C12P19/40

Microorganism having carbon dioxide fixation pathway introduced thereinto

An acetyl-CoA-producing microorganism, which is capable of efficiently synthesizing acetyl-CoA using carbon dioxide, and a substance production method using the same are provided. An acetyl-CoA-producing microorganism including an acetyl-CoA production cycle obtained by imparting at least one type of enzymatic activity selected from the group consisting of malate thiokinase, malyl-CoA lyase, glyoxylate carboligase, 2-hydroxy-3-oxopropionate reductase, and hydroxypyruvate reductase, to a microorganism.

S-ADENOSYLMETHIONINE (SAM) SYNTHASE VARIANTS FOR THE SYNTHESIS OF ARTIFICIAL COFACTORS

The present invention relates to isolated polypeptides that are derived from wildtype Bacillus subtilis S-Adenosylmethionine (SAM) synthase or from a biologically active fragment thereof, wherein said isolated polypeptides comprise an amino acid sequence that, in relation to the amino acid sequence of said wildtype Bacillus subtilis SAM synthase or of the biologically active fragment thereof, comprises at least one amino acid substitution, selected from the group consisting of amino acid substitutions at positions I317 and I105. The present invention further relates to respective isolated nucleic acids, vectors, host cells, uses and methods for the production of SAM derivatives.

S-ADENOSYLMETHIONINE (SAM) SYNTHASE VARIANTS FOR THE SYNTHESIS OF ARTIFICIAL COFACTORS

The present invention relates to isolated polypeptides that are derived from wildtype Bacillus subtilis S-Adenosylmethionine (SAM) synthase or from a biologically active fragment thereof, wherein said isolated polypeptides comprise an amino acid sequence that, in relation to the amino acid sequence of said wildtype Bacillus subtilis SAM synthase or of the biologically active fragment thereof, comprises at least one amino acid substitution, selected from the group consisting of amino acid substitutions at positions I317 and I105. The present invention further relates to respective isolated nucleic acids, vectors, host cells, uses and methods for the production of SAM derivatives.

ENZYMATIC SYNTHESIS OF 4'-ETHYNYL NUCLEOSIDE ANALOGS

The present invention relates to an enzymatic synthesis of 4′-ethynyl-2′-deoxy nucleosides and analogs thereof, for example EFdA, that eliminates the use of protecting groups on the intermediates, improves the stereoselectivity of glycosylation and reduces the number of process steps needed to make said compounds. It also relates to the novel intermediates employed in the process.

ENZYMATIC SYNTHESIS OF 4'-ETHYNYL NUCLEOSIDE ANALOGS

The present invention relates to an enzymatic synthesis of 4′-ethynyl-2′-deoxy nucleosides and analogs thereof, for example EFdA, that eliminates the use of protecting groups on the intermediates, improves the stereoselectivity of glycosylation and reduces the number of process steps needed to make said compounds. It also relates to the novel intermediates employed in the process.

Production of 2-Hydroxyacyl-CoAs and Derivatives Thereof
20220162661 · 2022-05-26 ·

The production of substituted 2-hydroxyacyl-CoA molecules by a novel reaction is described. The reaction involves the condensation of formyl-CoA with a carbonyl-containing molecule. Such carbonyl-containing molecules include a substituted aldehyde and a ketone. The reaction is catalyzed by enzymes using a TPP-dependent mechanism. Also described is the production of unsubstituted and substituted 2-hydroxyacyl-CoA molecules comprising the condensation of formyl-CoA with a carbonyl-containing molecule, wherein the condensation is catalyzed by a prokaryotic HACL. The 2-hydroxyacyl-CoA can be converted to chemical products having broad applications by using enzyme catalysts. The combination of enzyme catalysts comprises novel biochemical reaction pathways that can be deployed either as polypeptides in a reaction buffer or genetically encoded in recombinant microorganisms.

Production of 2-Hydroxyacyl-CoAs and Derivatives Thereof
20220162661 · 2022-05-26 ·

The production of substituted 2-hydroxyacyl-CoA molecules by a novel reaction is described. The reaction involves the condensation of formyl-CoA with a carbonyl-containing molecule. Such carbonyl-containing molecules include a substituted aldehyde and a ketone. The reaction is catalyzed by enzymes using a TPP-dependent mechanism. Also described is the production of unsubstituted and substituted 2-hydroxyacyl-CoA molecules comprising the condensation of formyl-CoA with a carbonyl-containing molecule, wherein the condensation is catalyzed by a prokaryotic HACL. The 2-hydroxyacyl-CoA can be converted to chemical products having broad applications by using enzyme catalysts. The combination of enzyme catalysts comprises novel biochemical reaction pathways that can be deployed either as polypeptides in a reaction buffer or genetically encoded in recombinant microorganisms.

Microorganism of the genus <i>Corynebacterium </i>producing 5′-xanthosine monophosphate and method for preparing 5′-xanthosine monophosphate using the same

The present disclosure relates to a microorganism of the genus Corynebacterium producing 5′-xanthosine monophosphate and a method for producing 5′-xanthosine monophosphate using the same.

Microorganism of the genus <i>Corynebacterium </i>producing 5′-xanthosine monophosphate and method for preparing 5′-xanthosine monophosphate using the same

The present disclosure relates to a microorganism of the genus Corynebacterium producing 5′-xanthosine monophosphate and a method for producing 5′-xanthosine monophosphate using the same.

Method for efficient catalytic synthesis of PAPS based on constructing ATP regeneration system
20230272444 · 2023-08-31 ·

The present disclosure discloses a method for efficient catalytic synthesis of PAPS based on constructing an ATP regeneration system, and belongs to the technical field of bioengineering. Efficient production of PAPS is realized through microbial recombination expression and artificial construction of PAPS bifunctional synthetase. On the basis, an ATP regeneration system coupling with polyphosphate kinase from Corynebacterium glutamicum and Mycobacterium tuberculosis can be used for recovering two byproducts: pyrophosphoric acid and ADP at the same time, the equivalent conversion of a substrate and a product is realized, the PAPS generated in a catalysis system has high purity, and the sulfonic acid group donation in most sulfonic acid transfer reactions can be realized.