Origin and evolution of medium chain alcohol dehydrogenases

Jörnvall, Hans; Hedlund, Joel; Bergman, Tomas; Kallberg, Yvonne; Cederlund, Ella; Persson, Bengt

doi:10.1016/j.cbi.2012.11.008

Cited by 34 publications

(25 citation statements)

References 37 publications

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“…Among these, two proteins were identified as a cell division protein, electron transport flavoprotein and three hypothetical proteins all showing similarity with the respective representative proteins from Actinomycetales group of bacteria. The description and NCBI accession numbers of identified proteins with score and coverage information obtained biodegradation of 4-NP has not been reported (Jörnvall et al, 2013). In this context, the involvement of ADH in 4-NP degradation is novel with respect to 4-NP degradation by bacteria.…”

Section: In Gel Digestion and Mass Spectrometry Analysismentioning

confidence: 99%

Biodegradation of 4-nitrophenol by a Rhodococcus species and a preliminary insight into its toxicoproteome based on mass spectrometry analysis

Sengupta¹,

Alam²,

Pailan³

et al. 2019

JEB

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The objective of this study was to understand the possible fate of 4-NP through the molecular mechanism and to identify potential enzymes involved in 4-NP biodegradation by Rhodococcus sp. strain BUPNP1. Biodegradation of 4-NP was detected spectrophotometrically at 400 nm and also confirmed by TLC and HPLC. Comparative study of proteomes was performed by 2-D gel electrophoresis followed by peptide mass fingerprinting and bioinformatic analysis to identify and/ or predict the possible functions of over-expressed proteins in 4-NP treated cells of BUNP1. Utilization of 4nitrophenol and its hydrolysis intermediate 4-nitrocatechol (4-NC) and 1,2,4-Benzenetriol as sole carbon source indicated the presence of genomic information encoding the enzyme necessary for the operation of 4-nitrophenol degradation pathway in the strain BUPNP1. It could transform 4-NP into 4-NC by monooxygenase whose major activity was detected during initial stage of degradation. The 4-NC further depleted in the medium to release nitrite ions. In order to investigate the molecular changes occurring d u r i n g d e g r a d a t i o n , a comparative study of proteome profiles was carried out where; 4nitrophenol treated cells were compared against cells grown on glucose as control. The comparative study indicated expression of several protein spots under 4-nitrophenol treated condition. This study showed the potential of BUPNP1 strain belonging to genus Rhodococcus towards induced expression of some unique proteins which might have possible role in 4-NP biodegradation process.

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Section: In Gel Digestion and Mass Spectrometry Analysismentioning

confidence: 99%

Biodegradation of 4-nitrophenol by a Rhodococcus species and a preliminary insight into its toxicoproteome based on mass spectrometry analysis

Sengupta¹,

Alam²,

Pailan³

et al. 2019

JEB

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“…ADH activity was reported for the rst time from the grains and anthers of the maize [2], and the expression and activity of this gene were widespread in the "normal" state or under various pressures. The ADH gene family is actually a relatively large family, which is mainly divided into several major superfamilies, namely, short-chain dehydrogenases/reductases (SDR)-ADH (containing about 250 amino acid residues), medium-chain dehydrogenases/reductases (MDR)-ADH (containing about 350 amino acid residues) and long-chain dehydrogenases/reductases (LDR)-ADH gene superfamily (about 385-900 amino acid residues) [3,4]. The ADHs of mammals, plants and yeast belongs to MDRs, whose active sites usually contain zinc ligands.…”

Section: Introductionmentioning

confidence: 99%

Alcohol dehydrogenase (ADH) genes family in wheat (Triticum aestivum): Genome-wide identification, characterization, phylogenetic relationship and expression patterns

Shen

Yuan

2020

Preprint

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Background Alcohol dehydrogenase (ADH) plays important roles in plant survival under anaerobic conditions. Although some research has been carried out the functions of ADH in other plants, that of wheat TaADH family genes in response to abiotic stress are unclear. Results A total of 22 ADH genes were obtained from 14 chromosomes of the wheat genome by systematic screening. Multiple sequence alignment and evolutionary relationship show that these genes contain the characteristics of GroES-like domain and Zinc-binding domain, and these belong to Medium-chain -ADH type and can be divided into three subfamilies. There are 17 pairs of fragment replication genes among TaADH family members in the wheat genome, while there are 9 pairs of collinear gene pairs from ADH family members between wheat and rice genome. We speculate that these fragment repetition events may be the main reason for the amplification of TaADH family genes. Ka/Ks analysis indicated that there were 64 repetitive gene pairs, and the Ka/Ks value of these gene pairs was less than 1, which indicated that these sequences of TaADH gene were relatively conservative and did not change greatly in the process of evolution. Promoter element analysis showed that almost all of the upstream promoters of these genes contained the responsive anaerobic inducible element. Tissue localized expression and expression patterns also demonstrated that the TaADH genes responded to abiotic stress and may play an important role in waterlogging stress during the seed germination stage. Conclusions The results of this study may be helpful to further study the function of TaADH genes and determine the candidate gene for wheat stress resistance breeding.

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“…ADHs catalyzes the interconversion of primary and secondary alcohols to aldehydes and ketones, respectively. ADHs are currently divided into three classes based on the protein's monomer chain length: medium‐chain dehydrogenases/reductases (MDR), short‐chain dehydrogenases/reductases (SDR) and long‐chain dehydrogenases/reductases (LDR). ADHs from the MDR superfamily of enzymes, which include horse‐liver alcohol dehydrogenase from Equus caballus (HLADH) and yeast ADHs (YADH) from Saccharomyces cerevisiae ( Sc ADH1), predominantly contain Zn 2+ within the active site.…”

Section: Introductionmentioning

confidence: 99%

An Alcohol Dehydrogenase from the Short‐Chain Dehydrogenase/Reductase Family of Enzymes for the Lactonization of Hexane‐1,6‐diol

et al. 2018

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Biocatalytic production of lactones, and in particular ϵ‐caprolactone (CL), have gained increasing interest as a greener route to polymer building blocks, especially through the use of Baeyer–Villiger monooxygenases (BVMOs). Despite several advances in the field, BVMOs, however, still suffer several practical limitations. Alcohol dehydrogenase (ADH)‐mediated lactonization of diols in turn has received far less attention and very few enzymes have been identified for the conversion of diols to lactones, with horse‐liver ADH (HLADH) remaining the catalyst of choice. Screening of a diverse panel of ADHs, AaSDR‐1, a member of the short‐chain dehydrogenase/reductase family, was found to produce ϵ‐caprolactone from hexane‐1,6‐diol. Moreover, cofactor regeneration by an NADH oxidase eliminated the requirement of co‐substrates, yielding water as the sole by‐product. Despite lower turnover frequencies as compared to HLADH, higher selectivity was found for the production of CL, with HLADH forming significant amounts of 6‐hydroxyhexanoic acid and adipic acid through aldehyde dehydrogenation/oxidation of the gem‐diol intermediates. Also, CL yield were shown to be dependent on buffer choice, as structural elucidation of a Tris adduct confirmed the buffer amine to react with aliphatic aldehydes forming a Schiff‐base intermediate which through further ADH oxidation, forms a tricyclic acetal product.

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Origin and evolution of medium chain alcohol dehydrogenases

Cited by 34 publications

References 37 publications

Biodegradation of 4-nitrophenol by a Rhodococcus species and a preliminary insight into its toxicoproteome based on mass spectrometry analysis

Biodegradation of 4-nitrophenol by a Rhodococcus species and a preliminary insight into its toxicoproteome based on mass spectrometry analysis

Alcohol dehydrogenase (ADH) genes family in wheat (Triticum aestivum): Genome-wide identification, characterization, phylogenetic relationship and expression patterns

An Alcohol Dehydrogenase from the Short‐Chain Dehydrogenase/Reductase Family of Enzymes for the Lactonization of Hexane‐1,6‐diol

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