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Isolation of a novel NADPH‐dependent reductase which coacts with chalcone synthase in the biosynthesis of 6′‐deoxychalcone
Author(s) -
Welle Roland,
Grisebach Hans
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80318-1
Subject(s) - reductase , chalcone synthase , enzyme , biochemistry , biosynthesis , chalcone , chemistry , atp synthase , affinity chromatography , stereochemistry
Enzyme synthesis of 6′‐deoxychalcone from 4‐coumaroyl‐CoA and malonyl‐CoA has been achieved, using purified soybean chalcone synthase (CHS), NADPH and a further protein (reductase). This reductase was purified to apparent homogeneity by a procedure including affinity chromatography on Blue Sepharose and elution with NADP + . This enzyme has a molecular mass of about 34 kDa and consists of a single polypeptide. Synthesis of deoxychalcone also occurred with parsley CHS, NADPH and the soybean reductase. The reductase catalyzed transfer of the pro‐ R hydrogen of [4‐ 3 H]NADPH to the substrate.