Iep Gmbh

Cambrex Iep Gmbh

Maria Bobkova

Antje Gupta

Anke Tschentscher

Maria Dupont

In a process for the enantioselective enzymatic reduction of a hydroxy ketone of general formula I wherein R&#x2550;C-Calkyl and R&#x2550;&#x2014;Cl, &#x2014;CN, &#x2014;OH, &#x2014;H or C-Calkyl, into a chiral diol of general formula II wherein Rand Rhave the same meaning as in formula I, the hydroxy ketone is reduced with an oxidoreductase in the presence of NADH or NADPH as a cofactor, wherein

Process for the enantioselective enzymatic reduction of hydroxy keto compounds

In a process for the stereoselective, in particular enantioselective enzymatic reduction of keto compounds to the corresponding chiral hydroxy compounds, wherein the keto compounds are reduced with an enantioselective, NADH-specific oxidoreductase, a polypeptide is used for reducing the keto compounds, which polypeptide exhibits an R-ADH-signature H-[P; A]-[I; A; Q; V; L]-[G; K]-R at positions 204-208 and the following further structural features in their entirety:

Process for the stereoselective enzymatic reduction of keto compounds

The invention relates to a process for the enantioselective enzymatic reduction of a keto compound to the corresponding chiral hydroxy compound, wherein the keto compound is reduced with an oxidoreductase in the presence of a cofactor, and is characterized in that an oxidoreductase is used which has an amino acid sequence in which (a) at least 70% of the amino acids are identical to the amino acids of one of the amino acid sequences SEQ ID No 1, SEQ ID No 6 and SEQ ID No 8, or (b) at least 55% of the amino acids are identical to the amino acids of the amino acid sequence SEQ ID No 2, or (c) at least 65% of the amino acids are identical to the amino acids of the amino acid sequence SEQ ID No 3, or (d) at least 75% of the amino acids are identical to the amino acids of the amino acid sequence SEQ ID No 4, or (e) at least 65% of the amino acids are identical to the amino acids of the amino acid sequence SEQ ID No 5, or (0 at least 50% of the amino acids are identical to the amino acids of the amino acid sequence SEQ ID No 7, or (g) at least 72% of the amino acids are identical to the amino acids of the amino acid sequence SEQ ID No 129.

Oxidoreductases for the stereoselective reduction of keto compounds

In a process for the enantioselective enzymatic reduction of a hydroxy ketone of general formula I wherein R=C-Calkyl and R=&#x2014;Cl, &#x2014;CN, &#x2014;OH, &#x2014;H or C-Calkyl, into a chiral diol of general formula II wherein Rand Rhave the same meaning as in formula I, the hydroxy ketone is reduced with an oxidoreductase in the presence of NADH or NADPH as a cofactor, whereina) the hydroxy ketone is provided in the reaction at a concentration of &#x2267;50 g/l,b) the oxidized cofactor NAD or NADP having formed is regenerated continuously by oxidation of a secondary alcohol of general formula RRCHOH, wherein R, Rindependently represent hydrogen, branched or unbranched C-C-alkyl and C&#x2267;3, andc) the reduction of the hydroxy ketone and the oxidation of the secondary alcohol are catalyzed by the same oxidoreductase.

A process for the enantioselective enzymatic reduction of a keto compound of general formula I wherein R may represent any protective group for amino functions (tert. butyloxycarbonyl group (BOC), benzyloxycarbonyl group, 9-fluorenylmethoxycarbonyl group) and X&#x2550;&#x2014;Cl, &#x2014;CN, &#x2014;OH, Br, F.

Process for the enantioselective enzymatic reduction of intermediates

The invention relates to a process for the enantioselective enzymatic reduction of secodione derivatives. The secodione derivative is reduced with an oxidoreductase/dehydrogenase in the presence of NADH or NADPH as a cofactor. The secodione derivative is used in the reaction batch at a concentration of &#x2267;10 g/l and the oxidized cofactor NAD or NADP formed by the oxidoreductase/dehydrogenase is regenerated continuously.

Process for the enantioselective enzymatic reduction of secodione derivatives

A process for the enantioselective reduction of compounds having a steroid structure (ABCD) including one or several heteroatoms, one or several double bonds and/or aromatic components in the ring structure and having at least one oxo group at positions 3, 7, 11, 12 or 17 in the steroid ring system or in the a-position of any carbon moiety of the steroid structure: comprising providing the oxosteroid compound in the reaction at a concentration of &#x2267;50 g/L, a reduced cofactor NADH or NADPH, a hydroxysteroid dehydrogenase and a secondary alcohol or cycloalknaol to effect the enantioselective reduction.

Process for the enantioselective reduction and oxidation, respectively, of steroids

The present invention relates to a process for the enantioselective enzymatic reduction of keto compounds, in particular of 4-halo-3-oxobutyric acid esters, to the corresponding R-alcohols or S-4-halo-3-hydroxybutyric acid esters, respectively, using an R-specific oxidoreductase in the presence of a cofactor.

Method for the enantioselective enzymatic reduction of keto compounds using R-specific oxidoreductase

The invention relates to a NADH-dependent oxidoreductase obtained from yeasts, for example, of the genus, more particularly from. The oxidoreductace used in an enzymatic process for enantioselective reduction of organic ketocompounds to the corresponding (S)-hydroxy compounds and in an enzymnatic process for an antioselective preparation of (S)-hydroxy compounds in a two phase system using the isolated, recombinantly overexpressed oxidoreductacse from

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The invention relates to a process for the preparation of 2-butanol by enzymatic-catalyzed reduction of 2-butanone with a carbonyl reductase and a coenzyme and is characterized in that an aqueous phase, which contains the carbonyl reductase and the coenzyme, is contacted with an alcoholic phase, which is not miscible with the aqueous phase and contains 2-butanone, in order to reduce the 2-butanone, with the proviso that the alcohol present in the alcoholic phase is a secondary alcohol capable of regenerating the coenzyme and exhibiting a boiling point which lies above that of water, whereupon the 2-butanol formed is separated.

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Eltville-Hattenheim, Germany

Anke Tschentscher