Tetrahydroxynaphthalene reductase: catalytic properties of an enzyme involved in reductive asymmetric naphthol dearomatization.
In reduced circumstances: tetrahydroxynaphthalene reductase shows a broad substrate range including alternate phenolic compounds and cyclic ketones. Structural modeling reveals major enzyme-substrate interactions; C-terminal truncation of the enzyme causes an altered substrate preference, in accordance with stabilization of the substrate by the C-terminal carboxylate. This effect allows the identification of a homologous enzyme.
Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Germany.
Michael A
MA
Schätzle
Stephan
S
Flemming
Syed Masood
SM
Husain
Michael
M
Richter
Stefan
S
Günther
Michael
M
Müller
D055162:Biocatalysis; D020134:Catalytic Domain; D005656:Fungal Proteins / Q000378:metabolism*; D007659:Ketones / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D020082:Magnaporthe / Q000201:enzymology; D009284:Naphthols / Q000378:metabolism*; D010084:Oxidation-Reduction; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000378:metabolism*; D013379:Substrate Specificity
D005656:Fungal Proteins; D007659:Ketones; D009284:Naphthols; C086024:tetrahydroxynaphthalene reductase; D044925:Oxidoreductases Acting on CH-CH Group Donors