Cover Feature: Exploiting the Catalytic Diversity of Short‐Chain Dehydrogenases/Reductases: Versatile Enzymes from Plants with Extended Imine Substrate Scope (ChemBioChem 17/2018) | Zendy

Roth Sebastian | Zendy; Kilgore Matthew B. | Zendy; Kutchan Toni M. | Zendy; Müller Michael | Zendy

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Cover Feature: Exploiting the Catalytic Diversity of Short‐Chain Dehydrogenases/Reductases: Versatile Enzymes from Plants with Extended Imine Substrate Scope (ChemBioChem 17/2018)

Author(s) -

Roth Sebastian,

Kilgore Matthew B.,

Kutchan Toni M.,

Müller Michael

Publication year - 2018

Publication title -

chembiochem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.201800455

Subject(s) - reductase , chemistry , enzyme , substrate (aquarium) , imine , stereochemistry , combinatorial chemistry , dehydrogenase , cover (algebra) , biochemistry , catalysis , biology , engineering , ecology , mechanical engineering

The cover feature picture shows the plant Narcissus pseudonarcissus , which contains the enzyme noroxomaritidine reductase (NR). This member of the short‐chain dehydrogenase/reductase (SDR) family serves as an enone reductase in Amaryllidaceae alkaloid biosynthesis. We have found NR to be active with a set of typical imine substrates, thus demonstrating that SDRs are suitable for biocatalytic C=N reduction. Moreover, NR accepts keto substrates as well, thereby highlighting the enzyme family′s versatility. With NR as a template, we have identified a novel imine‐reducing SDR. More information can be found in the communication by M. Müller et al. on page 1849 in Issue 17, 2018 (DOI: 10.1002/cbic.201800291).

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