|Publication type:||Article in scientific journal|
|Type of review:||Peer review (publication)|
|Title:||Novel Old Yellow Enzyme subclasses|
|Publisher / Ed. Institution:||Wiley|
|Subjects:||Biocatalytic toolbox; Ene reductase; Enzyme sourcing; Novel Old Yellow Enzyme subclasses; Phylogenetic analysis|
|Subject (DDC):||660.6: Biotechnology|
|Abstract:||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 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 while 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.|
|Fulltext version:||Published version|
|License (according to publishing contract):||Licence according to publishing contract|
|Departement:||Life Sciences and Facility Management|
|Organisational Unit:||Institute of Chemistry and Biotechnology (ICBT)|
|Appears in collections:||Publikationen Life Sciences und Facility Management|
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