Preparation of optically active N-benzyl-3-hydroxypyrrolidine by enzymatic hydroxylation

Hydroxylation of N-benzylpyrrolidine 2 with Pseudomonas oleovorans GPo1 afforded 62% of ( R)- N-benzyl-3-hydroxypyrrolidine 3 in 52% e.e. This reaction was catalyzed by the alkane hydroxylase system in this strain, which was demonstrated by hydroxylation of 2 with Escherichia coli GEc137 (pGEc47), a...

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Published in:Tetrahedron: asymmetry 1999-04, Vol.10 (7), p.1323-1333
Main Authors: Li, Zhi, Feiten, Hans-Jürgen, van Beilen, Jan B, Duetz, Wouter, Witholt, Bernard
Format: Article
Language:English
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Summary:Hydroxylation of N-benzylpyrrolidine 2 with Pseudomonas oleovorans GPo1 afforded 62% of ( R)- N-benzyl-3-hydroxypyrrolidine 3 in 52% e.e. This reaction was catalyzed by the alkane hydroxylase system in this strain, which was demonstrated by hydroxylation of 2 with Escherichia coli GEc137 (pGEc47), a recombinant strain that carries the genes for the alkane hydroxylase system of P. oleovorans GPo1. In a set of 70 alkane-degrading microorganisms, 12 were found to catalyze the biotransformation of 2 into 3 by screening with a microtiter plate technique. Hydroxylation of 2 with isolates HXN-1100 and HXN-200 gave 67% of ( R)- 3 in 70% e.e. and 62% of ( S)- 3 in 53% e.e., respectively.
ISSN:0957-4166
1362-511X
DOI:10.1016/S0957-4166(99)00124-X