Abstract: The present invention relates to a cellular transport system for bringing a sulfonic acid construct which carries a cargo into a cell and releasing the cargo in the cell's cytoplasm, the cellular transport system comprising: (i) a sulfonate transporter located in the cytoplasm membrane of the cell wherein said sulfonate transporter is capable of transporting said sulfonic acid construct across the cytoplasm membrane into the cytoplasm; (ii) a ?-glutamyl transferase (GGT; EC 2.3.2.2) which is modified to be located in the cytoplasm of the cell, wherein said ?-glutamyl transferase is capable of hydrolyzing said sulfonic acid construct so as to release the cargo. Moreover, the present invention relates to the use of a cellular transport system for bringing a sulfonic acid construct which contains a cargo into a cell and releasing the cargo in the cell's cytoplasm. Further, the present invention relates to a ?-glutamyl transferase for hydrolyzing a sulfonic acid construct which contains a cargo.

Abstract: Described are mevalonate diphosphate decarboxylase variants having improved activity in converting 3-phosphonoxyisovalerate into isobutene. Such variants can be employed in processes for biologically producing isobutene from 3-hydroxyisovalerate or from 3-hydroxy-3-methylbutyrate into isobutene, for biologically producing isoprenol from mevalonate or from mevalonate-3-phosphate or for biologically producing 1,3-butadiene from 3-hydroxypent-4-enoate or from 3-phosphonoxypent-4-enoate. Also described is an enzyme which is characterized in that it is capable of converting 3-phosphonoxyisovalerate into isobutene with a kcat of more than 0.1 s?1.

Abstract: Described are methods for the production of isobutene comprising the enzymatic conversion of 3-methylcrotonic acid into isobutene wherein said 3-methylcrotonic acid is obtained by the enzymatic conversion of 3-methylcrotonyl-CoA into 3-methylcrotonic acid or wherein said 3-methylcrotonic acid is obtained by the enzymatic conversion of 3-hydroxyisovalerate (HIV) into 3-methylcrotonic acid. It is described that the enzymatic conversion of 3-methylcrotonic acid into isobutene can, e.g., be achieved by making use of a 3-methylcrotonic acid decarboxylase, preferably an FMN-dependent decarboxylase associated with an FMN prenyl transferase, an aconitate decarboxylase (EC 4.1.1.6), a methylcrotonyl-CoA carboxylase (EC 6.4.1.4), or a geranoyl-CoA carboxylase (EC 6.4.1.5).

Abstract: Described is a method for the enzymatic production of an acyl phosphate from a 2-hydroxyaldehyde using a phosphoketolase or a sulfoacetaldehyde acetyltransferase.

Abstract: Described are recombinant microorganisms characterized by having phosphoketolase activity, having a diminished or inactivated Embden-Meyerhof-Parnas pathway (EMPP) by inactivation of the gene(s) encoding phosphofructokinase or by reducing phosphofructokinase activity as compared to a non-modified microorganism and having a diminished or inactivated oxidative branch of the pentose phosphate pathway (PPP) by inactivation of the gene(s) encoding glucose-6-phosphate dehydrogenase or by reducing glucose-6-phosphate dehydrogenase activity as compared to a non-modified microorganism. These microorganisms can be used for the production of useful metabolites such as acetone, isobutene or propene.

Abstract: Described is a method for the enzymatic production of acetyl phosphate from formaldehyde using a phosphoketolase or a sulfoacetaldehyde acetyltransferase.

Abstract: Described is a method for the enzymatic production of an acyl phosphate from a 2-hydroxyaldehyde using a phosphoketolase or a sulfoacetaldehyde acetyltransferase.

Abstract: Described is a method for the production of D-erythrose and acetyl phosphate comprising the enzymatic conversion of D-fructose into D-erythrose and acetyl phosphate by making use of a phosphoketolase. The produced D-erythrose can further be converted into glycolaldehyde by a method for the production of glycolaldehyde comprising the enzymatic conversion of D-erythrose into glycolaldehyde by making use of an aldolase, wherein aldolase is a 2-deoxyribose-5-phosphate aldolase (EC 4.1.2.4) or a fructose-bisphosphate aldolase (EC 4.1.2.13). The produced glycolaldehyde can finally be converted into acetyl phosphate by the enzymatic conversion of the thus produced glycolaldehyde into acetyl phosphate by making use of a phosphoketolase or a sulfoacetaldehyde acetyltransferase.

Abstract: Described are HIV kinase variants showing an improved activity in converting 3-hydroxyisovalerate (HIV) into 3-phosphonoxyisovalerate (PIV), methods for the production of PIV using such enzyme variants as well as methods for the production isobutene in a subsequent reaction.

Abstract: Described are 3-hydroxyisovalerate (HIV) synthase variants having improved activity in converting acetone and a compound which provides an activated acetyl group into 3-hydroxyisovalerate (HIV). Moreover, described are in particular methods for the production of 3-hydroxyisovalerate and methods for the production of isobutene from acetone utilizing the HIV synthase variants of the present invention.

Abstract: Described are recombinant microorganisms characterized by having phosphoketolase activity, having a diminished or inactivated Embden-Meyerhof-Parnas pathway (EMPP) by inactivation of the gene(s) encoding phosphofructokinase or by reducing phosphofructokinase activity as compared to a non-modified microorganism and having a diminished or inactivated oxidative branch of the pentose phosphate pathway (PPP) by inactivation of the gene(s) encoding glucose-6-phosphate dehydrogenase or by reducing glucose-6-phosphate dehydrogenase activity as compared to a non-modified microorganism. These microorganisms can be used for the production of useful metabolites such as acetone, isobutene or propene.

Abstract: Described is a method for the production of isobutene from 3-methylcrotonyl-CoA comprising the steps of: (a) enzymatically converting 3-methylcrotonyl-CoA into 3-methylbutyric acid; and (b) further enzymatically converting the thus produced 3-methylbutyric acid into isobutene. The conversion of 3-methylcrotonyl-CoA into 3-methylbutyric acid can be achieved by first enzymatically converting 3-methylcrotonyl-CoA into 3-methyl butyryl-CoA and further enzymatically converting the thus produced 3-methylbutyryl-CoA into 3-methylbutyric acid. Alternatively, the conversion of 3-methylcrotonyl-CoA into 3-methylbutyric acid can be achieved by first enzymatically converting 3-methylcrotonyl-CoA into 3-methylcrotonic acid and then further enzymatically converting the thus produced 3-methylcrotonic acid into 3-methylbutyric acid.

Abstract: Described are recombinant microorganisms characterized by having phosphoketolase activity, having a diminished or inactivated Embden-Meyerhof-Parnas pathway (EMPP) by inactivation of the gene(s) encoding phosphofructokinase or by reducing phosphofructokinase activity as compared to a non-modified microorganism and having a diminished or inactivated oxidative branch of the pentose phosphate pathway (PPP) by inactivation of the gene(s) encoding glucose-6-phosphate dehydrogenase or by reducing glucose-6-phosphate dehydrogenase activity as compared to a non-modified microorganism. These microorganisms can be used for the production of useful metabolites such as acetone, isobutene or propene.

Abstract: Described are methods for the production of isobutene comprising the enzymatic conversion of 3-methylcrotonic acid into isobutene wherein said 3-methylcrotonic acid is obtained by the enzymatic conversion of 3-methylcrotonyl-CoA into 3-methylcrotonic acid or wherein said 3-methylcrotonic acid is obtained by the enzymatic conversion of 3-hydroxyisovalerate (HIV) into 3-methylcrotonic acid. It is described that the enzymatic conversion of 3-methylcrotonic acid into isobutene can, e.g., be achieved by making use of a 3-methylcrotonic acid decarboxylase, preferably an FMN-dependent decarboxylase associated with an FMN prenyl transferase, an aconitate decarboxylase (EC 4.1.1.6), a methylcrotonyl-CoA carboxylase (EC 6.4.1.4), or a geranoyl-CoA carboxylase (EC 6.4.1.5).

Abstract: Described are alkenol dehydratase variants having improved activity in catalyzing the conversion of prenol into isoprene, methods for the production of isoprene using such enzyme variants and their uses in the production of isoprene from prenol.

Abstract: Described are HIV kinase variants showing an improved activity in converting 3-hydroxyisovalerate (HIV) into 3-phosphonoxyisovalerate (PIV), methods for the production of PIV using such enzyme variants as well as methods for the production isobutene in a subsequent reaction.

Abstract: Described are alkenol dehydratase variants having improved activity in catalyzing the conversion of a compound corresponding to the general formula CnH2nO into CnH2n-2 +H2O with 3<n<7. In particular, described are alkenol dehydratase variants having, e.g., an improved activity in converting but-2-en-1-ol (crotyl alcohol) into 1,3 butadiene and/or an improved activity in converting but-3-en-2-ol into 1,3 butadiene and/or an improved activity in converting 3-methylbut-2-en-1-ol (prenol) or 3-methylbut-3-en-2-ol (isoprenol) into isoprene and/or an improved activity in converting 2,3-dimethyl-but-2-en-1-ol into dimethyl-butadiene.

Abstract: The application describes a method for producing alkenes (for example propylene, ethylene, 1-butylene, isobutylene, isoamylene, butadiene or isoprene) from 3-hydroxycarboxylic acids via 3-hydroxycarboxyl-nucleotidylic acids.

Abstract: The present invention relates to a method for generating alkenes biologically. It relates more particularly to a method for producing terminal alkenes by enzymatic decarboxylation of 3-hydroxyalkanoate molecules. The invention also relates to the enzymatic systems and the microbial strains used, and also to the products obtained.

Abstract: Described is a method for generating isoprenol through a biological process. More specifically, described is a method for producing isoprenol from mevalonate.