Forschungszentrum Juelich Gmbh

Doerte Rother

Martina Pohl

Torsten Sehl

Robert Westphal

Lisa Marx

Alvaro Gomez Baraibar

A lyase has an amino acid sequence selected from SEQ ID NOs: 1, 2 and 3, wherein the amino acid isoleucine in position no. 468 in the protein ApPDC-E469G, which is modified with respect to the wild type from, is replaced by an amino acid which occupies less space than isoleucine.

Lyase and method for asymmetric synthesis of (S)-phenylacetylcarbinol

The invention relates to a lyase and a lyase-encoding DNA, to vectors containing the DNA and to a method for the asymmetric synthesis of (S)-phenylacetylcarbinol. According to the invention, a lyase is provided, in which tryptophan is replaced with an amino acid at position 543 in protein ApPDC-E469G, said protein being modified with respect to the wild type of, or in which it is less space-filling than tryptophan. According to the invention, deoxyribonucleic acids are furthermore provided, which encode the lyase. (S)-phenylacetylcarbinol can be produced with the lyase according to the invention from the educts benzaldehyde and pyruvate or acetaldehyde with an enantiomeric excess of at least 94%.

Lyase and lyase-encoding DNA, vectors containing the DNA, and method for the asymmetric synthesis of (S)-phenylacetylcarbinol

A method for producing cathine ((1S,2S)-norpseudoephedrine), in which, in a first reaction step, benzaldehyde is reacted with an acetyl donor according to formula (1), where R&#x2550;H or COOH, by way of an (S)-selective lease to yield an enantiomer mixture according to formulas (2) and (3) and, in a second step, the compound according to formula (3) is reacted with an amine donor by way of an (S)-selective transaminase to yield (1S,2S)-norpseudoephedrine.

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Huerth, Germany

Doerte Rother