Heterologous expression and characterization of the ene-reductases from Deinococcus radiodurans and Ralstonia metallidurans

Litthauer, Suzanne; Gargiulo, Serena; Heerden, Esta van; Hollmann, Frank; Opperman, Diederik J.

doi:10.1016/j.molcatb.2013.10.020

Cited by 28 publications

(35 citation statements)

References 52 publications

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“…However, characterized members of the "thermophilic-like" subfamily are evidently much fewer although they are not restricted to thermophilic origins. To the best of our knowledge, TOYE, CrS and GkOYE are the only three thermophilic counterparts that has been characterized [20,21,38], while other "thermophilic-like" OYEs are from mesophilic organism with moderate temperature optima [3,39], same as Chr-OYE3 in the present study. The enzyme shares the conserved residues involved in catalytic activity, FMN binding, substrate binding and subunits interaction within this subfamily.…”

Section: Discussionmentioning

confidence: 52%

Identification and characterization of a novel “thermophilic-like” Old Yellow Enzyme from the genome of Chryseobacterium sp. CA49

Pei

2014

Journal of Molecular Catalysis B: Enzymatic

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Section: Discussionmentioning

confidence: 52%

Identification and characterization of a novel “thermophilic-like” Old Yellow Enzyme from the genome of Chryseobacterium sp. CA49

Pei

2014

Journal of Molecular Catalysis B: Enzymatic

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“…Deinococcus radiodurans strain R1 (ATCC 13939) and Deinococcus geothermalis strain DSM 11300 were cultured according to methods reported previously (46)(47)(48) Total RNA extraction. Whole RNA was extracted as previously reported, with minor changes (50).…”

Section: Methodsmentioning

confidence: 99%

Transcriptional Analysis of Deinococcus radiodurans Reveals Novel Small RNAs That Are Differentially Expressed under Ionizing Radiation

Tsai

Liao

Chou

et al. 2015

Appl Environ Microbiol

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bSmall noncoding RNAs (sRNAs) are posttranscriptional regulators that have been identified in multiple species and shown to play essential roles in responsive mechanisms to environmental stresses. The natural ability of specific bacteria to resist high levels of radiation has been of high interest to mechanistic studies of DNA repair and biomolecular protection. Deinococcus radiodurans is a model extremophile for radiation studies that can survive doses of ionizing radiation of >12,000 Gy, 3,000 times higher than for most vertebrates. Few studies have investigated posttranscriptional regulatory mechanisms of this organism that could be relevant in its general gene regulatory patterns. In this study, we identified 199 potential sRNA candidates in D. radiodurans by whole-transcriptome deep sequencing analysis and confirmed the expression of 41 sRNAs by Northern blotting and reverse transcriptase PCR (RT-PCR). A total of 8 confirmed sRNAs showed differential expression during recovery after acute ionizing radiation (15 kGy). We have also found and confirmed 7 sRNAs in Deinococcus geothermalis, a closely related radioresistant species. The identification of several novel sRNAs in Deinococcus bacteria raises important questions about the evolution and nature of global gene regulation in radioresistance.

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“…Nevertheless, the enzymes AtOPR1-AtOPR3 from Arabidopsis thaliana [65,66], and LeOPR1-LeOPR3 from Solanum lycopersicum (tomato) [67,68], were characterised according to their structure, function and physiological role. Two thirds of the characterised OYEs have been obtained from various classes of bacteria including proteobacteria (28%) [69,70], actinobacteria (5%) [22,71,72], bacteroidetes (5%) [73,74], firmicutes (10%) [75][76][77], deinococcus-thermus (3%) [78][79][80], and cyanobacteria (17%) [21,81].…”

Section: Phylogenetic Classification Of Oyesmentioning

confidence: 99%

“…For β-methyl unsaturated substrates, class III enzymes afforded no conversion, whereas the average conversion of class II enzymes is slightly higher (30%) than that of class I enzymes (20%). [44], NemR [44], MR [44], NCR [42], EBP1 [44], OYE1 [42], OYE2 [42], OYE3 [42], RmER [80], DrER [80], TOYE [77], TsOYE [52], OYERo2 [22], FOYE-1 (unpublished data) and YqjM [12,18]. [44], NemR [44], MR [44], LeOPR1 [12,18], NCR [42], EBP1 [44], OYE1 [42], OYE2 [42], OYE3 [42], RmER [80], DrER [80], FOYE-1 (unpublished data) and YqjM [12,18].…”

Section: Classification Of Oyes With Respect To Substratesmentioning

confidence: 99%

Old Yellow Enzyme-Catalysed Asymmetric Hydrogenation: Linking Family Roots with Improved Catalysis

et al. 2017

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Asymmetric hydrogenation of activated alkenes catalysed by ene-reductases from the old yellow enzyme family (OYEs) leading to chiral products is of potential interest for industrial processes. OYEs' dependency on the pyridine nucleotide coenzyme can be circumvented through established artificial hydride donors such as nicotinamide coenzyme biomimetics (NCBs). Several OYEs were found to exhibit higher reduction rates with NCBs. In this review, we describe a new classification of OYEs into three main classes by phylogenetic and structural analysis of characterized OYEs. The family roots are linked with their use as chiral catalysts and their mode of action with NCBs. The link between bioinformatics (sequence analysis), biochemistry (structure-function analysis), and biocatalysis (conversion, enantioselectivity and kinetics) can enable an early classification of a putative ene-reductase and therefore the indication of the binding mode of various activated alkenes.

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Heterologous expression and characterization of the ene-reductases from Deinococcus radiodurans and Ralstonia metallidurans

Cited by 28 publications

References 52 publications

Identification and characterization of a novel “thermophilic-like” Old Yellow Enzyme from the genome of Chryseobacterium sp. CA49

Identification and characterization of a novel “thermophilic-like” Old Yellow Enzyme from the genome of Chryseobacterium sp. CA49

Transcriptional Analysis of Deinococcus radiodurans Reveals Novel Small RNAs That Are Differentially Expressed under Ionizing Radiation

Old Yellow Enzyme-Catalysed Asymmetric Hydrogenation: Linking Family Roots with Improved Catalysis

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