Two “classical” Old Yellow Enzymes from Chryseobacterium sp. CA49: Broad substrate specificity of Chr-OYE1 and limited activity of Chr-OYE2

Pei, Xiaokun; Xu, Mengyu; Wu, Zhong‐Liu

doi:10.1016/j.molcatb.2015.11.008

Cited by 13 publications

(8 citation statements)

References 42 publications

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“…; Pei et al . ). More recently, an OYE subfamily termed as ‘thermophilic‐like’, which contained fewer numbers of characterized OYEs, are identified (Wang et al .…”

Section: Resultsmentioning

confidence: 97%

The NADH:flavin oxidoreductase Nox fromRhodococcus erythropolisMI2 is the key enzyme of 4,4′-dithiodibutyric acid degradation

Khairy

Wübbeler

Steinbüchel

2016

Lett Appl Microbiol

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It was unequivocally demonstrated in this study that an NADH:flavin oxidoreductase from Rhodococcus erythropolis MI2 (Nox ) is able to cleave the xenobiotic disulphide 4,4'-dithiodibutyric acid (DTDB) into two molecules of 4-mercaptobutyric acid (4MB) with concomitant consumption of NADH. Nox showed a high substrate specificity as well as high heat stability. This study provides the first detailed characterization of the initial cleavage of DTDB, which is considered as a promising polythioester precursor.

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“…; Pei et al . ). More recently, an OYE subfamily termed as ‘thermophilic‐like’, which contained fewer numbers of characterized OYEs, are identified (Wang et al .…”

Section: Resultsmentioning

confidence: 97%

The NADH:flavin oxidoreductase Nox fromRhodococcus erythropolisMI2 is the key enzyme of 4,4′-dithiodibutyric acid degradation

Khairy

Wübbeler

Steinbüchel

2016

Lett Appl Microbiol

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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%

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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“…An argininea tt he Cterminus of class II OYEs assists in substrate binding of the adjacent monomer [15] leading to the formation of dimers, whereas the classical OYEs are found as monomers or dimers. [16] The classical OYE subgroup contains yeasts enzymes uch as OYE1 from Saccharomyces carlsbergensis, [7] as well as variants from proteobacteria (NCR, [17] MR, [18] PETNR [19] ), flavobacteria (Chr-OYE2 [20] )a nd plants (LeOPR1-3 [21] ). Recently,i tw as proposed to furthers ubdivide the classical OYEs into two groups: classicalO YEs from plants and bacteria andc lassical OYEs from fungal sources.…”

Section: Introductionmentioning

confidence: 99%

Novel Old Yellow Enzyme Subclasses

et al. 2019

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Many drug candidate molecules contain at least one chiral centre, and consequently, the development of biocatalytic strategies to complement existing metal‐ and organocatalytic approaches is of high interest. However, time is a critical factor in chemical process development, and thus, the introduction of biocatalytic steps, even if more suitable, is often prevented by the limited availability of off‐the‐shelf enzyme libraries. To expand the biocatalytic toolbox with additional ene reductases, we screened 19 bacterial strains for double bond reduction activity by using the model substrates cyclohexanone and carvone. Overall, we identified 47 genes coding for putative ene reductases. Remarkably, bioinformatic analysis of all genes and the biochemical characterization of four representative novel ene reductases led us to propose the existence of two new Old Yellow Enzyme subclasses, which we named OYE class III and class IV. Our results demonstrate that although, on a DNA level, each new OYE subclass features a distinct combination of sequence motifs previously known from the classical and the thermophilic‐like group, their substrate scope more closely resembles the latter subclass.

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Two “classical” Old Yellow Enzymes from Chryseobacterium sp. CA49: Broad substrate specificity of Chr-OYE1 and limited activity of Chr-OYE2

Cited by 13 publications

References 42 publications

The NADH:flavin oxidoreductase Nox fromRhodococcus erythropolisMI2 is the key enzyme of 4,4′-dithiodibutyric acid degradation

The NADH:flavin oxidoreductase Nox fromRhodococcus erythropolisMI2 is the key enzyme of 4,4′-dithiodibutyric acid degradation

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

Novel Old Yellow Enzyme Subclasses

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