EC Number | Cloned (Comment) | Organism |
---|---|---|
2.2.1.6 | recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Azoarcus sp. |
3.7.1.11 | recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Azoarcus sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.7.1.11 | cyclohexane-1,2-dione + H2O | Azoarcus sp. | - |
6-oxohexanoate | - |
? | |
3.7.1.11 | cyclohexane-1,2-dione + H2O | Azoarcus sp. 22Lin | - |
6-oxohexanoate | - |
? | |
3.7.1.11 | additional information | Azoarcus sp. | the enzyme catalyzes C-C bond cleavage of cyclohexane-1,2-dione to produce 6-oxohexanoic acid as the primary product, presumably followed by oxidation of the latter to adipic acid | ? | - |
? | |
3.7.1.11 | additional information | Azoarcus sp. 22Lin | the enzyme catalyzes C-C bond cleavage of cyclohexane-1,2-dione to produce 6-oxohexanoic acid as the primary product, presumably followed by oxidation of the latter to adipic acid | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.2.1.6 | Azoarcus sp. | - |
- |
- |
2.2.1.6 | Azoarcus sp. 22Lin | - |
- |
- |
3.7.1.11 | Azoarcus sp. | P0CH62 | - |
- |
3.7.1.11 | Azoarcus sp. 22Lin | P0CH62 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.2.1.6 | recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Azoarcus sp. |
3.7.1.11 | recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Azoarcus sp. |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.7.1.11 | culture condition:cyclohexane-1,2-diol-grown cell | cyclohexane-1,2-diol as the sole carbon source and electron donor, and nitrate as electron acceptor | Azoarcus sp. | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.2.1.6 | 1-naphthaldehyde + pyruvate | - |
Azoarcus sp. | (1R)-1-hydroxy-1-(naphthalen-1-yl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 1-naphthaldehyde + pyruvate | - |
Azoarcus sp. 22Lin | (1R)-1-hydroxy-1-(naphthalen-1-yl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 2-bromobenzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(2-bromophenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 2-bromobenzaldehyde + pyruvate | - |
Azoarcus sp. 22Lin | (R)-1-hydroxy-1-(2-bromophenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 2-chlorobenzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(2-chlorophenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 2-chlorobenzaldehyde + pyruvate | - |
Azoarcus sp. 22Lin | (R)-1-hydroxy-1-(2-chlorophenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 2-fluorobenzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(2-fluorophenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 2-hydroxybenzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(2-hydroxyphenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 2-iodobenzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(2-iodophenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 2-methoxybenzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(2-methoxyphenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 2-methylbenzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(2-methylphenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 2-naphthaldehyde + pyruvate | - |
Azoarcus sp. | (1R)-1-hydroxy-1-(naphthalen-2-yl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 2-nitrobenzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(2-nitrophenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 4-(tert-butyl)benzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(4-(tert-butyl)phenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 4-ethoxybenzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(4-ethoxyphenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 4-ethylbenzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(4-ethylphenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 4-isopropylbenzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(4-isopropylphenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | 4-phenylbenzaldehyde + pyruvate | - |
Azoarcus sp. | (R)-1-hydroxy-1-(4-ethylphenyl)propan-2-one + CO2 | - |
? | |
2.2.1.6 | additional information | in addition to its physiological C-C bond-cleavage activity, CDH catalyzes the asymmetric cross-benzoin reaction of a broad variety of aromatic aldehydes and pyruvate. In the case of the sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde, the respective 2-hydroxyketone products are obtained in high yield. The recombinant CDH shows the same C-C bond-cleavage and C-C bond-formation activity as the enzyme purified from its native source, Azoarcus sp. strain 22Lin. Enzyme CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92-99% ee). The enzyme accepts also hydroxybenzaldehydes and nitrobenzaldehydes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde are transformed into the corresponding 2-hydroxy ketone products in high yields, enzyme substrate specificity and enantioselectivity, overview | Azoarcus sp. | ? | - |
? | |
2.2.1.6 | additional information | in addition to its physiological C-C bond-cleavage activity, CDH catalyzes the asymmetric cross-benzoin reaction of a broad variety of aromatic aldehydes and pyruvate. In the case of the sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde, the respective 2-hydroxyketone products are obtained in high yield. The recombinant CDH shows the same C-C bond-cleavage and C-C bond-formation activity as the enzyme purified from its native source, Azoarcus sp. strain 22Lin. Enzyme CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92-99% ee). The enzyme accepts also hydroxybenzaldehydes and nitrobenzaldehydes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde are transformed into the corresponding 2-hydroxy ketone products in high yields, enzyme substrate specificity and enantioselectivity, overview | Azoarcus sp. 22Lin | ? | - |
? | |
2.2.1.6 | pyruvate + benzaldehyde | The enzyme is able to catalyze nonphysiological asymmetric C-C bond formation, the cross-benzoin reaction of benzaldehyde and pyruvate (after decarboxylation) to result in the R-configured 1-hydroxy-1-phenylpropan-2-one (98% ee) | Azoarcus sp. | (R)-phenylacetylcarbinol + CO2 | i.e. (R)-1-hydroxy-1-phenylpropan-2-one | ? | |
2.2.1.6 | pyruvate + benzaldehyde | The enzyme is able to catalyze nonphysiological asymmetric C-C bond formation, the cross-benzoin reaction of benzaldehyde and pyruvate (after decarboxylation) to result in the R-configured 1-hydroxy-1-phenylpropan-2-one (98% ee) | Azoarcus sp. 22Lin | (R)-phenylacetylcarbinol + CO2 | i.e. (R)-1-hydroxy-1-phenylpropan-2-one | ? | |
3.7.1.11 | cyclohexane-1,2-dione + H2O | - |
Azoarcus sp. | 6-oxohexanoate | - |
? | |
3.7.1.11 | cyclohexane-1,2-dione + H2O | - |
Azoarcus sp. 22Lin | 6-oxohexanoate | - |
? | |
3.7.1.11 | additional information | the enzyme catalyzes C-C bond cleavage of cyclohexane-1,2-dione to produce 6-oxohexanoic acid as the primary product, presumably followed by oxidation of the latter to adipic acid | Azoarcus sp. | ? | - |
? | |
3.7.1.11 | additional information | determination of the catalytic activity of recombinant enzyme CDH, both cleavage of cyclohexane-1,2-dione and the cross-benzoin reaction of benzaldehyde and pyruvate. The enzyme is able to catalyze nonphysiological asymmetric C-C bond formation, the cross-benzoin reaction of benzaldehyde and pyruvate (after decarboxylation) to result in the R-configured 1-hydroxy-1-phenylpropan-2-one (98% ee) is performed on an analytical scale. The recombinant CDH shows the same C-C bond-cleavage and C-C bond-formation activity as the enzyme purified from its native source, Azoarcus sp. strain 22Lin. Enzyme CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92-99% ee). The enzyme accepts also hydroxybenzaldehydes and nitrobenzaldehydes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde are transformed into the corresponding 2-hydroxy ketone products in high yields | Azoarcus sp. | ? | - |
? | |
3.7.1.11 | additional information | the enzyme catalyzes C-C bond cleavage of cyclohexane-1,2-dione to produce 6-oxohexanoic acid as the primary product, presumably followed by oxidation of the latter to adipic acid | Azoarcus sp. 22Lin | ? | - |
? | |
3.7.1.11 | additional information | determination of the catalytic activity of recombinant enzyme CDH, both cleavage of cyclohexane-1,2-dione and the cross-benzoin reaction of benzaldehyde and pyruvate. The enzyme is able to catalyze nonphysiological asymmetric C-C bond formation, the cross-benzoin reaction of benzaldehyde and pyruvate (after decarboxylation) to result in the R-configured 1-hydroxy-1-phenylpropan-2-one (98% ee) is performed on an analytical scale. The recombinant CDH shows the same C-C bond-cleavage and C-C bond-formation activity as the enzyme purified from its native source, Azoarcus sp. strain 22Lin. Enzyme CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92-99% ee). The enzyme accepts also hydroxybenzaldehydes and nitrobenzaldehydes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde are transformed into the corresponding 2-hydroxy ketone products in high yields | Azoarcus sp. 22Lin | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.2.1.6 | homodimer | the enzyme is a homodimer in solution, the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer | Azoarcus sp. |
2.2.1.6 | homotetramer | in the crystallized form | Azoarcus sp. |
3.7.1.11 | homodimer | the enzyme is a homodimer in solution, the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer | Azoarcus sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.7.1.11 | Cdh | - |
Azoarcus sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.2.1.6 | 30 | - |
assay at | Azoarcus sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.2.1.6 | 6.5 | - |
assay at | Azoarcus sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.2.1.6 | FAD | noncovalently bound, one FAD per monomer | Azoarcus sp. | |
2.2.1.6 | additional information | the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer | Azoarcus sp. | |
2.2.1.6 | thiamine diphosphate | dependent on, one thiamine diphosphate per monomer | Azoarcus sp. | |
3.7.1.11 | FAD | noncovalently bound, one FAD per monomer | Azoarcus sp. | |
3.7.1.11 | additional information | the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer | Azoarcus sp. | |
3.7.1.11 | thiamine diphosphate | dependent on, one thiamine diphosphate per monomer | Azoarcus sp. |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.7.1.11 | physiological function | thiamine diphosphate-dependent cyclohexane-1,2-dione hydrolase is the key enzyme of an anaerobic degradation pathway of alicyclic alcohols | Azoarcus sp. |