisms [ 19 , 20 , 21 ], while other functions include biosynthesis [ 22 , 23 ] and non-enzymatic roles, such as antioxidant [ 24 , 25 ], structural [ 26 ], and regulatory function [ 27 , 28 ].…”

Section: Introductionmentioning

confidence: 99%

“…While ALDHs have been well-characterised in humans, emerging research places a primary focus on their prokaryotic counterpart’s structure and function, which has been less explored until recently [ 29 , 30 , 31 ]. The scope of prokaryotic ALDH function spans much wider than eukaryotes [ 5 , 19 , 31 , 32 ]. For example, the E. coli enzymes phenylacetaldehyde dehydrogenase and lactaldehyde dehydrogenase were characterised after the ALDH1, 2, and 3 from humans [ 1 , 2 , 33 ], and are involved in the specific metabolic pathways of phenylalanine and fucose respectively.…”

Section: Introductionmentioning

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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“…2 ). Furthermore, overexpression of YPR015C led to a much better specific activity (9.5 U/mg) when compared to other earlier reports on aldehyde reductases, such as in the overexpression of Yll056cwp (0.47 U/mg), Ykl071wp (3.38 U/mg), Ykl107wp (2.56 U/mg), and Ymr152wp (5.05 U/mg) from S. cerevisiae for furfural reduction ( Wang et al 2017a ; Wang et al 2017b ; Ouyang et al 2021 ).…”

Section: Resultsmentioning

confidence: 52%

Contribution of YPRO15C Overexpression to the Resistance of Saccharomyces cerevisiae BY4742 Strain to Furfural Inhibitor

Abrha

Kuang

et al. 2023

Polish Journal of Microbiology

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Lignocellulosic biomass is still considered a feasible source of bioethanol production. Saccharomyces cerevisiae can adapt to detoxify lignocellulose-derived inhibitors, including furfural. Tolerance of strain performance has been measured by the extent of the lag phase for cell proliferation following the furfural inhibitor challenge. The purpose of this work was to obtain a tolerant yeast strain against furfural through overexpression of YPR015C using the in vivo homologous recombination method. The physiological observation of the overexpressing yeast strain showed that it was more resistant to furfural than its parental strain. Fluorescence microscopy revealed improved enzyme reductase activity and accumulation of oxygen reactive species due to the harmful effects of furfural inhibitor in contrast to its parental strain. Comparative transcriptomic analysis revealed 79 genes potentially involved in amino acid biosynthesis, oxidative stress, cell wall response, heat shock protein, and mitochondrial-associated protein for the YPR015C overexpressing strain associated with stress responses to furfural at the late stage of lag phase growth. Both up- and down-regulated genes involved in diversified functional categories were accountable for tolerance in yeast to survive and adapt to the furfural stress in a time course study during the lag phase growth. This study enlarges our perceptions comprehensively about the physiological and molecular mechanisms implicated in the YPR015C overexpressing strain’s tolerance under furfural stress. Construction illustration of the recombinant plasmid. a) pUG6-TEF1p-YPR015C, b) integration diagram of the recombinant plasmid pUG6-TEF1p-YPR into the chromosomal DNA of Saccharomyces cerevisiae.

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YMR152W from Saccharomyces cerevisiae encoding a novel aldehyde reductase for detoxification of aldehydes derived from lignocellulosic biomass

Cited by 11 publications

References 41 publications

Insights into Aldehyde Dehydrogenase Enzymes: A Structural Perspective

Insights into Aldehyde Dehydrogenase Enzymes: A Structural Perspective

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

Contribution of YPRO15C Overexpression to the Resistance of Saccharomyces cerevisiae BY4742 Strain to Furfural Inhibitor

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