Abstract: The present invention relates to an alcohol dehydrogenase from Rhodococcus erythropolis. By means of such cofactor-dependent ADHs, chiral alcohols, which can be of use for use in organic syntheses, can advantageously be obtained with a cofactor-regenerating enzyme in a coupled enzymatic system. A nucleotide sequence, vehicles containing this, a polypeptide sequence and processes for mutation and use of the sequences are claimed.

Abstract: The invention relates to recombinant microorganisms which, in comparison to the starting organism, have a higher concentration or activity of a D-amino acid oxidase, of an L-amino acid dehydrogenase, of an NADH cosubstrate regenerating enzyme and, if necessary, of a catalase. The invention also includes methods for preparing L-amino acids from D-amino acids using of these microorganisms.

Abstract: The present invention is directed to a nucleotide sequence encoding D-amino oxidase (D-AAO, EC 1.4.3.3) from Arthrobacter protophormiae. This may be inserted into an expression and used to transform a microbial host. The transformed microbial hosts ecomically produce D-AAO which may be used to oxidize D-amino acids.

Abstract: The present invention relates to an alcohol dehydrogenase from Rhodococcus erythropolis. By means of such cofactor-dependent ADHs, chiral alcohols which can be of use for use in organic syntheses can advantageously be obtained with a cofactor-regenerating enzyme in a coupled enzymatic system. A nucleotide sequence, vehicles containing this, a polypeptide sequence and processes for mutation and use of the sequences are claimed.

Abstract: The present application relates to a reaction system in which chemically valuable compounds can be obtained in high enantiomer concentrations with the aid of a coupled enzymatically operating transformation process. The coupled enzymatic reaction system comprises a cofactor-dependent enzymatic transformation of an organic compound and an enzymatic regeneration of the cofactor, wherein the reaction system operates in aqueous solution with an amount of substrate above the solubility limit thereof. In the preferred embodiments, an alcohol dehydrogenase is the cofactor-dependent enzyme, and the regeneration of the cofactor (e.g. NADH or NADPH) is acheved by means of formate dehydrogenase.

Abstract: The present application relates to a reaction system in which chemically valuable compounds can be obtained in high enantiomer purities with the aid of a coupled enzymatically operating transformation process. The coupled enzymatically operating reaction system in this context comprises an enzymatic transformation reaction which proceeds with the consumption of a cofactor, and recycling of the cofactor consumed, which proceeds enzymatically, wherein the procedure is carried out in a homogeneous aqueous solvent system comprising an organic hydrocarbon having at least two hydroxyl or ether groups.

Abstract: The present process relates to a coupled enzymatic reaction system which is implemented in a two-phase system consisting of organic phase and aqueous phase. The system operates with cofactor-dependent enzymes, the cofactor being continually regenerated enzymatically by an FDH derived from C. boidinii.

Abstract: The invention relates to recombinant microorganisms which, in comparison to the starting organism, have a higher concentration or activity of a D-amino acid oxidase, of an L-amino acid dehydrogenase, of an NADH cosubstrate regenerating enzyme and, if necessary, of a catalase. The invention also includes methods for preparing L-amino acids from D-amino acids using of these microorganisms.

Abstract: The present invention is directed to a new NADH oxidase from Lactobacillus, nucleic acids encoding the NADH oxidase, methods of producing the NADH oxidase, as well as there use in producing improved NADH oxidase enzymes and for producing chrial enantiomer-enriched organic compounds, such as alcohols and/or amino acids.

Abstract: The present invention is directed to a new NADH oxidase from Lactobacillus, nucleic acids encoding the NADH oxidase, methods of producing the NADH oxidase, as well as there use in producing improved NADH oxidase enzymes and for producing chrial enantiomer-enriched organic compounds, such as alcohols and/or amino acids.

Abstract: In a method of reducing diketocarboxylic acids or hydroxyketocarboxylic acids or their esters, at least one keto group is converted to a hydroxyl group in the presence of lactobacillus species.

Abstract: The present invention is directed to a nucleotide sequence encoding D-amino oxidase (D-AAO, EC 1.4.3.3) from Arthrobacter protophormiae. This may be inserted into an expression and used to transform a microbial host. The transformed microbial hosts ecomically produce D-AAO which may be used to oxidize D-amino acids.

Abstract: The present invention is directed to a new NADH oxidase from Lactobacillus, nucleic acids encoding the NADH oxidase, methods of producing the NADH oxidase, as well as there use in producing improved NADH oxidase enzymes and for producing chrial enantiomer-enriched organic compounds, such as alcohols and/or amino acids.

Abstract: The present invention relates to recombinantly modified enzymes, which exhibit increased NAD(H) affinity compared to a unmodified or wildtype enzyme, gene sequences or polynucleotides that code for the recombinantly modified enzymes, plasmids and microorganisms that contain these gene sequences; as well as, methods of making and methods of using the enzymes of the present invention.

Abstract: L-amino acid oxidases (L-AAO) from Rhodococcus species and nucleic acids, vectors and microorganisms expressing such L-AAOs. L-AAOs may be used to selectively transform the L-portion of a racemic mixture of an amino acid into keto acid, and thus purify the corresponding D-amino acid.

Abstract: L-amino acid oxidases (L-AAO) from Rhodococcus species and nucleic acids, vectors and microorganisms expressing such L-AAOs. L-AAOs may be used to selectively transform the L-portion of a racemic mixture of an amino acid into keto acid, and thus purify the corresponding D-amino acid.

Abstract: In a method of reducing diketocarboxylic acids or hydroxyketocarboxylic acids or their esters, at least one keto group is converted to a hydroxyl group in the presence of lactobacillus species.

Abstract: In a method for improving the NADH specificity of preferred NADPH-dependent dehydrogenases, the alkalinity of the enzyme is reduced in the coenzyme docking area by an appropriate change of the amino acid sequence achieved by genetic engineering means. The inventive process is especially used for obtaining short-chain dehydrogenases with coenzyme binding areas on the N-terminus from Lactobacillus brevis and Lactobacillus kefir.

Abstract: The invention relates to a method for the enantioselective reduction of 3,5-dioxocarboxylic acid derivatives and their syntheses. According to the invention, compounds of formula (4) are reacted with an alcohol dehydrogenase which preferably stems from Lactobacillus brevis and which is recombinantly over-expressed in Escherichia coli, in the presence of NADPH. The keto group in position 5 is enantioselectively reduced during this reaction. The keto group in position 3 can also be specifically syn- or anti-reduced in a further step by means of chemical or enzymatic reactions.

Abstract: Stable microbial enzyme with alcohol dehydrogenase activity having an activity maximum at ca. 50° C., process for its isolation and its use for the enantioselective reduction/oxidation of organic keto compounds/hydroxy compounds wherein, depending on the type of the starting compounds R- or S-hydroxy compounds are obtained. In particular an alcohol dehydrogenase obtainable from Lactobacillus brevis has proven to be suitable.