Wacker Chemie Ag

Consortium Fur Elektrochemische Industrie Gmbh

Susanne Leonhartsberger

Christoph Winterhalter

Kerstin Pfeiffer

Brigitte Bauer

Gerhard Schmid

Anton Candussio

Guenter Wich

Renate Flinspach

Thomas Schlösser

Günter Wich

The present invention comprises a signal peptide with a cleavage site to a recombinant protein, wherein the last three amino acids before the cleavage site are alanine-phenylalanine-alanine (AFA).

Signal peptide for the production of recombinant proteins

A microorganism strain comprises a gene coding for a recombinant protein and a mutated gene coding for a host protein that is not a protease. The recombinant protein is secreted during a fermentation and the mutated gene coding for the host protein has been mutated so as to cause reduced expression of the host protein compared to the wild-type gene on which the mutated gene is based.

Microorganism strain for producing recombinant proteins

A microorganism strain secreting S-adenosylmethionine having increased activity of the cmr (mdfA) gene product is provided.

Process for the fermentative production of S-adenosylmethionine

The invention concerns a homoserine transsuccinylase having at least one mutation compared to a wild-type homoserine transsuccinylase and reduced sensitivity towards a L-methionine or SAM, compared to the wild-type enzyme. The latter comprises an amino acid sequence including a partial AspGlyXaaXaaXaaThrGlyAlaPro sequence between position 90 and position 115 and a partial TyrGlnXaaThrPro sequence between position 285 and position 310, position 1 of the amino acid sequence corresponding to the initial methionine. The invention is characterized in that the mutation is a substitution of the aspartate in the partial AspGlyXaaXaaXaaThrGlyAlaPro sequence, or a substitution of the tyrosine in the partial TyrGlnXaaThrPro sequence.

Feedback-resistant homoserine transsuccinylases

The invention relates to a homoserine transsuccinylase, which exhibits reduced sensitivity towards L-methionine or SAM in comparison with a homoserine transsuccinylase wild-type enzyme, whereby the latter comprises an amino acid sequence containing a TyrGlnXaaThrPro sub-sequence, the Thr of said sub-sequence lying between positionsandof the amino acid sequence and positionbeing filled by the starter methionine. The inventive homoserine transsuccinylase is characterized in that in comparison with the wild-type enzyme at least 2 amino acids are modified, said modification taking place in the Thr of the sub-sequence or in the C-terminal.

Growing community of inventors

Munich, Germany

Susanne Leonhartsberger