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Recombinant Δ 4,5 ‐Steroid 5 β‐Reductases as Biocatalysts for the Reduction of Activated CC‐Double Bonds in Monocyclic and Acyclic Molecules
Author(s) -
Burda Edyta,
Kraußer Marina,
Fischer Gabriele,
Hummel Werner,
MüllerUri Frieder,
Kreis Wolfgang,
Gröger Harald
Publication year - 2009
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.200900024
Subject(s) - chemistry , steroid , double bond , stereochemistry , enantioselective synthesis , substrate (aquarium) , cofactor , isophorone , molecule , enzyme , biocatalysis , combinatorial chemistry , organic chemistry , catalysis , reaction mechanism , biochemistry , oceanography , hormone , geology
It was found that Δ 4,5 ‐steroid 5β‐reductases are capable of reducing also small molecules bearing an activated CC double bond such as monocyclic enones and acyclic enoate esters. As preferred Δ 4,5 ‐steroid 5β‐reductase (5β‐StR) for this purpose, 5β‐StR from Arabidopsis thaliana was used. In part, enzyme activities are even higher than that for progesterone. Successful preliminary biotransformations with enzymatic in situ cofactor recycling were also carried out. When using the prochiral compound isophorone as a substrate, a high enantioselective reaction course (>99% ee ) was observed.