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Diversity in Reduction with Short‐Chain Dehydrogenases: Tetrahydroxynaphthalene Reductase, Trihydroxynaphthalene Reductase, and Glucose Dehydrogenase
Author(s) -
Conradt David,
Schätzle Michael A.,
Husain Syed Masood,
Müller Michael
Publication year - 2015
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201500605
Subject(s) - diastereomer , stereochemistry , dehydrogenase , enzyme , reductase , stereoselectivity , biosynthesis , chemistry , oxidoreductase , nad+ kinase , bacillus subtilis , alcohol dehydrogenase , biochemistry , biology , catalysis , genetics , bacteria
NAD(P)H‐dependent oxidoreductases from the short‐chain dehydrogenases/reductases (SDRs) family possess high functional diversity. Three SDRs, namely, tetrahydroxy‐ and trihydroxynaphthalene reductases (T 4 HNR, T 3 HNR) involved in the dihydroxynaphthalene‐melanin biosynthesis of the phytopathogenic fungus Magnaporthe grisea , and glucose dehydrogenase (GDH) from Bacillus subtilis , were characterized regarding their substrate range and functional behavior. T 4 HNR and T 3 HNR share activities towards the stereoselective reduction of 2‐tetralone derivatives and 2,3‐dihydro‐1,4‐naphthoquinones and show distinct but different stereochemical outcome in the case of epoxy‐1,4‐napthoquinones as substrates. GDH shares the activity towards 2,3‐dihydro‐1,4‐naphthoquinones, however, with low stereocontrol. Moreover, GDH reduces 2‐hydroxy‐2,3‐dihydro‐1,4‐naphthoquinone into trans ‐4‐hydroxyscytalone with a high diastereomeric excess (96 %), whereas T 4 HNR gave the cis diastereomer (diastereomeric excess>99 %). Thus, SDRs provide a much higher functional and stereochemical diversity than previously thought, already exemplified by many transformations of three members of this enzyme family.