Forschungszentrum Juelich Gmbh

Forschungszentrum Julich Gmbh

Degussa Aktiengesellschaft

Evoxx Technologies Gmbh

Martina Pohl

Torsten Sehl

Doerte Rother

Maria-Regina Kula

Lisa Marx

Robert Westphal

Michael Müller

Heike Slusarczyk

Martin Diener

Alvaro Gomez Baraibar

Ayhan Demir

Karin Mesch

Karl-Erich Jaeger

Ulrich Krauss

Heike Bruhn

ÁLvaro Gómez Baraibar

Dörte Rother

Disclosed are catalytically active water-insoluble protein aggregates comprising fusion proteins which comprise a coiled-coil domain and a catalytic domain, methods of manufacturing such protein aggregates, and their use.

Catalytically active protein aggregates and methods for producing the same

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.

Method for producing cathine

The present invention relates to a nucleotide sequence which encodes a benzaldehyde lyase and to its use in a process for stereoselectively preparing 2-hydroxyketone group-containing compounds.

Nucleotide sequence encoding a benzaldehyde lyase, and process for stereoselectively synthesizing 2-hydroxyketones

Mutants of formate dehydrogenase from Candida boidinii, new gene sequences encoding these and use of the new formate dehydrogenases

A process for obtaining a pyruvate decarboxylase by isolation from a producer organism. The pyruvate decarboxylase is capable of forming (R)-(-)-phenylacetylcarbinole (I) in .gtoreq.95% enantiomer unit with a product ratio of (I) to 2-hydoxypropiophenone of .gtoreq.95%. In addition, the pyruvate decarboxylase has a specific activity with regard to phenylacetylcarbinole formation of &gt;1U/mg. It is the aim of the invention to obtain a pyruvate decarboxylase with improved synthesis capacity concerning the formation of (R)-(-)-phenylacetylcarbinole. The process of the invention developed for this purpose is characterized in that use is made of a producing organism with a gene coding for pyruvate decarboxylase from Zymomonas mobilis, in the DNA sequence of which the tryptophane radical coding codon TGG is replaced at position 1174-1176 by a codon which codes for an amino acid radical with a reduced volume ratio.

Process for obtaining acyloins, pyruvate decarboxylases suitable

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Aachen, Germany

Martina Pohl